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Collagen is a group of fibrous proteins found in all multicellular animals that impart tensile strength to connective tissues. There are 28 different types of collagen in our body. The main types of collagen are type I, type II and type III. Type I collagen is found in skin, nails, hair, muscles, tendons and bones. In bones, collagen is reinforced with calcium ions to support the body's weight. Type 2 collagen is found in joint cartilage. Animal gelatin is also produced from collagen by partial hydrolysis.


Collagen is obtained from the connective tissues of animals mainly cattle and pigs and from fish. Collagen taken internally is in the form of hydrolyzed collagen. Hydrolyzed collagen is collagen protein that has been processed by hydrolysis (breaking down the collagen molecule by heating in water). The product obtained is parts of the collagen protein chain.

Pharmacological Properties

Collagen has been used in skin creams for decades, usually making them more expensive. However, to reduce rather than just cover wrinkles, new collagen must become a part of the skin's inner layer, the dermis. Unfortunately, collagen molecules are too large to penetrate into the dermis when applied to the surface of the skin. Thus, when simply applied in a cream, collagen remains locked outside without affecting the skin structure, at best just temporarily covering wrinkles and helping moisturize the skin.

As was mentioned, aging of the skin shifts the balance between collagen production and breakdown leading to wrinkles, facial sag and rough skin texture. Stimulating skin cells to produce collagen can partly reverse this process. Stimulating collagen synthesis in aged skin was shown to reduce wrinkles and improve skin texture. The benefit of stimulating your own collagen production is that collagen is deposited in an orderly, structured manner and that there is no risk of allergy, immune reaction or injection-induced infection. Furthermore, many ingredients useful in stimulating collagen synthesis are relatively inexpensive and safe.

Stimulation of collagen synthesis in aging skin is realistic and can substantially improve the appearance of fine lines and even deeper wrinkles when done correctly. However, it often requires a comprehensive approach and specific stimulants. Among those the most effective are key amino acids. Like any other protein, collagen consists of amino acids, the building blocks of proteins. Altogether there are 20 different kinds of amino acids in human cells. However, collagen is unusually rich in a few particular amino acids (glycine and proline). Supplying these key amino acids in abundance helps stimulate collagen synthesis. The best mixture of amino acids in order to stimulate and facilitate the production of collagen within our body is hydrolyzed collagen derived from animals. The collagen fragments contain identical amino acids with our body’s collagen and therefore the new collagen synthesis becomes easy. 



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Curcumin, the main ingredient of turmeric, increases fatty acid oxidation, lipase levels, and kinase activity. The oxidation of fatty acids and the action of the enzymes lipase and kinase result in the dissolution of the fat already present in the body, preventing the production of new fat and increasing the metabolism.


Turmeric (scientific name: Curcuma longa - Long turmeric) or yellow root, is a rhizomatous, herbaceous, perennial plant of the Zingiberaceae family.

Botanical Description

Turmeric is a perennial herbaceous plant that reaches up to 1m in height. Multi-branched, yellow, orange, cylindrical, aromatic rhizomes are found. The leaves are alternately arranged in two rows. They are divided into leaf sheath, petiole (stem) and leaf blade. The stem is 50 to 115 cm long. Simple leaf blades are usually 76 to 115 cm long and rarely up to 230 cm. They are 38 to 45 cm wide and are elongated to elliptical, tapering towards the tip.

It is native to southern Asia, where it requires temperatures between 20 and 30 °C and a significant amount of annual rainfall to grow. The plants are harvested each year for their rhizomes and propagated in the following season from some of these rhizomes.

When not used fresh, the rhizomes are boiled for about 30-45 minutes, then dried in hot ovens and then ground into a bright orange-yellow powder.


Turmeric has been used in Asia for thousands of years and is an important part of Siddha medicine. Initially, it was used as a pigment and then later for its healing properties. The name comes from the Spanish "cúrcuma".

Pharmacological Properties

Curcumin, the main ingredient of turmeric helps to reduce weight in three ways: (a) by stimulating the production of new mitochondria which in turn increase the rate of oxidation of fatty acids, (b) by increasing the production of the enzyme lipase which is responsible for breaking down fats, and (c) by increasing the activity of the enzyme kinase which increases the "metabolic homeostasis" which is usually out of balance in overweight and obese individuals.

Curcumin also has a significant anti-inflammatory effect which is responsible for the elimination of bloating.



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Ginkgo Biloba is an ancient deciduous tree that has experienced very little change over millions of years. Ginkgo biloba leaf extract consists of groups of active plant compounds, the most important of which are flavonoid glycosides and terpenoids. Their properties are the increasing of blood circulation and the increased oxygenation of the blood vessels. Ginkgo biloba is widely known to increase cerebral blood flow and support the brain function.

Name - Species

It is the only surviving species of the Gingoid family in the Gingid order. It holds a special place in the evolutionary tree as it is the only living link between ferns and conifers. Its name comes from the Chinese word Ginkyo which means silver apricot.

Botanical Description

Although a gymnosperm, it is a particularly impressive, beautiful, deciduous tree. In autumn, its leaves change color from green to gold. It reaches a height of 50 meters and its trunk is cylindrical, having a diameter of up to 3 meters. Its bark is gray in color with deep furrows. Its leaves are large, broad, fan-shaped with a length of 9 cm and a width of up to 15 cm. They are divided into two characteristic lobes that have a central section in the middle. The fruits of the tree are silver in color and surrounded by a fleshy casing with a strong unpleasant smell like rancid butter due to the presence of butyric acid. The growth pattern is generally narrow in young trees and only really widens when they reach about 100 years of age. Unlike other gymnosperms it has separate sexes. This means that the female tree needs the presence of a male in order to be fertilized. Occasionally both sexes are found on the same tree.

The tree is considered a "living fossil", a term used to describe organisms that have experienced very little change over millions of years. In the case of the Ginkgo biloba species, there are 270,000,000 year old Paleolithic specimens from the Permian period.

According to a study by Chinese scientists, the genome of the Gigko tree is huge and includes about 10.6 billion "letters" of DNA. The human genome, by comparison, contains just three billion "letters" of DNA.


The first ginkgos appeared 270 million years ago, in the Permian period. During the middle Jurassic period there was a huge increase in species with peak biodiversity in the Cretaceous period (144 million years ago) in areas known today as Asia, Europe and North America. Due to cataclysmic disasters and gradual climate change, the ginkgo disappeared from North America 7 million years ago and from Europe 2.5 million years ago. Today it grows naturally mainly in areas of southwestern and eastern China, but it is also found in temples in Korea and Japan because of its symbolic importance in Confucianism.

Pharmacological Properties

Ginkgo biloba has multiple beneficial effects on the brain and its function:

(a) The active components of Ginkgo biloba are flavonoids and terpenoids. Diflavones, dilobalide, catechins, flavones, flavonols, glycosides, gigolites, ketones and steroids. Flavonoids and terpenoids improve blood circulation to the brain, resulting in more oxygen being supplied to the brain, which enhances mental function such as problem solving, cognitive function and good memory. In senile dementia, Ginkgo biloba is particularly useful when administered in the early stages of this disorder. According to many studies it can also be beneficial in the early stages of the Alzheimer's disease.

(b) Ginkgo biloba can stimulate brain-derived neurotrophic factor (BDNF), a protein in the brain and peripheral nervous system, essential for the regulation, growth and survival of brain cells, which is very important for the long-term memory. Its ability to increase BDNF means it can improve brain and cognitive function.

(c) Ginkgo biloba enhances neural stem cell differentiation and performance in the brain. Specifically, it positively modifies neural stem cells, a subset of cells in the brain that can give rise to the many different types of cells that make up the brain.



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Industrial cannabis, the cultivation of which is legal, contains the compound cannabidiol (CBD) known since ancient times for its relaxing and calming effect without other side effects. Medicinal cannabis, the free cultivation of which is illegal, contains the psychoactive substance Δ9-tetrahydrocannabinol, known as THC.

Name - Species

Cannabis is a plant genus in which three distinct plant species are usually classified: Cannabis sativa, Indian cannabis (Cannabis indica) and Cannabis ruderalis.

Botanical Description

In Greece it exists as a native and cultivated plant and has been known since ancient times. It is considered a fiber plant since from it, especially Sativa, fibers are obtained that are used for weaving and making ropes, canvas and other materials. Hemp is a tall plant, dioecious (ie male and female flowers on separate plants) and pollinated by the wind. In its fibrous varieties, the male plants have a higher fiber content and are of better quality. In recent years, of course, some self-cultivated varieties of uniform seed ripening have been selected which are considered more suitable for fiber production. It is found as a crop in the EU on a large scale in France followed by the Netherlands as well as Italy, the Czech Republic, Poland, Germany, Spain, etc.


Man's relationship with Cannabis is lost in the depths of millennia. From its original area, which was probably in Central Asia and northern India, cannabis spread over the centuries throughout the Eurasian space, almost in every inhabited place. The 18th century Swedish botanist Linnaeus believed that hemp was a type of plant that originally flourished in northern India. In the 1930s, however, the Russian botanist Nicolai Vavilov demonstrated in his studies that this plant came from the region of Samarkand, north of Afghanistan and the Indian Caucasus.

