Related ArticlesCorrection to: NMR structure of the HIV-1 reverse transcriptase thumb subdomain.
J Biomol NMR. 2017 Dec 12;:
Authors: Sharaf NG, Brereton AE, Byeon IL, Karplus PA, Gronenborn AM
Abstract
In the original publication of the article, the given name and family name of the author P. Andrew Karplus was published incorrectly. The name should read as "P. Andrew" - Given name and "Karplus" - Family name.
PMID: 29234947 [PubMed - as supplied by publisher]
Correction to: NMR structure of the HIV-1 reverse transcriptase thumb subdomain
Correction to: NMR structure of the HIV-1 reverse transcriptase thumb subdomain
Abstract
In the original publication of the article, the given name and family name of the author P. Andrew Karplus was published incorrectly. The name should read as "P. Andrew" â?? Given name and "Karplus" â?? Family name.
Source: Journal of Biomolecular NMR
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[NMR paper] NMR structure of the HIV-1 reverse transcriptase thumb subdomain.
NMR structure of the HIV-1 reverse transcriptase thumb subdomain.
Related Articles NMR structure of the HIV-1 reverse transcriptase thumb subdomain.
J Biomol NMR. 2016 Nov 17;
Authors: Sharaf NG, Brereton AE, Byeon IL, Andrew Karplus P, Gronenborn AM
Abstract
The solution NMR structure of the isolated thumb subdomain of HIV-1 reverse transcriptase (RT)*has been determined. A detailed comparison of the current structure with dozens of the highest resolution crystal structures of this domain in the context of the full-length enzyme...
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11-20-2016 09:20 PM
NMR structure of the HIV-1 reverse transcriptase thumb subdomain
NMR structure of the HIV-1 reverse transcriptase thumb subdomain
Abstract
The solution NMR structure of the isolated thumb subdomain of HIV-1 reverse transcriptase (RT)Â*has been determined. A detailed comparison of the current structure with dozens of the highest resolution crystal structures of this domain in the context of the full-length enzyme reveals that the overall structures are very similar, with only two regions exhibiting local conformational differences. The C-terminal capping pattern of the αH helix is subtly different, and the loop...
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11-19-2016 08:35 PM
[NMR paper] NMR characterization of HIV-1 reverse transcriptase binding to various non-nucleoside reverse transcriptase inhibitors with different activities.
NMR characterization of HIV-1 reverse transcriptase binding to various non-nucleoside reverse transcriptase inhibitors with different activities.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.nature.com-images-lo_npg.gif http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/https:--www.ncbi.nlm.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles NMR characterization of HIV-1 reverse transcriptase binding to various non-nucleoside reverse transcriptase inhibitors with different activities.
Sci Rep. 2015;5:15806
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09-24-2016 05:20 PM
[NMR paper] Conformational plasticity of the NNRTI-binding pocket in HIV-1 reverse transcriptase - A fluorine NMR study.
Conformational plasticity of the NNRTI-binding pocket in HIV-1 reverse transcriptase - A fluorine NMR study.
Related Articles Conformational plasticity of the NNRTI-binding pocket in HIV-1 reverse transcriptase - A fluorine NMR study.
Biochemistry. 2016 May 10;
Authors: Sharaf NG, Ishima R, Gronenborn AM
Abstract
HIV-1 reverse transcriptase (RT) is a major drug target in the treatment of HIV-1 infection. RT inhibitors currently in use include non-nucleoside, allosteric RT inhibitors (NNRTIs), which bind to a hydrophobic pocket,...
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05-11-2016 08:04 PM
[NMR paper] Application of Site-Specific Spin Labeling for NMR Detecting Inhibitor-Induced Conformational Change of HIV-1 Reverse Transcriptase.
Application of Site-Specific Spin Labeling for NMR Detecting Inhibitor-Induced Conformational Change of HIV-1 Reverse Transcriptase.
Related Articles Application of Site-Specific Spin Labeling for NMR Detecting Inhibitor-Induced Conformational Change of HIV-1 Reverse Transcriptase.
ChemMedChem. 2016 Jan 25;
Authors: Seetaha S, Yagi-Utsumi M, Yamaguchi T, Ishii K, Hannongbua S, Choowongkomon K, Kato K
Abstract
Paramagnetism-assisted nuclear magnetic resonance (NMR) techniques can provide long-range structural information...
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01-26-2016 03:40 PM
[NMR paper] NMR assignments of the N-terminal domain of Ogataea polymorpha telomerase reverse transcriptase.
NMR assignments of the N-terminal domain of Ogataea polymorpha telomerase reverse transcriptase.
Related Articles NMR assignments of the N-terminal domain of Ogataea polymorpha telomerase reverse transcriptase.
Biomol NMR Assign. 2015 Dec 31;
Authors: Polshakov VI, Petrova OA, Parfenova YY, Efimov SV, Klochkov VV, Zvereva MI, Dontsova OA
Abstract
Telomerase is a ribonucleoprotein enzyme that adds telomeric DNA fragments to the ends of chromosomes. This enzyme is the focus of substantial attention, both because its structure and...
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01-03-2016 01:25 AM
Correction for Li et al., Mechanism of E-cadherin dimerization probed by NMR relaxation dispersion [Correction]
Correction for Li et al., Mechanism of E-cadherin dimerization probed by NMR relaxation dispersion
...
Date: 2013-11-26
BIOPHYSICS AND COMPUTATIONAL BIOLOGY Correction for “Mechanism of E-cadherin dimerization probed by NMR relaxation dispersion,” by Ying Li, Nicole L. Altorelli, Fabiana Bahna, Barry Honig, Lawrence Shapiro, and Arthur G. Palmer III, which appeared in issue 41, October 8, 2013, of Proc Natl Acad Sci USA (110:16462–16467; first published September... Read More
PNAS:
Number: 48
Correction to: NMR structure of the HIV-1 reverse transcriptase thumb subdomain.
Linear Mode
