Intramembrane proteolysis plays a fundamental role in many biological and pathological processes. Intramembrane proteases thus represent promising pharmacological targets, but few selective inhibitors have been identified. This is in contrast to their soluble counterparts, which are inhibited by many common drugs, and is in part explained by the inherent difficulty to characterize the binding of drug-like molecules to membrane proteins at atomic resolution. Here, we investigated the binding of...
[NMR paper] Structure and Dynamics of the Rhomboid Protease GlpG in Liposomes Studied by Solid-State NMR.
Structure and Dynamics of the Rhomboid Protease GlpG in Liposomes Studied by Solid-State NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles Structure and Dynamics of the Rhomboid Protease GlpG in Liposomes Studied by Solid-State NMR.
J Am Chem Soc. 2019 10 30;141(43):17314-17321
Authors: Shi C, Öster C, Bohg C, Li L, Lange S, Chevelkov V, Lange A
Abstract
Rhomboid proteases are intramembrane proteases that hydrolyze substrate peptide bonds within...
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[NMR paper] The Interaction of Fluorinated Glycomimetics with DC-SIGN: Multiple Binding Modes Disentangled by the Combination of NMR Methods and MD Simulations.
The Interaction of Fluorinated Glycomimetics with DC-SIGN: Multiple Binding Modes Disentangled by the Combination of NMR Methods and MD Simulations.
Related Articles The Interaction of Fluorinated Glycomimetics with DC-SIGN: Multiple Binding Modes Disentangled by the Combination of NMR Methods and MD Simulations.
Pharmaceuticals (Basel). 2020 Aug 04;13(8):
Authors: Martínez JD, Infantino AS, Valverde P, Diercks T, Delgado S, Reichardt NC, Ardá A, Cañada FJ, Oscarson S, Jiménez-Barbero J
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Fluorinated glycomimetics are...
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[ASAP] High-Affinity Binding of LDL Receptor-Related Protein 1 to Matrix Metalloprotease 1 Requires Protease:Inhibitor Complex Formation
High-Affinity Binding of LDL Receptor-Related Protein 1 to Matrix Metalloprotease 1 Requires Protease:Inhibitor Complex Formation
https://pubs.acs.org/na101/home/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.0c00442/20200806/images/medium/bi0c00442_0010.gif
Biochemistry
DOI: 10.1021/acs.biochem.0c00442
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[NMR paper] Escherichia coli topoisomerase IV E subunit and an inhibitor binding mode revealed by NMR spectroscopy.
Escherichia coli topoisomerase IV E subunit and an inhibitor binding mode revealed by NMR spectroscopy.
Escherichia coli topoisomerase IV E subunit and an inhibitor binding mode revealed by NMR spectroscopy.
J Biol Chem. 2016 Jun 30;
Authors: Li Y, Wong YL, Ng FM, Liu B, Wong YX, Poh ZY, Liu S, Then SW, Lee MY, Ng HQ, Huang Q, Hung AW, Cherian J, Hill J, Keller TH, Kang C
Abstract
Bacterial topoisomerases are attractive antibacterial drug targets due to their importance in bacterial growth and low homology with other human...
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[NMR paper] Probing the cation binding modes of macrocyclic HCV protease inhibitor BILN 2061 by multinuclear NMR.
Probing the cation binding modes of macrocyclic HCV protease inhibitor BILN 2061 by multinuclear NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Probing the cation binding modes of macrocyclic HCV protease inhibitor BILN 2061 by multinuclear NMR.
J Pharm Biomed Anal. 2012 Nov;70:609-13
Authors: Busacca CA, Jones PJ, Campbell SJ, Saha AK, Gonnella NC, Senanayake CH
Abstract
The ability of the macrocyclic HCV protease inhibitor BILN 2061 to bind different...
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Combined X-ray, NMR and kinetic analyses reveal uncommon binding characteristics of the HCV NS3-NS4A protease inhibitor BI 201335.
Combined X-ray, NMR and kinetic analyses reveal uncommon binding characteristics of the HCV NS3-NS4A protease inhibitor BI 201335.
Combined X-ray, NMR and kinetic analyses reveal uncommon binding characteristics of the HCV NS3-NS4A protease inhibitor BI 201335.
J Biol Chem. 2011 Jan 26;
Authors: Lemke CT, Goudreau N, Zhao S, Hucke O, Thibeault D, Llinás-Brunet M, White PW
Hepatitis C virus (HCV) infection, a major cause of liver disease world-wide, is curable but currently approved therapies have suboptimal efficacy. Supplementing these therapies...
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NMR Reveals a Different Mode of Binding of the Stam2 VHS Domain to Ubiquitin and Diubiquitin,
NMR Reveals a Different Mode of Binding of the Stam2 VHS Domain to Ubiquitin and Diubiquitin,
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/bi101594a/aop/images/medium/bi-2010-01594a_0006.gif
Biochemistry
DOI: 10.1021/bi101594a
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NMR reveals a different mode of binding of the Stam2 VHS domain to ubiquitin and diubiquitin.
NMR reveals a different mode of binding of the Stam2 VHS domain to ubiquitin and diubiquitin.
Related Articles NMR reveals a different mode of binding of the Stam2 VHS domain to ubiquitin and diubiquitin.
Biochemistry. 2010 Dec 1;
Authors: Lange A, Hoeller D, Wienk H, Marcillat O, Lancelin JM, Walker O
The VHS domain of the Stam2 protein is a ubiquitin binding domain involved in the recognition of ubiquitinated proteins committed to lysosomal degradation. Among all VHS domains, the VHS domain of Stam proteins is the strongest binder to...
A combination of solid-state NMR and MD simulations reveals the binding mode of a rhomboid protease inhibitor
Linear Mode