Traces of hemp in the form of clothing, resin and seeds have been discovered in many archaeological sites in Central Asia and northern India, thus indicating that its use, in one form or another, was endemic to these regions since ancient times. Despite all this, the oldest archaeological finds with hemp come from regions of China and date several thousand years before Christ.

Traces of rope made from cannabis plants have been found in fragments of pottery, while pieces of clothing and paper made from cannabis have also seen the light in archaeological excavations. Herodotus, in 450 BC, compared clothes made of cannabis with those of linen, remarking that only an expert could decide whether they were made of cannabis or linen.

The Greek name Cannabis, by which this plant is now known throughout the world, probably comes from the Assyrian words "Qunuby" and "Qunabu", which mean a kind of intoxicating smoke, as the psychotropic and euphoric properties of cannabis were known since ancient times.

Pharmacological Properties

CBD achieves relaxation and anxiety reduction in two ways: (a) by increasing anandamine levels and (b) by activating serotonin receptors.

Anandamine is a neurotransmitter that contributes to many processes such as mood, sleep and appetite. Research shows that low levels of anandamine lead to mood disorders and anxiety. High levels offer better mood and reduced stress. CBD increases anandamine levels by blocking the enzymes that break it down.

CBD binds to serotonin receptors which are activated and affect the body's response to stress, creating greater mental balance and calmness.

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Collagen Bibliography

1. Anesey, J., Scott, P., Veis, A. and Chyatte, D. The Isolation of a Soluble Type III Collagen Precursor from Rat Skin, Biochem Biophys Res Commun, 62, 946, 1975

2. Bailey, A., Sims, T. and Light, N. Cross-Linking in Type IV Collagen Biochem J 218, 713, 1984

3. Bailey, A., Sims, T., LeLouis, M. and Brazin, S. Collagen Polymorphism in Experimental Granulation Tissue, Biochem Biophys Res Commun, 66, 1160, 1975

4. Bashey, R., Halpem, S., Stephens, R., Perlish, J. and Fleischmajer, R. Solubility of Collagen from Normal and Scleroderma Fibroblasts in Culture, Biochem Biophys Res Commun 62, 303, 1975

5. Becker, H., Furthmayr, H. and Trimple, R. Tryptic Peptides from the Cross-Linking Regions of Insoluble Calf Skin Collagen, Physiol Chem 356, 21 1975

6. Berthet-Colominas, C., Miller, A., Herbage, D., Ronziere, M. and Tocchetti, D. Structural Studies of Collagen Fibres from Intervertebral Disc, Biochim Biophys Acta 706, 50, 1982

7. Birk, D., Fitch, J., Babiarz, J., Doane, K. and Lisenmayer, T. Collagen Fibrilogenesis in vitro: Interaction of Types I and V Collagen Regulates Fibril Diameter, J Cell Sci 95, 649, 1990

8. Bornstein, P. and Sage, H. Structurally Distinct Collagen Types, Annu Rev Biochem 49, 957, 1980

9. Bruckner, P. and van der Rest, M. Structure and Function of Cartilage Collagens, Microsc Res Tech 28, 378, 1994

10. Bruns, R. Beaded Filaments and Long-Spacing Fibrils: Relation to Type VI Collagen, J Ultrastruct Res 89, 136, 1984

11. Burgeson, R. and Nimni, M. Collagen Types - Molecular Structure and Tissue Distribution, Clin Orthop 282, 250, 1992

12. Butler, W., Henning, B., Beegle, W., Taylor, R. and Chung, E. Proteins of the Periodontium. Identification of Collagens with the [alpha-1(I)]2 alpha-2 and [alpha-1(III)]3 Structures in Bovine Periodontal Ligament, J Biol Chem 250, 8907, 1975

13. Campa, J., McAnulty, R. and Laurent, G. Application of High-Pressure Liquid Chromatography to Studies of Collagen Production by Isolated Cells in Culture, Anal Biochem

186, 257, 1990

14. Canalis, E., McCarthy, T. and Centrella, M. Differential Effects of Continuous and Transient Treatment with Parathyroid Hormone Related Peptide (PHrp) on Bone Collagen Synthesis, Endocrinology 126, 1806, 1990

15. Cannon, J. and Cintron, C. Collagen Cross-Linking in Corneal Scar Formation, Biochim Biophys Acta 412, 18, 1975

16. Charonis, A. and Tsilibary, E. Structural and Functional Changes of Laminin and Type-IV Collagen after Nonenzymatic Glycation, Diabetes 41, 49, 1992

17. Chesney, C., Harper, E. and Colman, R. Critical Role of the Carbohydrate Side Chains of Collagen in Platelet Aggregation, J Clin Invest 51, 2693, 1972

18. Cheung, D., DiCesare, P., Benya, P., Libow, E. and Nimni, M. The Presence of Intermolecular Disulfide Crosslinks in Type III Collagen, J Biol Chem 258, 7774, 1983

19. Chiang, T., Beachey, E. and Kang, A. Interaction of a Chick Skin Collagen Fragment (alpha1-CB5) with Human Platelets. Biochemical Studies During the Aggregation and Release Reaction, J Biol Chem 250, 6916, 1975

20. Cooper, D. and Davidson, R. The Effect of Ultraviolet Irradiation on Collagen-Fold Formation, Biochem J 98, 655, 1966

21. Cooper, D. and Davidson, R. The Effect of Ultraviolet Irradiation on Soluble Collagen, Biochem J 97, 139, 1965 22. Daniels, J. and Chu, G. Basement Membrane Collagen of Renal Glomerulus, J Biol Chem

250, 3531, 1975

23. Davidson, J., McEneany, L. and Bornstein, P. Intermediates in the Limited Proteolytic Conversion of Procollagen to Collagen, Biochemistry 14, 5188, 1975

24. Davis, N., Risen, O. and Pringle, G. Stable Nonreducible Cross-Links of Mature Collagen, Biochemistry 14, 2031, 1975

25. Davis, N. Stable Crosslinks of Collagen, Biochem Biophys Res Commun 54, 914, 1973

26. Davison, P. and Brennan, M. Collagenase Digestion Demonstrates Carboxy-Terminal Crosslinking in Acid-Soluble Collagen, Biochim Biophys Acta 708, 141, 1982

27. Davison, P. Diamines and Aminoalcohols: Neutral Solvents for Native Collagen, Conn Tissue Res 24, 129, 1990

28. Deshmukh, K. and Nimni, M. Effects of Lysosomal Enzymes on the Type of Collagen Synthesized by Bovine Articular Cartilage, Biochem Biophys Res Commun 53, 424, 1973

29. Diegelmann, R., Bryson, G., Flood, L. and Graham, M. A Microassay to Quantitate Collagen Synthesis by Cells in Culture, Anal Biochem 186, 296, 1990

30. Dixit, S., Kang, A. and Gross, J. Covalent Structure of Collagen: Amino Acid Sequence of alpha1-CB3 of Chick Skin Collagen, Biochemistry 14, 1929, 1975

31. Dixit, S., Seyer, J., Oronsky, A., Corbett, C., Kang, A. and Gross, J. Covalent Structure of Collagen: Amino Acid Sequence of alpha1-CB6A of Chick Skin Collagen, Biochemistry 14, 1933, 1975

32.Doyle, B., Hukins, D., Hulmes, D., Miller, A., Rattew, C. and Woodhead-Galloway, J.

Origins and Implication of the D Stagger in Collagen, Biochem Biophys Res Commun 60, 858, 1974

33. Drake, M., Davison, P., Bump, S. and Schmitt, F. Action of Proteolytic Enzymes on Tropocollagen and Insoluble Collagen, Biochemistry 5, 301, 1966

34. Dublet, B. and van der Rest, M. Type XII Collagen is Expressed in Embryonic Chick Tendons. Isolation of Pepsin-Derived Fragments, J Biol Chem 262, 17724, 1987

35. Einbinder, J. and Schubert, M. Binding of Mucopolysaccharides and Dyes by Collagen, J Biol Chem 188, 335, 1951

36. Elliot, R. and Gardner, D. A Comparison of Acid-Ninhydrin and Isolation Methods for the Measurement of Proline in Collagen Hydrolysates, Biochem Soc Trans 2, 741, 1975

37. Epstein, E. and Munderloh, N. Isolation and Characterization of CNBr Peptides of Human [alpha-1(III)]3Collagen and Tissue Distribution of [alpha-1(I)]2alpha-2 and [alpha-1(III)]3 Collagens, J Biol Chem 250, 9304, 1975

38. Etherington, D. The Purification of Bovine Cathepsin B1 and its Mode of Action on Bovine Collagens, Biochem J 137, 547, 1974

39. Evans, C. and Drouven, B. The Promotion of Collagen Polymerization by Lanthanide and Calcium Ions, Biochem J 213, 751, 1983

40. Eyre, D., Paz, M. and Gallop, P. Cross-Linking in Collagen and Elastin, Annu Rev Biochem 53, 717, 1984

41. Ferwerda, W., Feltkamp-Vroom, T. and Smit, J. Collagen and Glycoprotein Components Derived from Bovine Tubular Basement Membrane: Chemical and Immunological Properties, Biochem Soc Trans 2, 640, 1975

