Engineering, biophysical characterisation and binding properties of a soluble mutant form of annexin A2 domain IV that adopts a partially folded conformation.
about
Protein structure and oligomerization are important for the formation of export-competent HIV-1 Rev-RRE complexes.Domains I and IV of annexin A2 affect the formation and integrity of in vitro capillary-like networks.PKU mutation p.G46S prevents the stereospecific binding of l-phenylalanine to the dimer of human phenylalanine hydroxylase regulatory domain.Domain IV of Annexin A5 Is Critical for Binding Calcium and Guarantees Its Maximum Binding to the Phosphatidylserine Membrane.
P2860
Engineering, biophysical characterisation and binding properties of a soluble mutant form of annexin A2 domain IV that adopts a partially folded conformation.
description
2006 nî lūn-bûn
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name
Engineering, biophysical chara ...... partially folded conformation.
@en
Engineering, biophysical chara ...... partially folded conformation.
@nl
type
label
Engineering, biophysical chara ...... partially folded conformation.
@en
Engineering, biophysical chara ...... partially folded conformation.
@nl
prefLabel
Engineering, biophysical chara ...... partially folded conformation.
@en
Engineering, biophysical chara ...... partially folded conformation.
@nl
P2093
P1476
Engineering, biophysical chara ...... partially folded conformation
@en
P2093
Anni Vedeler
Frode Berven
Gilles Travé
Hanne Hollås
Ingvild Aukrust
Lasse Evensen
Torgeir Flatmark
P304
P356
10.1016/J.JMB.2006.08.042
P407
P50
P577
2006-08-22T00:00:00Z