Position of single amino acid substitutions in the collagen triple helix determines their effect on structure of collagen fibrils

This publication has 42 references indexed in Scilit:

• Skeletal abnormalities and ultrastructural changes of cartilage in transgenic mice expressing a collagen II gene (COL2A1) with a Cys for Arg-α1-519 substitution
  Osteoarthritis and Cartilage, 2002
• Collagen II Containing a Cys Substitution for Arg-α1−519: Abnormal Interactions of the Mutated Molecules with Collagen IX
  Biochemistry, 2001
• Collagen XI Nucleates Self-assembly and Limits Lateral Growth of Cartilage Fibrils
  Journal of Biological Chemistry, 2000
• Collagen II containing a Cys substitution for Arg-α1-519. Analysis by atomic force microscopy demonstrates that mutated monomers alter the topography of the surface of collagen II fibrils
  Matrix Biology, 1999
• Collagen II Containing a Cys Substitution for Arg-α1-519: HOMOTRIMERIC MONOMERS CONTAINING THE MUTATION DO NOT ASSEMBLE INTO FIBRILS BUT ALTER THE SELF-ASSEMBLY OF THE NORMAL PROTEIN
  Published by Elsevier ,1997
• Assembly of Thin and Thick Fibrils of Collagen II from Recombinant Procollagen II
  Journal of Biological Chemistry, 1996
• Arg⁵¹⁹‐Cys Mutation in COL2A1: Evidence for Multiple Foundersa
  Annals of the New York Academy of Sciences, 1996
• Single base mutation in the type II procollagen gene (COL2A1) as a cause of primary osteoarthritis associated with a mild chondrodysplasia.
  Proceedings of the National Academy of Sciences, 1990
• Collagen type I and type V are present in the same fibril in the avian corneal stroma.
  The Journal of cell biology, 1988
• Collagen type IX: Evidence for covalent linkages to type II collagen in cartilage
  FEBS Letters, 1987