42. Fietzek, P. and Kuhn, K. The Covalent Structure of Collagen: Amino Acid Sequence of the N-Terminal Region of alpha2-CB5 from Rat Skin Collagen, F.E.B.S. Lett. 36, 289, 1973

43. Fietzek, P. and Kuhn, K. The Covalent Structure of Collagen: Amino-Acid Sequence of the Cyanogen-Bromide Peptides alpha1-CB2, alpha1-CB4 and alpha1-CB5 from Calf-Skin Collagen, Eur J Biochem 52, 77, 1975

44. Fietzek, P. and Rexrodt, F. The Covalent Structure of Collagen. The Amino-Acid Sequence of alpha 2-CB4 from Calf-Skin Collagen, Eur J Biochem 59, 113, 1975

45. Fietzek, P., Rexrodt, F., Hopper, K. and Kuhn, K. The Covalent Structure of Collagen. 2. The Amino-Acid Sequence of alpha 1-CB7 from Calf Skin Collagen, Eur J Biochem 38, 396, 1973

46. Fine, A., Poliks, C., Smith, B. and Goldstein, R. The Accumulation of Type I Collagen mRNAs in Human Embryonic Lung Fibroblast Stimulated by Transforming Growth Factor beta, Conn Tissue Res 24, 237, 1990

47. Folkhard, W., Geercken, W., Knorzer, E., Mosler, E., Nemetschek-Gansler, H., Nemetschek, T. and Koch, M. Structural Dynamic of Native Tendon Collagen, J Mol Biol 193, 405, 1987

48. Fuji, K., Corcoran, D. and Tanzer, M. Isolation and Structure of a Cross-Linked Tripeptide from Calf Bone Collagen, Biochemistry 14, 4409, 1975

49. Fujimori, E. and Shambaugh, N. Cross-Linking and Fluorescence of Pyrene-Labeled Collagen, Biochim Biophys Acta 742, 155, 1983

50. Fujimori, E. Changes Induced by Ozone and Ultraviolet Light in Type I Collagen. Bovine Achilles Tendon Collagen versus Rat Tail Tendon Collagen, Eur J Biochem 152, 299, 1985

51. Fukae, M., Mechanic, G., Adamy, L. and Schwartz, E. Chromatographically Different Type II Collagens from Human Normal and Osteoarthritic Cartilage, Biochem Biophys Res Commun 67, 1575, 1975

52. Gallop, P. and Seifter, S. Preparation and Properties of Soluble Collagens, Methods Enzymol 6, 635, 1963

53. Gay, S. and Miller, E. What is Collagen, What is Not Ultrastruct Pathol 4, 365, 1983

54. Glowacki, J. and Gross, J. Self-Assembly of Mixtures of Collagen Alpha-Chains, Biochim Biophys Acta 668, 216, 1981

55. Gordon, M., Gerecke, D. and Olsen, B. Type XII Collagen: Distinct Extracellular Matrix Component Discovered by cDNA Cloning, Proc Natl Acad Sci USA 84, 6040, 1987

56. Gordon, M., Gerecke, D., Dublet, B., van der Rest, M., Sugrue, S. and Olsen, B. The Structure of Type XII Collagen, Ann N Y Acad Sci 580, 8, 1990

57. Grillo, H. and Gross, J. Thermal Reconstitution of Collagen from Solution and the Response to its Heterologous Implantation, J Surg Res 2, 69, 1962

58. Haidar, A., Wigglesworth, J. and Krausz, T. Type IV Collagen in Developing Human Lung: A Comparison Between Normal and Hypoplastic Fetal Lungs, Early Human Devt 21, 175, 1990

59. Hamlin, C., Kohn, R. and Luschin, J. Apparent Accelerated Aging of Human Collagen in Diabetes Mellitus, Diabetes 24, 902, 1975

60. Hanada, E. and Anan, F. Isolation and Properties of the Insoluble Collagen Fraction from Bovine Nasal Septal Cartilage, J. Biochem. 74, 505, 1973

61. Hayashi, T. and Nagai, Y. Effect of pH on the Stability of Collagen Molecule in Solution, J. Biochem. 73, 999, 1973

62. Hayashi, T. and Nagai, Y. Time-Dependent Increase in Stability of Collagen Fibrils Formed in vitro. Effect of Temperature, J. Biochem. 75, 651, 1974

63. Helseth, D. and Veis, A. Collagen Self-Assembly in vitro. Differentiating Specific Telopeptide-Dependent Interactions Using Selective Enzyme Modification and the Addition of Free Amino Telopeptide, J Biol Chem 256, 7118, 1981

64. Hessle, H. and Engvall, E. Type VI Collagen. Studies on its Localization, Structure, and Biosynthetic Form with Monoclonal Antibodies, J Biol Chem 259, 3955, 1984

65. Highberger, J., Corbett, C., Kang, A. and Cross, J. The Amino Acid Sequence of Chick Skin Collagen alpha 1-CB7, Biochemistry 14, 2872, 1975

66. Hirai, K., Shimizu, Y. and Hino, T. Epithelial Regeneration in Collagen-Coated and Uncoated Patch Grafts Implanted into Dog Tracheas, J Exp Pathol 71, 51, 1990

67. Housley, T., Tanzer, M., Henson, E. and Gallop, P. Collagen Crosslinking: Isolation of Hydroxyaldol-Histidine, a Naturally-Occurring Crosslink, Biochem Biophys Res Commun 67, 824, 1975

68. Hudson, B., Wieslander, J., Wisdom, B. and Noelken, M. Goodpasture Syndrome: Molecular Architecture and Function of Basement Membrane Antigen, Lab Invest 61, 256, 1989

69. Hunt, E. and Morris, H. Collagen Cross-Links. A Mass-Spectrometric and G- and 13C-Nuclear Magnetic-Resonance Study, Biochem J 135, 833, 1973

70. Igarashi, S., Trelstad, R. and Kang, A. Physical and Chemical Properties of Chick Cartilage Collagen, Biochim Biophys Acta 295, 514, 1973

71. Jamieson, G., Urban, C. and Barber, A. Enzymatic Basis for Platelet Aggregation: Collagen Adhesion as the Primary Step in Haemostasis, Nature New Biol 234, 5, 1971

72. Jander, R., Troyer, D. and Rauterberg, J. A Collagen-Like Glycoprotein of the Extracellular Matrix is the Undegraded Form of Type VI Collagen, Biochemistry 23, 3675, 1984

73. Kahn, L. and Witnauer, L. The Viscometric Behavior of Solubilized Calf Skin Collagen at Low Rates of Shear, J Biol Chem 241, 1784, 1966

74. Kapoor, R., Sakai, L., Funk, S., Roux, E., Bornstein, P. and Sage, E. Type VIII Collagen Has a Restricted Distribution in Specialized Extracellular Matrices, J Cell Biol 107, 721, 1988

75. Kasten, M., Burkhardt, H., von Roden, H. and Rauls, S. A Spectroscopic Collagenase Assay Using Peroxidase-Labeled Collagen, Anal Biochem 176, 150, 1989

76. Katzman, R., Kang, A. and Beachey, E. Collagen-Induced Platelet Aggregation: Involvement of an Active Glycopeptide Fragment (a1-CB5), Science 181, 670, 1973

77. Keene, D., Engvall, E. and Glanville, R. Ultrastructure of Type VI Collagen in Human Skin and Cartilage Suggests an Anchoring Function for This Filamentous Network, J Cell Biol 107, 1995, 1988

78. Kittelberger, R., Davis, P., Flynn, D. and Greenhill, N. Distribution of Type VIII Collagen in Tissues: An Immunohistochemical Study, Conn Tissue Res 24, 303, 1990

79. Lampiaho, K., Kari, A., Niinikoski, J. and Kulonen, E. Time Course of Action of Pepsin on Insoluble and Soluble Collagens, Acta Chem Scand 20, 1446, 1966

80. Lenaers, A. and Lapiere, C. Type III Procollagen and Collagen in Skin, Biochim Biophys Acta 400, 121, 1975

81. Lichenstein, J., Byers, P., Smith, B. and Martin, G. Identification of the Collagenous Proteins Synthesized by Cultured Cells from Human Skin, Biochemistry 14, 1589, 1975

82. Lunstrum, G., Mcdonough, A., Marinkovich, M., Keene, D., Morris, N. and Burgeson, R. Identification and Partial Purification of a Large, Variant Form of Type-XII Collagen, J Biol Chem 267, 20087, 1992

83. Meredith, S. and Kezdy, F. The Chromatographic Purification of Native Types I, II and III Collagens, Biochim Biophys Acta 668, 357, 1981

84. Miller, E. and Matukas, V. Chick Cartilage Collagen: A New Type of alpha 1 Chain Not Present in Bone or Skin of the Species, Proc Natl Acad Sci USA 64, 1264, 1969

85. Mitchell, T. and Rigby, B. in vivo and in vitro Aging of Collagen Examined Using an Isometric Melting Technique, Biochim Biophys Acta 393, 531, 1975

