Solution structure of Kti11p from Saccharomyces cerevisiae reveals a novel zinc-binding module.
about
Structure and mechanistic insights into novel iron-mediated moonlighting functions of human J-protein cochaperone, Dph4The diphthamide modification pathway from Saccharomyces cerevisiae--revisitedStructure of the Elongator cofactor complex Kti11/Kti13 provides insight into the role of Kti13 in Elongator-dependent tRNA modificationA genome-wide screen identifies genes required for formation of the wobble nucleoside 5-methoxycarbonylmethyl-2-thiouridine in Saccharomyces cerevisiae.The biosynthesis and biological function of diphthamideAllele-specific suppressors of lin-1(R175Opal) identify functions of MOC-3 and DPH-3 in tRNA modification complexes in Caenorhabditis elegansDph3, a small protein required for diphthamide biosynthesis, is essential in mouse developmentAn Iron Reservoir to the Catalytic Metal: THE RUBREDOXIN IRON IN AN EXTRADIOL DIOXYGENASE.Dph3 is an electron donor for Dph1-Dph2 in the first step of eukaryotic diphthamide biosynthesis.The tRNA modification complex elongator regulates the Cdc42-dependent mitogen-activated protein kinase pathway that controls filamentous growth in yeast.Zinc cysteine active sites of metalloproteins: a density functional theory and x-ray absorption fine structure study.Structural asymmetry in the eukaryotic Elongator complex.Structural insights into the function of Elongator.An iron-sulfur cluster domain in Elp3 important for the structural integrity of elongator.
P2860
Q24306304-190064D8-8BCC-4C61-AEFF-48ED14BDBCADQ27011240-D82C584E-7E2E-4EBF-B3FC-C7E948D458D7Q27697604-AFD35C73-5CBF-4897-9184-7A181CC105C0Q27936390-1153161C-EEF5-4A2E-A472-D13CB5A21FBFQ28297199-B455A620-CF4C-4C7B-ABA1-E008CC8850B9Q34082199-D9992EDA-0591-431C-AD5A-50967E275945Q34717308-DB216FBF-7441-499E-8C38-05647AFAE596Q35860669-92C1436E-B1AA-4A2D-B900-573CC3A99F79Q38732919-4DC3B968-C4CD-499F-B0A5-FE45B1295D91Q41888858-060F0FA1-1934-4869-B892-C9F7CE32E03EQ46686459-692559A6-7417-4298-9BA3-4E7CCC8B67FAQ47727561-72027ECD-A40B-4722-9A3A-394DAEC95771Q48248158-08C6B9FA-F98B-4D04-B9C9-3780D2B8D708Q52590116-ED09D30A-69BF-4E8E-897D-E364DE70DA98
P2860
Solution structure of Kti11p from Saccharomyces cerevisiae reveals a novel zinc-binding module.
description
2005 nî lūn-bûn
@nan
2005 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
Solution structure of Kti11p f ...... s a novel zinc-binding module.
@ast
Solution structure of Kti11p f ...... s a novel zinc-binding module.
@en
type
label
Solution structure of Kti11p f ...... s a novel zinc-binding module.
@ast
Solution structure of Kti11p f ...... s a novel zinc-binding module.
@en
prefLabel
Solution structure of Kti11p f ...... s a novel zinc-binding module.
@ast
Solution structure of Kti11p f ...... s a novel zinc-binding module.
@en
P2093
P356
P1433
P1476
Solution structure of Kti11p f ...... ls a novel zinc-binding module
@en
P2093
Fangming Wu
Jiahai Zhang
Jianping Sun
P304
P356
10.1021/BI0504714
P407
P577
2005-06-01T00:00:00Z