Molecular basis for the polymerization of octopus lens S-crystallin
about
Structure of a Highly Active Cephalopod S-crystallin Mutant: New Molecular Evidence for Evolution from an Active Enzyme into Lens-Refractive ProteinLower urinary tract physiology and pharmacology.Symmetry, equivalence, and molecular self-assembly.Increased contractility of diabetic rabbit corpora smooth muscle in response to endothelin is mediated via Rho-kinase beta.
P2860
Molecular basis for the polymerization of octopus lens S-crystallin
description
2000 nî lūn-bûn
@nan
2000 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
Molecular basis for the polymerization of octopus lens S-crystallin
@ast
Molecular basis for the polymerization of octopus lens S-crystallin
@en
Molecular basis for the polymerization of octopus lens S-crystallin
@nl
type
label
Molecular basis for the polymerization of octopus lens S-crystallin
@ast
Molecular basis for the polymerization of octopus lens S-crystallin
@en
Molecular basis for the polymerization of octopus lens S-crystallin
@nl
prefLabel
Molecular basis for the polymerization of octopus lens S-crystallin
@ast
Molecular basis for the polymerization of octopus lens S-crystallin
@en
Molecular basis for the polymerization of octopus lens S-crystallin
@nl
P2093
P2860
P1433
P1476
Molecular basis for the polymerization of octopus lens S-crystallin
@en
P2093
P2860
P304
P356
10.1016/S0006-3495(00)76754-3
P407
P577
2000-04-01T00:00:00Z