86. Mustard, J., Cazevave, J., Packham, M. and Toronto, H. Adherence of Platelets to a Collagen-Coated Surface: Development of a Quantitive Method, J Lab Clin Med 82, 978, 1973

87. Myers, J., Jones, T., Pohjolainen, E., Kadri, A., Goddard, A., Sheer, D., Solomon, E. and Pihlajaniemi, T. Molecular Cloning of alpha 5(IV) Collagen and Assignment of the Gene to the Region of the X Chromosome Containing the Alport Syndrome Locus, Am J Hum Genet 46, 1024, 1990

88. Na, G., Butz, L. and Carroll, R. Mechanism of in vitro Collagen Assembly. Kinetic and Morphological Studies, J Biol Chem 261, 12290, 1986

89. Na, G. Interaction of Calf Skin Collagen with Glycerol: Linked Function Analysis, Biochemistry 25, 967, 1986

90. Nakanishi, M., Imamura, H. and Goto, K. Potentiation of the ADP-Induced Platelet Aggregation by Collagen and its Inhibition by a Tetrahydrothieno-Pyridine Derivative (gamma-3642), Biochem Pharmacol 20, 2116, 1971

91. Negro, A., Garbisa, S., Gotte, L. and Spina, M. The Use of Reverse-Phase High-Performance Liquid Chromatography and Precolumn Derivatization with Dansyl Chloride for Quantitation of Specific Amino Acids in Collagen and Elastin, Anal Biochem 160, 39, 1987

92. Newman, R. and Langner, R. Comparison of TCA and Collagenase in the Isolation of Tissue Collagen, Anal Biochem 66, 175, 1975

93. Obrink, B., Laurent, T. and Carlsson, B. The Binding of Chondroitin Sulphate to Collagen, F.E.B.S. Lett. 56, 166, 1975

94. Oikawa, T., Sayama, K., Matsuda, Y., Fujimoto, Y., Iwaguchi, T. and Matsuzawa, A. Characterization of Two Possible Forms of Type IV Collagen from Human Kidney Cortex, Biochem Int 19, 615, 1989

95. Ono, M., Aratani, Y., Kitagawa, I. and Kitagawa, Y. Ascorbic Acid Phosphate Stimulates Type IV Collagen Synthesis and Accelerates Adipose Conversion of 3T3-L1 Cells, Exp Cell Res 187, 309, 1990

96. Ooshima, A., Fuller, G., Cardinale, G., Spector, S. and Udenfriend, S Collagen Biosynthesis in Blood Vessels of Brain and Other Tissues of the Hypertensive Rat, Science 190, 898, 1975

97. Oryan, A., Moshiri, A., Meimandi-Parizi, A. and Maffulli, N. Role of Xenogenous Bovine Platelet Gel Embedded within Collagen Implant on Tendon Healing: An in vitro and in vivo Study., Exp Biol Med 240, 194, 2015

98. Packman, M. and Guccione, M. Inhibition of the Platelet Responses to Synergistic Effects of Collagen and ADP, Fed Proc 32, 844, 1973

99. Pardo, A. and Tamayo, R. The Presence of Collagenase in Collagen Preparations, Biochim Biophys Acta 392, 121, 1975

100. Parreno, J., Raju, S., Niaki, M., Andrejevic, K., Jiang, A., Delve, E. and Kandel, R.

Expression of Type I Collagen and Tenascin C is Regulated by Actin Polymerization Through MRTF in Dedifferentiated Chondrocytes, F.E.B.S. Lett. 588, 3677, 2014

101. Piez, K. and Torchida, D. Possible Contribution of Ionic Clustering to Molecular Packing of Collagen, Nature 258, 87, 1975

102. Puett, D., Wasserman, B., Ford, J. and Cunningham, L. Collagen-mediated Platelet Aggregation. Effects of Collagen Modification Involving the Protein and Carbohydrate Moieties, J Clin Invest 52, 2495, 1973

103. Puett, D. and Cunningham, L. Effect of Collagen Modification on Platelet Aggregation, Fed Proc 32, 614, 1973

104. Quteish, D., Singh, G. and Dobly, A. Development and Testing of a Human Collagen Graft Material, J Biomed Mater Res 24, 749, 1990

105. Rexrodt, F., Fietzek, P. and Kuhn, K. The Covalent Structure of Collagen. The Chymotrypsin, Trypsin and Hydroxylamine Peptides Derived form alpha2-CB4 of Calf-Skin Collagen, Eur J Biochem 59, 105, 1975

106. Rexrodt, F., Hopper, K., Fietzek, P. and Kuhn, K. The Covalent Structure of Collagen. 1. The Chymotrypsin, Trypsin and Thermolysin-Derived Peptides of alpha1-CB7 from Calf-Skin Collagen, Eur J Biochem 38, 384, 1973

107. Ricard-Blum, S. The Collagen Family, Cold Spring Harb Perspect Biol 3, a004978, 2011

108. Robertson, W., Rose, K., Hudson, B. and Vanacore, R. Supramolecular Organization of the alpha121-alpha565 Collagen IV Network, J Biol Chem 289, 25601, 2014

109. Robins, S. and Bailey, A. The Chemistry of the Collagen Cross-Links. The Characterization of Fraction C, a Possible Artifact Produced During the Reduction of Collagen Fibres with Borohydride, Biochem J 135, 657, 1973

110. Robins, S. and Bailey, A. The Chemistry of the Collagen Cross-Links. The Mechanism of Stabilization of the Reducible Intermediate Cross-Links, Biochem J 149, 381, 1975

111. Robins, S., Shimokomaki, M. and Bailey, A. The Chemistry of the Collagen Cross-Links. Age-Related Changes in Reducible Components of Intact Bovine Collagen Fibres, Biochem J 131, 771, 1973

112. Roelofs, L., Kortmann, B., Oosterwijk, E., Eggink, A., Tiemessen, D., Crevels, A., Wijnen, R., Daamen, W., van Kuppevelt, T., Geutjes, P. and Feitz, W. Tissue Engineering of Diseased Bladder Using a Collagen Scaffold in a Bladder Exstrophy Model, BJU Int 114, 447, 2014

113. Russell, A. Effect of pH on Thermal Stability of Collagen in the Dispersed and Aggregated States, Biochem J 139, 277, 1974

114. Ryhanen, L., Zaragoza, E. and Uitto, J. Conformational Stability of Type 1 Collagen Triple Helix: Evidence for Temporary and Local Relaxation of the Protein Conformation Using a Proteolytic Probe, Arch Biochem Biophys 223, 562, 1983

115. Salem, G. and Traub, W. Conformation Implications of Amino Acid Sequence Regularities in Collagen, F.E.B.S. Lett. 51, 94, 1975

116. Sandberg, M., Tamminen, M., Hirvonen, H., Vuorio, E. and Pihlajaniemi, T.

Expression of mRNAs Coding for the alpha 1 Chain of Type XIII Collagen in Human Fetal Tissues: Comparison with Expression of mRNAs for Collagen types I, II, and III, J Cell Biol 109, 1371, 1989

117. Schmid, T. and Linsenmayer, T. Denaturation-Renaturation Properties of Two Molecular Forms of Short-Chain Cartilage Collagen, Biochemistry 23, 553, 1984

118. Scott, P. Spectroscopic Study of Environment-Dependent Changes in the Conformation of the Isolated Carboxy-Terminal Telopeptide of Type I Collagen, Biochemistry 25, 974, 1986

119. Seifter, S. and Gallop, P., The Proteins, 2nd ed Vol. IV, H. Neurath, Academic Press, NY, 238, 1966

120. Shen, G., Butkowski, R., Cheng, T., Wieslander, J., Katz, A., Cass, J. and Fish, R. Comparison of Non-collagenous Type IV Collagen Subunits in Human Glomerular Basement Membrane, Alveolar Basement Membrane, and Placenta, Conn Tissue Res 24, 289, 1990

121. Shuttleworth, C. and Forrest, L. Changes in Guinea-Pig Dermal Collagen During Development, Eur J Biochem 55, 391, 1975

122. Shuttleworth, C., Forrest, L. and Jackson, D. Comparison of the Cyanogen Bromide Peptides of Insoluble Guinea-Pig Skin and Scar Collagen, Biochim Biophys Acta 379, 207, 1975

123. Siegel, R. and Lian, J. Lysyl Oxidase Dependent Synthesis of a Collagen Cross-Link Containing Histidine, Biochem Biophys Res Commun 67, 1353, 1975

124. Stanley, N., Alper, R., Cunningham, E., Cherniack, N. and Kefalides, N. Effects of a Molecular Changes in Collagen on Lung Structure and Mechanical Function, J Clin Invest 55, 1195, 1975

125. Stevens, F. and Thomas, H. Preparation of Insoluble Collagen from Human Cartilage, Biochem J 135, 245, 1973

126. Stinson, R. Structural Deterioration of Tendon Collagen in Genetic Muscular Dystrophy, Biochim Biophys Acta 400, 255, 1975

127. Sugrue, S., Gordon, M., Seyer, J., Dublet, B., van der Rest, M. and Olsen, B. Immunoidentification of Type XII Collagen in Embryonic Tissues, J Cell Biol 109, 939, 1989

