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2. 5 Best Weight Loss Supplements to Kickstart Your Health ... - AOL

   www.aol.com/entertainment/5-best-weight-loss...

   It’s made from collagen derived from 4 authentic food sources (eggshell, fish, beef and chicken) and contains silica to increase bioavailability. Pros: Low-calorie supplement

3. Gelatin - Wikipedia

   en.wikipedia.org/wiki/Gelatin

   It may also be referred to as hydrolyzed collagen, collagen hydrolysate, gelatine hydrolysate, hydrolyzed gelatine, and collagen peptides after it has undergone hydrolysis. It is commonly used as a gelling agent in food, beverages, medications, drug or vitamin capsules, photographic films, papers, and cosmetics.

4. Vitamin K - Wikipedia

   en.wikipedia.org/wiki/Vitamin_K

   Vitamin K is a family of structurally similar, fat-soluble vitamers found in foods and marketed as dietary supplements. [1] The human body requires vitamin K for post-synthesis modification of certain proteins that are required for blood coagulation ("K" from Danish koagulation, for "coagulation") or for controlling binding of calcium in bones and other tissues. [2]

5. Chondroitin sulfate - Wikipedia

   en.wikipedia.org/wiki/Chondroitin_sulfate

   Chemical structure of one unit in a chondroitin sulfate chain. Chondroitin-4-sulfate: R 1 = H; R 2 = SO 3 H; R 3 = H. Chondroitin-6-sulfate: R 1 = SO 3 H; R 2, R 3 = H.. Chondroitin sulfate is a sulfated glycosaminoglycan (GAG) [1] composed of a chain of alternating sugars (N-acetylgalactosamine and glucuronic acid).

6. AOL Mail

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   Get AOL Mail for FREE! Manage your email like never before with travel, photo & document views. Personalize your inbox with themes & tabs. You've Got Mail!

7. Collagen receptor - Wikipedia

   en.wikipedia.org/wiki/Collagen_receptor

   Collagen binding is primarily provided by integrins α1β1, α2β1, α10β1 and α11β1. Integrin α1β1 binds to collagen via the MIDAS motif in the α subunit I domain. It preferentially binds collagens IV, VI and type XIII collagen, but also fibril-forming collagens. Specific binding sites in collagen I and IV have been identified.