[ASAP] Dimerization of Human Drebrin-like Protein Governs Its Biological Activity
Dimerization of Human Drebrin-like Protein Governs Its Biological Activity
https://pubs.acs.org/na101/home/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.9b01095/20200417/images/medium/bi9b01095_0005.gif
Biochemistry
DOI: 10.1021/acs.biochem.9b01095
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nmrlearner
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04-20-2020 05:10 PM
[ASAP] Hinge-Type Dimerization of Proteins by a Tetracysteine Peptide of High Pairing Specificity
Hinge-Type Dimerization of Proteins by a Tetracysteine Peptide of High Pairing Specificity
https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.8b00475/20180614/images/medium/bi-2018-00475f_0006.gif
Biochemistry
DOI: 10.1021/acs.biochem.8b00475
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http://feeds.feedburner.com/~r/acs/bichaw/~4/WiUDl3gyVOs
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nmrlearner
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06-15-2018 04:21 AM
[ASAP] Cyanylated Cysteine Reports Site-Specific Changes at Protein–Protein-Binding Interfaces Without Perturbation
Cyanylated Cysteine Reports Site-Specific Changes at Protein–Protein-Binding Interfaces Without Perturbation
https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.8b00283/20180605/images/medium/bi-2018-00283c_0004.gif
Biochemistry
DOI: 10.1021/acs.biochem.8b00283
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06-11-2018 07:38 PM
[ASAP] Lysine Side-Chain Dynamics in the Binding Site of Homeodomain/DNA Complexes As Observed by NMR Relaxation Experiments and Molecular Dynamics Simulations
Lysine Side-Chain Dynamics in the Binding Site of Homeodomain/DNA Complexes As Observed by NMR Relaxation Experiments and Molecular Dynamics Simulations
https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.8b00195/20180430/images/medium/bi-2018-001959_0008.gif
Biochemistry
DOI: 10.1021/acs.biochem.8b00195
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http://feeds.feedburner.com/~r/acs/bichaw/~4/609FbT_MCUM
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05-01-2018 10:57 PM
[ASAP] Extratelomeric Binding of the Telomere Binding Protein TRF2 at the PCGF3 Promoter Is G-Quadruplex Motif-Dependent
Extratelomeric Binding of the Telomere Binding Protein TRF2 at the PCGF3 Promoter Is G-Quadruplex Motif-Dependent
https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.8b00019/20180410/images/medium/bi-2018-00019w_0005.gif
Biochemistry
DOI: 10.1021/acs.biochem.8b00019
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http://feeds.feedburner.com/~r/acs/bichaw/~4/kty9sAc251I
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nmrlearner
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04-12-2018 01:01 AM
Sequential DNA Binding and Dimerization Processesof the Photosensory Protein EL222
Sequential DNA Binding and Dimerization Processesof the Photosensory Protein EL222
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.7b01206/20180219/images/medium/bi-2017-01206b_0009.gif
Biochemistry
DOI: 10.1021/acs.biochem.7b01206
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http://feeds.feedburner.com/~r/acs/bichaw/~4/BCK4ZL28R1Q
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nmrlearner
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02-21-2018 12:45 AM
[NMR paper] NMR investigation of main-chain dynamics of the H80E mutant of bovine neurophysin-I: demonstration of dimerization-induced changes at the hormone-binding site.
NMR investigation of main-chain dynamics of the H80E mutant of bovine neurophysin-I: demonstration of dimerization-induced changes at the hormone-binding site.
Related Articles NMR investigation of main-chain dynamics of the H80E mutant of bovine neurophysin-I: demonstration of dimerization-induced changes at the hormone-binding site.
Biochemistry. 2005 Sep 6;44(35):11766-76
Authors: Naik MT, Lee H, Bracken C, Breslow E
Neurophysins are hormone-binding proteins composed of two partially homologous domains. Ligand-binding (localized to the...
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12-01-2010 06:56 PM
[NMR paper] NMR analysis of intra- and inter-molecular stems in the dimerization initiation site
NMR analysis of intra- and inter-molecular stems in the dimerization initiation site of the HIV-1 genome.
Related Articles NMR analysis of intra- and inter-molecular stems in the dimerization initiation site of the HIV-1 genome.
J Biochem. 2000 Apr;127(4):681-6
Authors: Takahashi K, Baba S, Hayashi Y, Koyanagi Y, Yamamoto N, Takaku H, Kawai G
Two positive-strand HIV-1 genomic RNAs form a dimer in virion particles through interaction of the dimerization initiation sites (DIS). The DIS RNA fragment spontaneously formed a "loose-dimer" and was...