128. Swann, D., Chesney, C., Constable, I., Colman, R., Caulfield, J. and Harper, E. The Role of Vitreous Collagen in Platelet Aggregation in vitro and in vivo, J Lab Clin Med 84, 264, 1974

129. Tanzer, M., Housley, T., Berube, L., Fairweather, R., Franzblau, C. and Gallop, P. Structure of Two Histidine-Containing Cross-Links from Collagen, J Biol Chem 248, 393, 1973

130. Tekari, A., Luginbuehl, R., Hofstetter, W. and Egli, R. Chondrocytes Expressing Intracellular Collagen Type II Enter the Cell Cycle and Co-Express Collagen Type I in Monolayer Culture, J Orthop Res 32, 1503, 2014

131. Terajima, M., Perdivara, I., Sricholpech, M., Deguchi, Y., Pleshko, N., Tomer, K. and Yamauchi, M. Glycosylation and Cross-Linking in Bone Type I Collagen, J Biol Chem 289, 22636, 2014

132. Thomas, J., Ayad, S. and Grant, M. Cartilage Collagens: Strategies for the Study of Their Organisation and Expression in the Extracellular Matrix, Ann Rheum Dis 53, 488, 1994

133. Toole, B. and Lowther, D. Precipitation of Collagen Fibrils in vitro by Protein Polysaccharides, Biochem Biophys Res Commun 29, 515, 1967

134. Torbet, J. and Ronziere, M. Magnetic Alignment of Collagen During Self-Assembly, Biochem J 219, 1057, 1984

135. Tristram, G., Worral, J. and Streer, D. Thermal Denaturation of Soluble Calf Skin Collagen, Biochem J 95, 350, 1965

136. Tseng, S., Savion, N., Gospodarowicz, D. and Stern, R. Characterization of Collagens Synthesized by Cultured Bovine Corneal Endothelial Cells, J Biol Chem 256, 3361, 1981

137. Uitto, J., Hoffmann, H. and Prockop, K. Retention of Nonhelical Procollagen Containing cis-Hydroxyproline in Rough Endoplasmic Reticulum, Science 190, 1202, 1975

138. Venkatasubramanian, K., Saini, R. and Vieth, W. On the Mechanism of Enzyme and Whole Microbial Cell Attachment to Collagen, Ferm Tech 52, 268, 1974

139. Venn, G., Mehta, M. and Mason, R. Characterization of Collagen from Normal and Scoliolic Human Spinal Ligament, Biochim Biophys Acta 757, 259, 1983

140. Verzar, F. and Stritmattier-Ackershott, E. Studies on Ageing of Collagen by Perchlorate Reactions, Experientia 31, 1183, 1975

141. Wang, S. and Vieth, W. Collagen-Enzyme Complex Membranes and Their Perfomance in Biocatalytic Modules, Biotechnol Bioeng 15, 93, 1973

142. Weber, S., Engel, J., Wiedemann, H., Glanville, R. and Timple, R. Subunit Structure and Assembly of the Globular Domain of Basement-Membrane Collagen Type IV, Eur J Biochem 139, 401, 1984

143. Weinstock, M. and Leblond, C. Synthesis, Migration, and Release of Precursor Collagen by Odontoblasts as Visualized by Radioautography After [3H] Proline Administration, J Cell Biol 60, 92, 1974

144. Weiss, J., Shuttleworth, C., Brown, R. and Hunter, J. Letter: Polymeric Type-III Collagen in Inflamed Human Synovia, Lancet 2, 85, 1975

145. Weiss, J., Shuttleworth, C., Brown, R., Sedowfia, K., Baildam, A. and Hunter, J. Occurence of Type III Collagen in Inflamed Synovial Membranes: A Comparison Between Non-Rheumatoid, Rheumatoid, and Normal Synovial Collagens, Biochem Biophys Res Commun 65, 907, 1975

146. Wilkinson, M., Cohen, R. and Shuman M. A Nonradioactive Assay for Type IV Collagen Degradation, Anal Biochem 185, 294, 1990

147. Woodhead-Galloway, J., Hukins, D. and Wray, J. Closest Packing of Two-Stranded Coiled-Coils as a Model for the Collagen Fibril, Biochem Biophys Res Commun 64, 1237, 1975

148. Wu, J. and Eyre, D. Covalent Interactions of Type IX Collagen in Cartilage, Conn Tissue Res 20, 241, 1989

149. Yamaguchi, N., Benya, P., van der Rest, M. and Ninomiya, Y. The Cloning and Sequencing of alpha 1(VIII) Collagen cDNAs Demonstrate that Type VIII Collagen is a Short

149. Chain Collagen and Contains Triple-Helical and Carboxyl-Terminal Non-Triple-Helical Domains Similar to Those of Type X Collagen, J Biol Chem 264, 16022, 1989

150. Yasui, N., Benya, P. and Nimni, M. Identification of a Large Interrupted Helical Domain of Disulfide-bonded Cartilage Collagen, J Biol Chem 259, 14175, 1984

151. York, T., Kahan, L., Lake, S. and Gruev, V. Real-Time High-Resolution Measurement of Collagen Alignment in Dynamically Loaded Soft Tissue, J Biomed Opt 19, 066011, 2014

152. Yurchenco, P. and Furthmayr, H. Self-Assembly of Basement Membrane Collagen, Biochemistry 23, 1839, 1984


Turmeric Bibliography

1. The Effects of Curcumin on Weight Loss Among Patients With Metabolic Syndrome and Related Disorders: A Systematic Review and Meta-Analysis of Randomized Controlled Trials. Maryam Akbari, Kamran B. Lankarani, Reza Tabrizi, Majid Ghayour-Mobarhan, Payam Peymani, Gordon Ferns, Amir Ghaderi, and Zatollah Asemi. Front Pharmacol. 2019; 10: 649. Published online 2019 Jun 12. doi: 10.3389/fphar.2019.00649

2. Adab Z., Eghtesadi S., Vafa M., Heydari I., Shojaei A., Haqqani H., et al. (2013). Effect of turmeric on body measurement indices, glycemic condition, and lipid profile in hyperlipidemic patients with type 2 diabetes. Iranian J. Nutr. Sci. Food Technol. 8 (3), 217–227.

3. Amin F., Islam N., Anila N., Gilani A. H. (2015). Clinical efficacy of the co-administration of Turmeric and Black seeds (Kalongi) in metabolic syndrome - a double blind randomized controlled trial - TAK-MetS trial. Complement. Ther. Med. 23 (2), 165–174. 10.1016/j.ctim.2015.01.008  [CrossRef]

4. Binion D. G., Otterson M. F., Rafiee P. (2008). Curcumin inhibits VEGF-mediated angiogenesis in human intestinal microvascular endothelial cells through COX-2 and MAPK inhibition. Gut 57 (11), 1509–1517. 10.1136/gut.2008.152496 [PMC free article]  [CrossRef]

5. Chainani-Wu N. (2003). Safety and anti-inflammatory activity of curcumin: a component of tumeric (Curcuma longa). J. Altern. Complement. Med. 9 (1), 161–168. 10.1089/107555303321223035 

 6. Chuengsamarn S., Rattanamongkolgul S., Luechapudiporn R., Phisalaphong C., Jirawatnotai S. (2012). Curcumin extract for prevention of type 2 diabetes. Diabetes Care 35 (11), 2121–2127. 10.2337/dc12-0116 [PMC free article] 

7. Chuengsamarn S., Rattanamongkolgul S., Phonrat B., Tungtrongchitr R., Jirawatnotai S. (2014). Reduction of atherogenic risk in patients with type 2 diabetes by curcuminoid extract: a randomized controlled trial. J. Nutr. Biochem. 25 (2), 144–150. 10.1016/j.jnutbio.2013.09.013 

8. Di Pierro F., Bressan A., Ranaldi D., Rapacioli G., Giacomelli L., Bertuccioli A. (2015). Potential role of bioavailable curcumin in weight loss and omental adipose tissue decrease: preliminary data of a randomized, controlled trial in overweight people with metabolic syndrome. Eur. Rev. Med. Pharmacol. Sci. 19 (21), 4195–4202. 

9. Dong S.z., Zhao S.p., Wu Z.h. (2007). Curcumin induced adiponectin expression in adipocyte through PPARγ. J. Clin. Res. 8, 1.

