Allosteric control in a metalloprotein dramatically alters function.
about
Utilizing a dynamical description of IspH to aid in the development of novel antimicrobial drugsPierced Lasso Bundles are a new class of knot-like motifsMolecular Dynamics Simulations of the [2Fe-2S] Cluster-Binding Domain of NEET Proteins Reveal Key Molecular Determinants That Induce Their Cluster Transfer/Release.Flavin nucleotides act as electron shuttles mediating reduction of the [2Fe-2S] clusters in mitochondrial outer membrane protein mitoNEET.Structure of the human monomeric NEET protein MiNT and its role in regulating iron and reactive oxygen species in cancer cells.The unique fold and lability of the [2Fe-2S] clusters of NEET proteins mediate their key functions in health and disease.
P2860
Allosteric control in a metalloprotein dramatically alters function.
description
2012 nî lūn-bûn
@nan
2012 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2012 թվականի դեկտեմբերին հրատարակված գիտական հոդված
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2012年の論文
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2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
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name
Allosteric control in a metalloprotein dramatically alters function
@nl
Allosteric control in a metalloprotein dramatically alters function.
@ast
Allosteric control in a metalloprotein dramatically alters function.
@en
type
label
Allosteric control in a metalloprotein dramatically alters function
@nl
Allosteric control in a metalloprotein dramatically alters function.
@ast
Allosteric control in a metalloprotein dramatically alters function.
@en
prefLabel
Allosteric control in a metalloprotein dramatically alters function
@nl
Allosteric control in a metalloprotein dramatically alters function.
@ast
Allosteric control in a metalloprotein dramatically alters function.
@en
P2093
P2860
P356
P1476
Allosteric control in a metalloprotein dramatically alters function.
@en
P2093
Aina E Cohen
Charles Wang
Elizabeth Leigh Baxter
Herbert L Axelrod
John A Zuris
Jose N Onuchic
Mark L Paddock
Patricia A Jennings
Phu Luong T Vo
P2860
P304
P356
10.1073/PNAS.1208286110
P407
P577
2012-12-27T00:00:00Z