Molecular Simulations Reveal an Unresolved Conformationof the Type IA Protein Kinase A Regulatory Subunit and Suggest ItsRole in the cAMP Regulatory Mechanism
Molecular Simulations Reveal an Unresolved Conformationof the Type IA Protein Kinase A Regulatory Subunit and Suggest ItsRole in the cAMP Regulatory Mechanism
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Biochemistry
DOI: 10.1021/acs.biochem.7b00461
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07-18-2017 07:52 AM
Mechanism of Selective Nickel Transfer from HypB toHypA, Escherichia coli [NiFe]-Hydrogenase AccessoryProteins
Mechanism of Selective Nickel Transfer from HypB toHypA, Escherichia coli -Hydrogenase AccessoryProteins
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.6b00706/20161130/images/medium/bi-2016-00706s_0007.gif
Biochemistry
DOI: 10.1021/acs.biochem.6b00706
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12-01-2016 12:20 AM
Substrate–Protein Interactions of Type II NADH:QuinoneOxidoreductase from Escherichia coli
Substrate–Protein Interactions of Type II NADH:QuinoneOxidoreductase from Escherichia coli
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.6b00070/20160505/images/medium/bi-2016-00070d_0011.gif
Biochemistry
DOI: 10.1021/acs.biochem.6b00070
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05-06-2016 03:39 AM
[NMR paper] NMR Binding and Crystal Structure Reveal that Intrinsically-unstructured Regulatory Domain Auto-inhibits PAK4 by a Mechanism Different for that of PAK1.
NMR Binding and Crystal Structure Reveal that Intrinsically-unstructured Regulatory Domain Auto-inhibits PAK4 by a Mechanism Different for that of PAK1.
NMR Binding and Crystal Structure Reveal that Intrinsically-unstructured Regulatory Domain Auto-inhibits PAK4 by a Mechanism Different for that of PAK1.
Biochem Biophys Res Commun. 2013 Jul 19;
Authors: Wang W, Lim L, Baskaran Y, Manser E, Song J
Abstract
Six human PAK members are classified into groups I (PAKs 1-3) and II (PAK4-6). Previously, only group I PAKs were thought to be...
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07-24-2013 04:52 PM
Discovered a new regulatory mechanism of c-Src, the human protein bound to ... - HealthCanal.com
Discovered a new regulatory mechanism of c-Src, the human protein bound to ... - HealthCanal.com
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Discovered a new regulatory mechanism of c-Src, the human protein bound to ...
HealthCanal.com
... leader of the Biomolecular Nuclear Magnetic Resonance (NMR) Research Group, affiliated with the Department of Organic Chemistry of the UB, â??the discovery of a new regulatory mechanism in such a relevant and extensively studied protein proves the ...
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02-20-2013 05:54 AM
[NMR paper] NMR characterization of the Escherichia coli nitrogen regulatory protein IIANtr in so
NMR characterization of the Escherichia coli nitrogen regulatory protein IIANtr in solution and interaction with its partner protein, NPr.
Related Articles NMR characterization of the Escherichia coli nitrogen regulatory protein IIANtr in solution and interaction with its partner protein, NPr.
Protein Sci. 2005 Apr;14(4):1082-90
Authors: Wang G, Peterkofsky A, Keifer PA, Li X
The solution form of IIA(Ntr) from Escherichia coli and its interaction with its partner protein, NPr, were characterized by nuclear magnetic resonance (NMR)...
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11-24-2010 11:14 PM
[NMR paper] NMR characterization of a single-cysteine mutant of Escherichia coli thioredoxin and
NMR characterization of a single-cysteine mutant of Escherichia coli thioredoxin and a covalent thioredoxin-peptide complex.
Related Articles NMR characterization of a single-cysteine mutant of Escherichia coli thioredoxin and a covalent thioredoxin-peptide complex.
Eur J Biochem. 1998 Oct 15;257(2):299-308
Authors: Jeng MF, Reymond MT, Tennant LL, Holmgren A, Dyson HJ
The mechanism of disulfide reduction by thioredoxin in the cell is thought to occur through the formation and subsequent destruction of a mixed-disulfide intermediate between...
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11-17-2010 11:15 PM
[NMR paper] Dynamics of tryptophan binding to Escherichia coli Trp repressor wild type and AV77 m
Dynamics of tryptophan binding to Escherichia coli Trp repressor wild type and AV77 mutant: an NMR study.
Related Articles Dynamics of tryptophan binding to Escherichia coli Trp repressor wild type and AV77 mutant: an NMR study.
Biochemistry. 1995 Oct 10;34(40):13183-9
Authors: Schmitt TH, Zheng Z, Jardetzky O
Binding of L-tryptophan to Escherichia coli trp repressor wild type (WT) and AV77 mutant was studied by 1H NMR spectroscopy. Ligand binding to the proteins resulted in changes in line widths and chemical shifts of ligand resonances, but...
![[ASAP] Changes in Protein Dynamics in Escherichia coli SufS Reveal a Possible Conserved Regulatory Mechanism in Type II Cysteine Desulfurase Systems](http://www.bionmr.com/forum/iconimages/journal-club-9/%5Basap%5D-changes-protein-dynamics-escherichia-coli-sufs-reveal-possible-conserved-regulatory-mechanism-type-ii-cysteine-desulfurase-systems_ltr.gif)
[ASAP] Changes in Protein Dynamics in Escherichia coli SufS Reveal a Possible Conserved Regulatory Mechanism in Type II Cysteine Desulfurase Systems
Linear Mode
