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70 in total

1. Activation of expression of genes coding for extracellular matrix proteins in Tat-producing glioblastoma cells.

Authors: J P Taylor; C Cupp; A Diaz; M Chowdhury; K Khalili; S A Jimenez; S Amini
Journal: Proc Natl Acad Sci U S A Date: 1992-10-15 Impact factor: 11.205

2. A dominant mutation in the COL1A1 gene that substitutes glycine for valine causes recurrent lethal osteogenesis imperfecta.

Authors: J Bonaventure; L Cohen-Solal; C Lasselin; P Maroteaux
Journal: Hum Genet Date: 1992-08 Impact factor: 4.132

3. Lysyl hydroxylation in collagens from hyperplastic callus and embryonic bones.

Authors: H W Lehmann; M Bodo; C Frohn; A Nerlich; D Rimek; H Notbohm; P K Müller
Journal: Biochem J Date: 1992-03-01 Impact factor: 3.857

4. Designed to fail: a novel mode of collagen fibril disruption and its relevance to tissue toughness.

Authors: Samuel P Veres; J Michael Lee
Journal: Biophys J Date: 2012-06-19 Impact factor: 4.033

5. A single base mutation in type I procollagen (COL1A1) that converts glycine alpha 1-541 to aspartate in a lethal variant of osteogenesis imperfecta: detection of the mutation with a carbodiimide reaction of DNA heteroduplexes and direct sequencing of products of the PCR.

Authors: J P Zhuang; C D Constantinou; A Ganguly; D J Prockop
Journal: Am J Hum Genet Date: 1991-06 Impact factor: 11.025

6. Location of glycine mutations within a bacterial collagen protein affects degree of disruption of triple-helix folding and conformation.

Authors: Haiming Cheng; Shayan Rashid; Zhuoxin Yu; Ayumi Yoshizumi; Eileen Hwang; Barbara Brodsky
Journal: J Biol Chem Date: 2010-11-11 Impact factor: 5.157

7. Type-III procollagen assembly in semi-intact cells: chain association, nucleation and triple-helix folding do not require formation of inter-chain disulphide bonds but triple-helix nucleation does require hydroxylation.

Authors: N J Bulleid; R Wilson; J F Lees
Journal: Biochem J Date: 1996-07-01 Impact factor: 3.857

Proteolytic enzymes as probes for the triple-helical conformation of procollagen.