✦ LIBER ✦

Altered collagen structure in mouse tail tendon lacking the α2(I) chain

✍ Scribed by Daniel J McBride Jr; Vincent Choe; Jay R Shapiro; Barbara Brodsky

Book ID: 115627997
Publisher: Elsevier Science
Year: 1997
Tongue: English
Weight: 360 KB
Volume: 270
Category: Article
ISSN: 0022-2836
DOI: 10.1006/jmbi.1997.1106

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

Covalent Structure of Collagen : Salient

Covalent Structure of Collagen : Salient Differences in the α2(I) Polypeptide Chain

✍ JEROME M. SEYER; ANDREW H. KANG 📂 Article 📅 1985 🏛 John Wiley and Sons 🌐 English ⚖ 141 KB

Identification of Two Repressor Elements

Identification of Two Repressor Elements in the Mouse α2(I) Collagen Promoter

✍ Kai Miao; James J. Potter; Frank A. Anania; Lynda Rennie-Tankersley; Esteban Mez 📂 Article 📅 1999 🏛 Elsevier Science 🌐 English ⚖ 349 KB

A Structurally Abnormal α2(I) Collagen C

A Structurally Abnormal α2(I) Collagen Chain in a Further Patient with the Ehlers-Danlos Syndrome Type VII

✍ BEAT STEINMANN; VELIDI H. RAO; RICHARD GITZELMANN 📂 Article 📅 1985 🏛 John Wiley and Sons 🌐 English ⚖ 185 KB

The Role of the α2 Chain in the Stabiliz

The Role of the α2 Chain in the Stabilization of the Collagen Type I Heterotrimer: A Study of the Type I Homotrimer in oim Mouse Tissues

✍ Christopher A. Miles; Trevor J. Sims; Nancy P. Camacho; Allen J. Bailey 📂 Article 📅 2002 🏛 Elsevier Science 🌐 English ⚖ 186 KB

Structural requirements of antigenic det

Structural requirements of antigenic determinants in the aminoterminal region of the rat collagen α2 chain

✍ Heinz Furthmayr; Rupert Timpl 📂 Article 📅 1972 🏛 Elsevier Science 🌐 English ⚖ 366 KB

(G586V) substitutions in the α1 and α2 c

(G586V) substitutions in the α1 and α2 chains of collagen I: Effect of α-chain stoichiometry on the phenotype of osteogenesis imperfecta?

✍ Allan M. Lund; Flemming Skovby; Marianne Schwartz 📂 Article 📅 1997 🏛 John Wiley and Sons 🌐 English ⚖ 166 KB 👁 1 views

Osteogenesis imperfecta (OI) is a congenital disease of connective tissue, most often caused by single amino acid substitutions of glycine residues within the triple helical region of collagen I. Collagen I consists of two alpha 1 chains and one alpha 2 chain. Thus, a substitution in the alpha 1(I)