Mutation of amino acid residues in the mobile loop region of the NAD(H)-binding domain of proton-translocating transhydrogenase-Reference-Cited by-同舟云学术

登录注册会员服务联系我们

Mutation of amino acid residues in the mobile loop region of the NAD(H)-binding domain of proton-translocating transhydrogenase

Published:1998-11 Issue:1 Volume:1409 Page:25-38
ISSN:0005-2728
Container-title:Biochimica et Biophysica Acta (BBA) - Bioenergetics
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Bioenergetics

Author:

Gupta Susmita,Quirk Philip G.,Venning Jamie D.,Slade James,Bizouarn Tania,Grimley Rachel L.,Cotton Nick P.J.,Jackson J.Baz

Publisher

Elsevier BV

Subject

Cell Biology,Biochemistry,Biophysics

Reference34 articles.

1. J.B. Jackson, P.G. Quirk, N.P.J. Cotton, J.D. Venning, S. Gupta, T. Bizouarn, S.J. Peake, C.M. Thomas, Biochim. Biophys. Acta (1998) in press.

2. Molecular biology of nicotinamide nucleotide transhydrogenase — a unique proton pump

3. Nicotinamide nucleotide transhydrogenase: a model for utilization of substrate binding energy for proton translocation

4. Physiological roles of nicotinamide nucleotide transhydrogenase

5. Proton-translocating transhydrogenase and NAD- and NADP-linked isocitrate dehydrogenases operate in a substrate cycle which contributes to fine regulation of the tricarboxylic acid cycle activity in mitochondria

Cited by 11 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Review and Hypothesis. New insights into the reaction mechanism of transhydrogenase: Swivelling the dIII component may gate the proton channel;FEBS Letters;2015-07-02

2. Substitution of Tyrosine 146 in the dI Component of Proton-translocating Transhydrogenase Leads to Reversible Dissociation of the Active Dimer into Inactive Monomers;Journal of Biological Chemistry;2007-12

3. The Role of Invariant Amino Acid Residues at the Hydride Transfer Site of Proton-translocating Transhydrogenase;Journal of Biological Chemistry;2006-05

4. Active-Site Conformational Changes Associated with Hydride Transfer in Proton-Translocating Transhydrogenase,;Biochemistry;2004-08-01

5. Glutamine 132 in the NAD(H)-Binding Component of Proton-Translocating Transhydrogenase Tethers the Nucleotides before Hydride Transfer;Biochemistry;2003-01-16

同舟云学术

1.学者识别学者识别

2.学术分析学术分析

3.人才评估人才评估

"同舟云学术"是以全球学者为主线，采集、加工和组织学术论文而形成的新型学术文献查询和分析系统，可以对全球学者进行文献检索和人才价值评估。用户可以通过关注某些学科领域的顶尖人物而持续追踪该领域的学科进展和研究前沿。经过近期的数据扩容，当前同舟云学术共收录了国内外主流学术期刊6万余种，收集的期刊论文及会议论文总量共计约1.5亿篇，并以每天添加12000余篇中外论文的速度递增。我们也可以为用户提供个性化、定制化的学者数据。欢迎来电咨询！咨询电话：010-8811{复制后删除}0370

www.globalauthorid.com

TOP

Copyright © 2019-2024 北京同舟云网络信息技术有限公司
京公网安备11010802033243号京ICP备18003416号-3