10. Ejaz A., Wu D., Kwan P., Meydani M. (2009). Curcumin inhibits adipogenesis in 3T3-L1 adipocytes and angiogenesis and obesity in C57/BL mice. J. Nutr. 139 (5), 919–925. 10.3945/jn.108.100966 

11. Ewang-Emukowhate M., Perera D., Wierzbicki A. S. (2014). Dyslipidaemia related to insulin resistance and cardiovascular disease in South Asian and West African populations. Curr. Pharm. Des. 20 (40), 6270–6275. 10.2174/1381612820666140620114948 

12. Ghazimoradi M., Saberi-Karimian M., Mohammadi F., Sahebkar A., Tavallaie S., Safarian H., et al. (2017). The effects of curcumin and curcumin–phospholipid complex on the serum pro-oxidant–antioxidant balance in subjects with metabolic syndrome. Phytother. Res. 31 (11), 1715–1721. 10.1002/ptr.5899 

13. Hu G. X., Lin H., Lian Q. Q., Zhou S. H., Guo J., Zhou H. Y., et al. (2013). Curcumin as a potent and selective inhibitor of 11beta-hydroxysteroid dehydrogenase 1: improving lipid profiles in high-fat-diet-treated rats. PLoS One 8 (3), e49976. 10.1371/journal.pone.0049976 [PMC free article]   

14. Ismail N. A., El Dayem S. M., Salama E., Ragab S., El Baky A. N., Ezzat W. M. (2016). Impact of curcumin intake on gluco-insulin homeostasis, leptin and adiponectin in obese subjects. Res. J. Pharm. Biol. Chem. Sci. 7 (1), 1891–1897.

15. Ismail N. A., Ragab S., El Baky A., Hamed M., Ibrahim A. (2014). Effect of oral curcumin administration on insulin resistance, serum resistin and fetuin-A in obese children: randomized placebo-controlled study. Res. J. Pharm. Biol. Chem. Sci. 5, 887–896.

16. Kocher A., Bohnert L., Schiborr C., Frank J. (2016). Highly bioavailable micellar curcuminoids accumulate in blood, are safe and do not reduce blood lipids and inflammation markers in moderately hyperlipidemic individuals. Mol. Nutr. Food Res. 60 (7), 1555–1563. 10.1002/mnfr.201501034 

17. Lee Y. K., Lee W. S., Hwang J. T., Kwon D. Y., Surh Y. J., Park O. J. (2009). Curcumin exerts antidifferentiation effect through AMPKalpha-PPAR-gamma in 3T3-L1 adipocytes and antiproliferatory effect through AMPKalpha-COX-2 in cancer cells. J. Agric. Food. Chem. 57 (1), 305–310. 10.1021/jf802737z 

18. Mohammadi A., Sadeghnia H. R., Saberi-Karimian M., Safarian H., Ferns G. A., Ghayour-Mobarhan M. (2017). Effects of curcumin on serum vitamin E concentrations in individuals with metabolic syndrome. Phytother. Res. 31 (4), 657–662. 10.1002/ptr.5779 

19. Mohammadi A., Sahebkar A., Iranshahi M., Amini M., Khojasteh R., Ghayour-Mobarhan M., et al. (2013). Effects of supplementation with curcuminoids on dyslipidemia in obese patients: a randomized crossover trial. Phytother. Res. 27 (3), 374–379. 10.1002/ptr.4715 

20. Nieman D. C., Cialdella-Kam L., Knab A. M., Shanely R. A. (2012). Influence of red pepper spice and turmeric on inflammation and oxidative stress biomarkers in overweight females: a metabolomics approach. Plant Foods Hum. Nutr. 67 (4), 415–421. 10.1007/s11130-012-0325-x 

21. Panahi Y., Hosseini M. S., Khalili N., Naimi E., Simental-Mendia L. E., Majeed M., et al. (2016). Effects of curcumin on serum cytokine concentrations in subjects with metabolic syndrome: a post-hoc analysis of a randomized controlled trial. Biomed. Pharmacother. 82, 578–582. 10.1016/j.biopha.2016.05.037 

22. Panahi Y., Khalili N., Hosseini M. S., Abbasinazari M., Sahebkar A. (2014). Lipid-modifying effects of adjunctive therapy with curcuminoids-piperine combination in patients with metabolic syndrome: results of a randomized controlled trial. Complement. Ther. Med. 22 (5), 851–857. 10.1016/j.ctim.2014.07.006 

23. Panahi Y., Khalili N., Sahebi E., Namazi S., Karimian M. S., Majeed M., et al. (2017. a). Antioxidant effects of curcuminoids in patients with type 2 diabetes mellitus: a randomized controlled trial. Inflammopharmacology 25 (1), 25–31. 10.1007/s10787-016-0301-4 

24. Panahi Y., Kianpour P., Mohtashami R., Jafari R., Simental-Mendia L. E., Sahebkar A. (2017. b). Efficacy and safety of phytosomal curcumin in non-alcoholic fatty liver disease: a randomized controlled trial. Drug Res. 67 (4), 244–251. 10.1055/s-0043-100019 

25. Rahimi H. R., Mohammadpour A. H., Dastani M., Jaafari M. R., Abnous K., Ghayour Mobarhan M., et al. (2016). The effect of nano-curcumin on HbA1c, fasting blood glucose, and lipid profile in diabetic subjects: a randomized clinical trial. Avicenna J. Phytomed. 6 (5), 567–577. [PMC free article] 

26. Rahmani S., Asgary S., Askari G., Keshvari M., Hatamipour M., Feizi A., et al. (2016). Treatment of non-alcoholic fatty liver disease with curcumin: a randomized placebo-controlled trial. Phytother. Res. 30 (9), 1540–1548. 10.1002/ptr.5659 

27. Sahebkar A., Mohammadi A., Atabati A., Rahiman S., Tavallaie S., Iranshahi M., et al. (2013). Curcuminoids modulate pro-oxidant-antioxidant balance but not the immune response to heat shock protein 27 and oxidized LDL in obese individuals. Phytother. Res. 27 (12), 1883–1888. 10.1002/ptr.4952 

28. Wang S. L., Li Y., Wen Y., Chen Y. F., Na L. X., Li S. T., et al. (2009). Curcumin, a potential inhibitor of up-regulation of TNF-alpha and IL-6 induced by palmitate in 3T3-L1 adipocytes through NF-kappaB and JNK pathway. Biomed. Environ. Sci. 22 (1), 32–39. 10.1016/S0895-3988(09)60019-2 

29. Weisberg S. P., Leibel R., Tortoriello D. V. (2008). Dietary curcumin significantly improves obesity-associated inflammation and diabetes in mouse models of diabesity. Endocrinology 149 (7), 3549–3558. 10.1210/en.2008-0262 [PMC free article] 

30. Yang Y. S., Su Y. F., Yang H. W., Lee Y. H., Chou J. I., Ueng K. C. (2014). Lipid-lowering effects of curcumin in patients with metabolic syndrome: a randomized, double-blind, placebo-controlled trial. Phytother. Res. 28 (12), 1770–1777. 10.1002/ptr.5197 



Ginkgo biloba Bibliography

1. Allain H, Raoul P, Lieury A, LeCoz F, Gandon JM, D’Arbigny P. Effect of two doses of Gingko biloba extract (EGb 761) on the dual-coding test in elderly subjects. Clinical Therapeutics. 1993;15(3):549–558.

2. Itil T, Martorano D. Natural substances in psychiatry (Ginkgo biloba in dementia) Psychopharmacology Bulletin. 1995;31(1):147–158.

3. Kanowski S, Herrmann WM, Stephan K, Wierich W, Hörr R. Proof of efficacy of the ginkgo biloba special extract EGb 761 in outpatients suffering from mild to moderate primary degenerative dementia of the Alzheimer type or multi-infarct dementia. Pharmacopsychiatry. 1996;29(2):47–56.

4. Le Bars PL, Katz MM, Berman N, Itil TM, Freedman AM, Schatzberg AF. A placebo-controlled, double-blind, randomized trial of an extract of Ginkgo biloba for dementia. Journal of the American Medical Association. 1997;278(16):1327–1332.

5. Ramassamy C, Longpre F, Christen Y. Ginkgo biloba extract (EGb 761) in Alzheimer’s disease: is there any evidence? Current Alzheimer Research. 2007;4(3):253–262.

6. Zimmermann M, Colciaghi F, Cattabeni F, Di Luca M. Ginkgo biloba extract: from molecular mechanisms to the treatment of Alzhelmer’s disease. Cellular and Molecular Biology. 2002;48(6):613–623.

7. Elsabagh S, Hartley DE, Ali O, Williamson EM, File SE. Differential cognitive effects of Ginkgo biloba after acute and chronic treatment in healthy young volunteers. Psychopharmacology. 2005;179(2):437–446.

8. Gertz HJ, Kiefer M. Review about Ginkgo biloba special extract EGb 761 (Ginkgo) Current Pharmaceutical Design. 2004;10(3):261–264.

9. Kennedy DO, Jackson PA, Haskell CF, Scholey AB. Modulation of cognitive performance following single doses of 120 mg Ginkgo biloba extract administered to healthy young volunteers. Human Psychopharmacology. 2007;22(8):559–566.

10. Kennedy DO, Scholey AB, Wesnes KA. The dose-dependent cognitive effects of acute administration of Ginkgo biloba to healthy young volunteers. Psychopharmacology. 2000;151(4):416–423.

11. Kurz A, Van Baelen B. Ginkgo biloba compared with cholinesterase inhibitors in the treatment of dementia: a review based on meta-analyses by the cochrane collaboration. Dementia and Geriatric Cognitive Disorders. 2004;18(2):217–226.

12. Mazza M, Capuano A, Bria P, Mazza S. Ginkgo biloba and donepezil: a comparison in the treatment of Alzheimer's dementia in a randomized placebo-controlled double-blind study. European Journal of Neurology. 2006;13(9):981–985.

