Minimal motif peptide structure of metzincin clan zinc peptidases in micelles-Reference-Cited by-同舟云学术

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Minimal motif peptide structure of metzincin clan zinc peptidases in micelles

Published:2009-10-14 Issue:12 Volume:15 Page:832-841
ISSN:1075-2617
Container-title:Journal of Peptide Science
language:en
Short-container-title:J. Peptide Sci.

Author:

Onoda Akira,Suzuki Takako,Ishizuka Hiroaki,Sugiyama Rumiko,Ariyasu Shinya,Yamamura Takeshi

Funder

Ministry of Education, Culture, Sports, Science, and Technology (MEXT) of the Japanese Government

Publisher

Wiley

Subject

Organic Chemistry,Drug Discovery,Pharmacology,Molecular Biology,Molecular Medicine,General Medicine,Biochemistry,Structural Biology

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1002/psc.1184/fullpdf

Reference35 articles.

1. Positive shift of redox potential of [F4S4(Z-cys-Gly-Ala-OMe)4]2- in Dichloromethane;Ueyama;J. Am. Chem. Soc.,1986

2. Conformation control of peptides by metal ions. Coordination conformation correlation observed in a model for Cys-X-Y-Cys/M2+ in Proteins;Yamamura;Inorg. Chem.,1997

3. A 2.2 A resolution crystal structure of a designed zinc finger protein bound to DNA;Kim;Nature Struct. Biol.,1996

4. Metal ion affinities of the zinc finger domains of the metal responsive element-binding transcription factor-1 (MTF-1);Guerrerio;Biochemistry,2004

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2. Two-step functional screen on multiple proteinaceous substrates reveals temperature-robust proteases with a broad-substrate range;Applied Microbiology and Biotechnology;2021-03-26

3. Zn(II) and Ni(II) complexes with poly-histidyl peptides derived from a snake venom;Inorganica Chimica Acta;2018-03

4. The unusual binding mechanism of Cu(ii) ions to the poly-histidyl domain of a peptide found in the venom of an African viper;Dalton Trans.;2014-09-10

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