Chemical properties of the peptide extension in the pα 1 chain of dermatosparactic skin procollagen
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(72)80723-3/fullpdf
Reference18 articles.
1. Studies on protocollagen: Identification of a precursor of proto α1
2. Evidence for Procollagen, a Biosynthetic Precursor of Collagen
3. A Transport Form of Collagen from Embryonic Tendon: Electron Microscopic Demonstration of an NH2-Terminal Extension and Evidence Suggesting the Presence of Cystine in the Molecule
4. Characterization of the Pro-α1 Chain of Procollagen
5. Collagen Made of Extended alpha-Chains, Procollagen, in Genetically-Defective Dermatosparaxic Calves
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2. Characterization of the Alzheimer's Disease-associated CLAC Protein and Identification of an Amyloid β-Peptide-binding Site;Journal of Biological Chemistry;2005-01
3. Initial observations of human dermatosparaxis: Ehlers-Danlos syndrome type VIIC;The Journal of Pediatrics;1992-10
4. Fetal antigen 2: An amniotic protein identified as the aminopropeptide of the α1 chain of human procollagen type I;APMIS;1992-07
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