13. Rigney U, Kimber S, Hindmarch I. The effects of acute doses of standardized Ginkgo biloba extract on memory and psychomotor performance in volunteers. Phytotherapy Research. 1999;13(5):408–415.

14. Scholey A, Kennedy D. Acute, dose-dependent cognitive effects of Ginkgo biloba, Panax ginseng and their combination in healthy young volunteers: differential interactions with cognitive demand. Human Psychopharmacology. 2002;17(1):35–44.

15. Stough C, Clarke J, Lloyd J, Nathan PJ. Neuropsychological changes after 30-day Ginkgo biloba administration in healthy participants. International Journal of Neuropsychopharmacology. 2001;4(2):131–134.

16. Subhan Z, Hindmarch I. The psychopharmacological effects of Ginkgo biloba extract in normal healthy volunteers. International Journal of Clinical Pharmacology Research. 1984;4(2):89–93.

17. Wesnes K, Simmons D, Rook M, Simpson P. A double-blind placebo-controlled trial of Tanakan in the treatment of idiopathic cognitive impairment in the elderly. Human Psychopharmacology. 1987;2:159–169.

18. Weinmann S, Roll S, Schwarzbach C, Vauth C, Willich SN. Effects of Ginkgo biloba in dementia: systematic review and meta-analysis. BMC Geriatrics. 2010;10 Article ID 14. [PMC free article]

19. DeKosky ST, Williamson JD, Fitzpatrick AL, et al. Ginkgo biloba for prevention of dementia: a randomized controlled trial. Journal of the American Medical Association. 2008;300(19):2253–2262. 

20. Andrieu S, Ousset PJ, Coley N, Ouzid M, Mathiex-Fortunet H, Vellas B. GuidAge study: a 5-year double blind, randomised trial of EGb 761 for the prevention of Alzheimer’s disease in elderly subjects with memory complaints. I. Rationale, design and baseline data. Current Alzheimer Research. 2008;5(4):406–415.

21. IPSEN. Encouraging results of GuidAge, large scale European trial conducted in the prevention of Alzheimer’s Dementia. 2010. 22 June. http://www.ipsen.com/en/encouraging-results-guidage-large-scale-european-trial-conducted-prevention-alzheimer-s-dementia.

22. Kaschel R. Ginkgo biloba: specificity of neuropsychological improvement—a selective review in search of differential effects. Human Psychopharmacology. 2009;24(5):345–370.

23. Kennedy DO, Scholey AB, Wesnes KA. Differential, dose dependent changes in cognitive performance following acute administration of a Ginkgo biloba/Panax ginseng combination to healthy young volunteers. Nutritional Neuroscience. 2001;4(5):399–412.

24. Polich J, Gloria R. Cognitive effects of a Ginkgo biloba/vinpocetine compound in normal adults: systematic assessment of perception, attention and memory. Human Psychopharmacology. 2001;16(5):409–416.

25. DeFeudis FV, Drieu K. Ginkgo biloba extract (EGb 761) and CNS functions: basic studies and clinical applications. Current Drug Targets. 2000;1(1):25–58.

26. Ahlemeyer B, Krieglstein J. Neuroprotective effects of Ginkgo biloba extract. Cellular and Molecular Life Sciences. 2003;60(9):1779–1792.

27. Nathan P. Can the cognitive enhancing effects of Ginkgo biloba be explained by its pharmacology? Medical Hypotheses. 2000;55(6):491–493.

28. Mahadevan S, Park Y. Multifaceted therapeutic benefits of Ginkgo biloba L.: chemistry, efficacy, safety, and uses. Journal of Food Science. 2008;73(1):R14–R19.

29. Krištofiková Z. In vitro effect of Ginkgo biloba extract (EGb 761) on the activity of presynaptic cholinergic nerve terminals in rat hippocampus. Dementia and Geriatric Cognitive Disorders. 1997;8(1):43–48.

30. Rendeiro C, Spencer JPE, Vauzour D, Butler LT, Ellis JA, Williams CM. The impact of flavonoids on spatial memory in rodents: from behaviour to underlying hippocampal mechanisms. Genes and Nutrition. 2009;4(4):251–270. [PMC free article]

31. Chopin P, Briley M. Effects of four non-cholinergic cognitive enhancers in comparison with tacrine and galanthamine on scopolamine-induced amnesia in rats. Psychopharmacology. 1992;106(1):26–30.

32. Taylor JE. Neuromediator binding to receptors in the rat brain. The effect of chronic administration of Ginkgo biloba extract. Presse Medicale. 1986;15:491–493.

33. Ellis KA, Nathan PJ. The pharmacology of human working memory. International Journal of Neuropsychopharmacology. 2001;4(3):299–313.

34. Furey ML, Pietrini P, Alexander GE, Schapiro MB, Horwitz B. Cholinergic enhancement improves performance on working memory by modulating the functional activity in distinct brain regions: a positron emission tomography regional cerebral blood flow study in healthy humans. Brain Research Bulletin. 2000;51(3):213–218.

35. Furey ML, Pietrini P, Haxby JV. Cholinergic enhancement and increased selectivity of perceptual processing during working memory. Science. 2000;290(5500):2315–2319.

36. Rombouts SARB, Barkhof F, Van Meel CS, Scheltens P. Alterations in brain activation during cholinergic enhancement with rivastigmine in Alzheimer’s disease. Journal of Neurology Neurosurgery and Psychiatry. 2002;73(6):665–671. [PMC free article]

37. Terry AV, Jackson WJ, Buccafusco JJ. Effects of concomitant cholinergic and adrenergic stimulation on learning and memory performance by young and aged monkeys. Cerebral Cortex. 1993;3(4):304–312.

38. Mori K, Yamashita H, Nagao M, Horiguchi J, Yamawaki S. Effects of anticholinergic drug withdrawal on memory, regional cerebral blood flow and extra-pyramidal side effects in schizophrenic patients. Pharmacopsychiatry. 2002;35(1):6–11.

39. Rusted JM. Dissociative effects of scopolamine on working memory in healthy young volunteers. Psychopharmacology. 1988;96(4):487–492.

40. Itil TM, Eralp E, Tsambis E, Itil KZ, Stein U. Central nervous system effects of Ginkgo biloba, a plant extract. American Journal of Therapeutics. 1996;3(1):63–73.

41. Kennedy DO, Scholey AB, Drewery L, Marsh VR, Moore B, Ashton H. Electroencephalograph effects of single doses of Ginkgo biloba and Panax ginseng in healthy young volunteers. Pharmacology Biochemistry and Behavior. 2003;75(3):701–709.

42. Hofferberth B. The efficacy of EGb 761 in patients with senile dementia of the Alzheimer type, a double-blind, placebo-controlled study on different levels of investigation. Human Psychopharmacology. 1994;9(3):215–222.

43. Klimesch W. EEG alpha and theta oscillations reflect cognitive and memory performance: a review and analysis. Brain Research Reviews. 1999;29(2-3):169–195.

44. Semlitsch HV, Anderer P, Saletu B, Binder GA, Decker KA. Cognitive psychophysiology in nootropic drug research: effects of Ginkgo biloba on event-related potentials (P300) in age-associated memory impairment. Pharmacopsychiatry. 1995;28(4):134–142.

45. Santos RF, Galduróz JCF, Barbieri A, Castiglioni MLV, Ytaya LY, Bueno OFA. Cognitive performance, SPECT, and blood viscosity in elderly non-demented people using Ginkgo biloba. Pharmacopsychiatry. 2003;36(4):127–133.

46. Timerbaeva SL, Suslina ZA, Bodareva EA, Fedin PA, Korepina OS, Pervozvansky BE. Tanakan in the treatment of primary manifestations of insufficiency of brain blood supply. Zhurnal Nevropatolgii i Psikhiatrii im. S S Korsakova. 2000;100(8):24–28.

47. Silberstein RB, Farrow M, Levy F, Pipingas A, Hay DA, Jarman FC. Functional brain electrical activity mapping in boys with attention- deficit/hyperactivity disorder. Archives of General Psychiatry. 1998;55(12):1105–1112.

48. Silberstein RB, Nunez PL, Pipingas A, Harris P, Danieli F. Steady state visually evoked potential (SSVEP) topography in a graded working memory task. International Journal of Psychophysiology. 2001;42(2):219–232.

49. Naghavi HR, Nyberg L. Common fronto-parietal activity in attention, memory, and consciousness: shared demands on integration? Consciousness and Cognition. 2005;14(2):390–425.

50. Wager TD, Smith EE. Neuroimaging studies of working memory: a meta-analysis. Cognitive, Affective and Behavioral Neuroscience. 2003;3(4):255–274.

51. Vanderplas JM, Garvin EA. The association value of random shapes. Journal of Experimental Psychology. 1959;57(3):147–154.

52. Silberstein RB, Schier MA, Pipingas A, Ciorciari J, Wood SR, Simpson DG. Steady-state visually evoked potential topography associated with a visual vigilance task. Brain Topography. 1990;3(2):337–347.

