Many RNA-binding proteins undergo liquid-liquid phase separation, which underlies the formation of membraneless organelles, such as stress granules and P-bodies. Studies of the molecular mechanism of phase separation in vitro are hampered by the coalescence and sedimentation of organelle-sized droplets interacting with glass surfaces. Here, we demonstrate that liquid droplets of fused in sarcoma (FUS)-a protein found in cytoplasmic aggregates of amyotrophic lateral sclerosis and frontotemporal...
[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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08-07-2020 02:42 AM
[NMR paper] Assigned NMR backbone resonances of the ligand-binding region domain of the pneumococcal serine-rich repeat protein (PsrP-BR) reveal a rigid monomer in solution.
Assigned NMR backbone resonances of the ligand-binding region domain of the pneumococcal serine-rich repeat protein (PsrP-BR) reveal a rigid monomer in solution.
Related Articles Assigned NMR backbone resonances of the ligand-binding region domain of the pneumococcal serine-rich repeat protein (PsrP-BR) reveal a rigid monomer in solution.
Biomol NMR Assign. 2020 Apr 20;:
Authors: Schulte T, Sala BM, Nilvebrant J, Nygren PĆ, Achour A, Shernyukov A, Agback T, Agback P
Abstract
The pneumococcal serine rich repeat protein (PsrP) is...
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Solution Binding and Structural Analyses Reveal PotentialMultidrug Resistance Functions for SAV2435 and CTR107 and Other GyrI-likeProteins
Solution Binding and Structural Analyses Reveal PotentialMultidrug Resistance Functions for SAV2435 and CTR107 and Other GyrI-likeProteins
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.6b00651/20160817/images/medium/bi-2016-00651b_0012.gif
Biochemistry
DOI: 10.1021/acs.biochem.6b00651
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08-19-2016 04:05 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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NMR Study on the BZJunction Formation ofDNA Duplexes Induced by Z-DNA Binding Domain of Human ADAR1
NMR Study on the BZJunction Formation ofDNA Duplexes Induced by Z-DNA Binding Domain of Human ADAR1
Yeon-Mi Lee, Hee-Eun Kim, Chin-Ju Park, Ae-Ree Lee, Hee-Chul Ahn, Sung Jae Cho, Kwang-Ho Choi, Byong-Seok Choi and Joon-Hwa Lee
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja211581b/aop/images/medium/ja-2011-11581b_0005.gif
Journal of the American Chemical Society
DOI: 10.1021/ja211581b
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NMR Studies Reveal anUnexpected Binding Site for a Redox Inhibitor of AP Endonuclease 1
NMR Studies Reveal anUnexpected Binding Site for a Redox Inhibitor of AP Endonuclease 1
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/bi201071g/aop/images/medium/bi-2011-01071g_0007.gif
Biochemistry
DOI: 10.1021/bi201071g
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11-10-2011 07:38 AM
NMR, biophysical and biochemical studies reveal the minimal calmodulin-binding domain of the HIV-1 matrix protein.
NMR, biophysical and biochemical studies reveal the minimal calmodulin-binding domain of the HIV-1 matrix protein.
NMR, biophysical and biochemical studies reveal the minimal calmodulin-binding domain of the HIV-1 matrix protein.
J Biol Chem. 2011 Jul 28;
Authors: Samal AB, Ghanam RH, Fernandez TF, Monroe EB, Saad JS
Subcellular distribution of Calmodulin (CaM) in human immunodeficiency virus type-1 (HIV-1) infected cells is distinct from that observed in uninfected cells. CaM has been shown to interact and co-localize with the HIV-1 Gag protein...
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07-30-2011 11:23 AM
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...
NMR and EPR reveal a compaction of the RNA-binding protein FUS upon droplet formation
Linear Mode
