XLOS-observed mutations of MID1 Bbox1 domain cause domain unfolding.
about
Molecular dynamics simulation reveals insights into the mechanism of unfolding by the A130T/V mutations within the MID1 zinc-binding Bbox1 domain.Structural and functional observations of the P151L MID1 mutation reveal alpha4 plays a significant role in X-linked Opitz Syndrome.Obtaining Soluble Folded Proteins from Inclusion Bodies Using Sarkosyl, Triton X-100, and CHAPS: Application to LB and M9 Minimal Media.
P2860
XLOS-observed mutations of MID1 Bbox1 domain cause domain unfolding.
description
2014 nî lūn-bûn
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2014 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2014 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2014年の論文
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2014年論文
@yue
2014年論文
@zh-hant
2014年論文
@zh-hk
2014年論文
@zh-mo
2014年論文
@zh-tw
2014年论文
@wuu
name
XLOS-observed mutations of MID1 Bbox1 domain cause domain unfolding.
@ast
XLOS-observed mutations of MID1 Bbox1 domain cause domain unfolding.
@en
type
label
XLOS-observed mutations of MID1 Bbox1 domain cause domain unfolding.
@ast
XLOS-observed mutations of MID1 Bbox1 domain cause domain unfolding.
@en
prefLabel
XLOS-observed mutations of MID1 Bbox1 domain cause domain unfolding.
@ast
XLOS-observed mutations of MID1 Bbox1 domain cause domain unfolding.
@en
P2093
P2860
P1433
P1476
XLOS-observed mutations of MID1 Bbox1 domain cause domain unfolding.
@en
P2093
Haijuan Du
Katharine M Wright
Kuanlin Wu
Michael A Massiah
Omotolani Babatunde
P2860
P304
P356
10.1371/JOURNAL.PONE.0107537
P407
P577
2014-09-12T00:00:00Z