53. Silberstein RB. Steady-state visually evoked potentials, brain resonances, and cognitive processes. In: Nunez PL, editor. Neocortical Dynamics and Human EEG Rhythms. New York, NY, USA: Oxford University Press; 1995. pp. 272–303.

54. Silberstein RB, Ciorciari J, Pipingas A. Steady-state visually evoked potential topography during the Wisconsin card sorting test. Electroencephalography and Clinical Neurophysiology. 1995;96(1):24–35.

55. Regan D. Human Brain Electrophysiology: Evoked Potentials and Evoked Magnetic Fields in Science and Medicine. New York, NY, USA: Elsevier; 1989.

56. Gasser T, Sroka L, Mocks J. The transfer of EOG activity into the EEG for eyes open and closed. Electroencephalography and Clinical Neurophysiology. 1985;61(2):181–193.

57. Nunez PL, Silberstein RB, Cadusch PJ, Wijesinghe R. Comparison of high resolution EEG methods having different theoretical bases. Brain Topography. 1993;5(4):361–364.

58. Duffy FH, Bartels PH, Burchfiel JL. Significance probability mapping: an aid in the topographic analysis of brain electrical activity. Electroencephalography and Clinical Neurophysiology. 1981;51(5):455–462.

59. Harner RN. Topographic analysis of multichannel EEG data. In: Samson-Dollfus D, editor. Statistics and Topography in Quantitative EEG. New York, NY, USA: Elsevier; 1988. pp. 49–61.

60. Silberstein RB, Cadusch PJ. Measurement processes and spatial principal components analysis. Brain Topography. 1992;4(4):267–276.

61. Perlstein WM, Cole MA, Larson M, Kelly K, Seignourel P, Keil A. Steady-state visual evoked potentials reveal frontally-mediated working memory activity in humans. Neuroscience Letters. 2003;342(3):191–195.

62. Perlstein WM, Elbert T, Stenger VA. Dissociation in human prefrontal cortex of affective influences on working memory-related activity. Proceedings of the National Academy of Sciences of the United States of America. 2002;99(3):1736–1741. [PMC free article]

63. Jensen O, Gelfand J, Kounios J, Lisman JE. Oscillations in the alpha band (9-12 Hz) increase with memory load during retention in a short-term memory task. Cerebral Cortex. 2002;12(8):877–882.

64. Klimesch W, Doppelmayr M, Schwaiger J, Auinger P, Winkler TH. ‘Paradoxical‘ alpha synchronization in a memory task. Cognitive Brain Research. 1999;7(4):493–501.

65. Van Rooy C, Stough C, Pipingas A, Hocking C, Silberstein RB. Spatial working memory and intelligence biological correlates. Intelligence. 2001;29(4):275–292.

66. Pfurtscheller G, Lopes Da Silva FH. Event-related EEG/MEG synchronization and desynchronization: basic principles. Clinical Neurophysiology. 1999;110(11):1842–1857.

67. Itil TM, Eralp E, Ahmed I, Kunitz A, Itil KZ. The pharmacological effects of Ginkgo biloba, a plant extract, on the brain of dementia patients in comparison with tacrine. Psychopharmacology Bulletin. 1998;34(3):391–397.

68. R. B. Silberstein, A. Pipingas, J. Song, D. A. Camfield, P. J. Nathan, and C. Stough. Examining Brain-Cognition Effects of Ginkgo Biloba Extract: Brain Activation in the Left Temporal and Left Prefrontal Cortex in an Object Working Memory Task. Evid Based Complement Alternat Med. 2011; 2011: 164139.


Cannabidiol (CBD) Bibliography

1. Iffland K, Grotenhermen F. An Update on Safety and Side Effects of Cannabidiol: A Review of Clinical Data and Relevant Animal Studies. Cannabis Cannabinoid Res. 2017;2(1):139-154. [PMC free article]

2. Davies C, Bhattacharyya S. Cannabidiol as a potential treatment for psychosis. Ther Adv Psychopharmacol. 2019;9:2045125319881916. [PMC free article]

3. Li H, Liu Y, Tian D, Tian L, Ju X, Qi L, Wang Y, Liang C. Overview of cannabidiol (CBD) and its analogues: Structures, biological activities, and neuroprotective mechanisms in epilepsy and Alzheimer's disease. Eur J Med Chem. 2020 Apr 15;192:112163.

4. Silvestro S, Mammana S, Cavalli E, Bramanti P, Mazzon E. Use of Cannabidiol in the Treatment of Epilepsy: Efficacy and Security in Clinical Trials. Molecules. 2019 Apr 12;24(8) [PMC free article]

5. Lattanzi S, Brigo F, Trinka E, Zaccara G, Striano P, Del Giovane C, Silvestrini M. Adjunctive Cannabidiol in Patients with Dravet Syndrome: A Systematic Review and Meta-Analysis of Efficacy and Safety. CNS Drugs. 2020 Mar;34(3):229-241.

6. Laczkovics C, Kothgassner OD, Felnhofer A, Klier CM. Cannabidiol treatment in an adolescent with multiple substance abuse, social anxiety and depression. Neuropsychiatr. 2021 Mar;35(1):31-34. [PMC free article]

7. Levinsohn EA, Hill KP. Clinical uses of cannabis and cannabinoids in the United States. J Neurol Sci. 2020 Apr 15;411:116717.

8. Crippa JA, Guimarães FS, Campos AC, Zuardi AW. Translational Investigation of the Therapeutic Potential of Cannabidiol (CBD): Toward a New Age. Front Immunol. 2018;9:2009. [PMC free article]

9. Watt G, Karl T. In vivo Evidence for Therapeutic Properties of Cannabidiol (CBD) for Alzheimer's Disease. Front Pharmacol. 2017;8:20. [PMC free article]

10. Gray RA, Whalley BJ. The proposed mechanisms of action of CBD in epilepsy. Epileptic Disord. 2020 Jan 01;22(S1):10-15.

10. Millar SA, Stone NL, Yates AS, O'Sullivan SE. A Systematic Review on the Pharmacokinetics of Cannabidiol in Humans. Front Pharmacol. 2018;9:1365. [PMC free article]

11. MacCallum CA, Russo EB. Practical considerations in medical cannabis administration and dosing. Eur J Intern Med. 2018 Mar;49:12-19.

12. O'Connell BK, Gloss D, Devinsky O. Cannabinoids in treatment-resistant epilepsy: A review. Epilepsy Behav. 2017 May;70(Pt B):341-348.

13. Devinsky O, Patel AD, Thiele EA, Wong MH, Appleton R, Harden CL, Greenwood S, Morrison G, Sommerville K., GWPCARE1 Part A Study Group. Randomized, dose-ranging safety trial of cannabidiol in Dravet syndrome. Neurology. 2018 Apr 03;90(14):e1204-e1211. [PMC free article]

14. Chen JW, Borgelt LM, Blackmer AB. Cannabidiol: A New Hope for Patients With Dravet or Lennox-Gastaut Syndromes. Ann Pharmacother. 2019 Jun;53(6):603-611.

15. Brown JD, Winterstein AG. Potential Adverse Drug Events and Drug-Drug Interactions with Medical and Consumer Cannabidiol (CBD) Use. J Clin Med. 2019 Jul 08;8(7) [PMC free article]

16. Ali S, Scheffer IE, Sadleir LG. Efficacy of cannabinoids in paediatric epilepsy. Dev Med Child Neurol. 2019 Jan;61(1):13-18.

17. Gaston TE, Szaflarski JP. Cannabis for the Treatment of Epilepsy: an Update. Curr Neurol Neurosci Rep. 2018 Sep 08;18(11):73.

18. Serafini G, Pompili M, Innamorati M, Rihmer Z, Sher L, Girardi P. Can cannabis increase the suicide risk in psychosis? A critical review. Curr Pharm Des. 2012;18(32):5165-87.

19. White CM. A Review of Human Studies Assessing Cannabidiol's (CBD) Therapeutic Actions and Potential. J Clin Pharmacol. 2019 Jul;59(7):923-934.

20. Bergamaschi MM, Queiroz RH, Zuardi AW, Crippa JA. Safety and side effects of cannabidiol, a Cannabis sativa constituent. Curr Drug Saf. 2011 Sep 01;6(4):237-49.

21. VanDolah HJ, Bauer BA, Mauck KF. Clinicians' Guide to Cannabidiol and Hemp Oils. Mayo Clin Proc. 2019 Sep;94(9):1840-1851.

22. Zaheer S, Kumar D, Khan MT, Giyanwani PR, Kiran F. Epilepsy and Cannabis: A Literature Review. Cureus. 2018 Sep 10;10(9):e3278. [PMC free article]

23. Cao D, Srisuma S, Bronstein AC, Hoyte CO. Characterization of edible marijuana product exposures reported to United States poison centers. Clin Toxicol (Phila). 2016 Nov;54(9):840-846.

24. Szkudlarek HJ, Desai SJ, Renard J, Pereira B, Norris C, Jobson CEL, Rajakumar N, Allman BL, Laviolette SR. Δ-9-Tetrahydrocannabinol and Cannabidiol produce dissociable effects on prefrontal cortical executive function and regulation of affective behaviors. Neuropsychopharmacology. 2019 Mar;44(4):817-825.