[ASAP] Overcharging of the Zinc Ion in the Structure of the Zinc-Finger Protein Is Needed for DNA Binding Stability
Overcharging of the Zinc Ion in the Structure of the Zinc-Finger Protein Is Needed for DNA Binding Stability
https://pubs.acs.org/na101/home/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.9b01055/20200220/images/medium/bi9b01055_0010.gif
Biochemistry
DOI: 10.1021/acs.biochem.9b01055
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02-29-2020 09:52 PM
[ASAP] Identifying the Protein Interactions of the Cytosolic Iron–Sulfur Cluster Targeting Complex Essential for Its Assembly and Recognition of Apo-Targets
Identifying the Protein Interactions of the Cytosolic Iron–Sulfur Cluster Targeting Complex Essential for Its Assembly and Recognition of Apo-Targets
https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.7b00072/20180409/images/medium/bi-2017-00072x_0007.gif
Biochemistry
DOI: 10.1021/acs.biochem.7b00072
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04-10-2018 12:35 AM
[ASAP] CH···O Hydrogen Bonds Mediate Highly Specific Recognition of Methylated CpG Sites by the Zinc Finger Protein Kaiso
CH···O Hydrogen Bonds Mediate Highly Specific Recognition of Methylated CpG Sites by the Zinc Finger Protein Kaiso
https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.8b00065/20180326/images/medium/bi-2018-000652_0009.gif
Biochemistry
DOI: 10.1021/acs.biochem.8b00065
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03-27-2018 06:28 AM
[NMR paper] Paramagnetic Properties of a Crystalline Iron-Sulfur Protein by Magic-Angle Spinning NMR Spectroscopy.
Paramagnetic Properties of a Crystalline Iron-Sulfur Protein by Magic-Angle Spinning NMR Spectroscopy.
Related Articles Paramagnetic Properties of a Crystalline Iron-Sulfur Protein by Magic-Angle Spinning NMR Spectroscopy.
Inorg Chem. 2017 May 24;
Authors: Bertarello A, Schubeis T, Fuccio C, Ravera E, Fragai M, Parigi G, Emsley L, Pintacuda G, Luchinat C
Abstract
We present the first solid-state NMR study of an iron-sulfur protein. The combined use of very fast (60 kHz) magic-angle spinning and tailored radiofrequency irradiation...
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05-26-2017 08:36 PM
[NMR paper] Solution structure of an archaeal DNA binding protein with an eukaryotic zinc finger fold.
Solution structure of an archaeal DNA binding protein with an eukaryotic zinc finger fold.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.plosone.org-images-pone_120x30.png http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Solution structure of an archaeal DNA binding protein with an eukaryotic zinc finger fold.
PLoS One. 2013;8(1):e52908
Authors: Guillière F, Danioux C, Jaubert C, Desnoues N, Delepierre M, Prangishvili D, Sezonov G, Guijarro JI
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02-03-2013 10:19 AM
[NMR paper] Solution NMR structure of the iron-sulfur cluster assembly protein U (IscU) with zinc
Solution NMR structure of the iron-sulfur cluster assembly protein U (IscU) with zinc bound at the active site.
Related Articles Solution NMR structure of the iron-sulfur cluster assembly protein U (IscU) with zinc bound at the active site.
J Mol Biol. 2004 Nov 19;344(2):567-83
Authors: Ramelot TA, Cort JR, Goldsmith-Fischman S, Kornhaber GJ, Xiao R, Shastry R, Acton TB, Honig B, Montelione GT, Kennedy MA
IscU is a highly conserved protein that serves as the scaffold for IscS-mediated assembly of iron-sulfur () clusters. We report the NMR...
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11-24-2010 10:03 PM
[NMR paper] NMR chemical shift perturbation mapping of DNA binding by a zinc-finger domain from t
NMR chemical shift perturbation mapping of DNA binding by a zinc-finger domain from the yeast transcription factor ADR1.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles NMR chemical shift perturbation mapping of DNA binding by a zinc-finger domain from the yeast transcription factor ADR1.
Protein Sci. 1997 Sep;6(9):1835-48
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08-22-2010 05:08 PM
[NMR paper] Zinc- and sequence-dependent binding to nucleic acids by the N-terminal zinc finger o
Zinc- and sequence-dependent binding to nucleic acids by the N-terminal zinc finger of the HIV-1 nucleocapsid protein: NMR structure of the complex with the Psi-site analog, dACGCC.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Zinc- and sequence-dependent binding to nucleic acids by the N-terminal zinc finger of the HIV-1 nucleocapsid protein: NMR...