Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Abdalin Asinas"'
Autor:
Abdalin Asinas, Usha Nair, Sirano Dhe-Paganon, Xianyang Fang, Abdellah Allali-Hassani, George V. Avvakumov, Xiaobing Zuo, John R. Walker, Yun-Xing Wang, Sheng Xue, Keith D. Wilkinson
Publikováno v:
Biochemistry
Human ubiquitin-specific cysteine protease 5 (USP5, also known as ISOT and isopeptidase T), an 835-residue multidomain enzyme, recycles ubiquitin by hydrolyzing isopeptide bonds in a variety of unanchored polyubiquitin substrates. Activation of the e
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::25c8f245869cbe08a412dc0a3c6787a9
https://doi.org/10.1021/bi200854q
https://doi.org/10.1021/bi200854q
Autor:
Christine Munger, Miroslaw Cygler, Rong Shi, R. Gary Sawers, Yunge Li, Svetlana Petkun, Linhua Zhang, Mandy Waclawek, Basem Soboh, Abdalin Asinas
Publikováno v:
Structure. 19:1773-1783
[NiFe]-hydrogenases are multimeric proteins. The large subunit contains the NiFe(CN) 2CO bimetallic active center and the small subunit contains Fe-S clusters. Biosynthesis and assembly of the NiFe(CN) 2CO active center requires six Hyp accessory pro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e4edddb294e400ffb2e8c5b1a06c8522
https://doi.org/10.1016/j.str.2011.09.023
https://doi.org/10.1016/j.str.2011.09.023
Autor:
Abdalin Asinas, Miroslaw Cygler, Robert J. Maier, Allan Matte, Stéphane L. Benoit, Erica F. Miller, Christine Munger, Rong Shi
Publikováno v:
Biochemistry. 49:7080-7088
The crystal structure of the urease maturation protein UreE from Helicobacter pylori has been determined in its apo form at 2.1 A resolution, bound to Cu(2+) at 2.7 A resolution, and bound to Ni(2+) at 3.1 A resolution. Apo UreE forms dimers, while t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d0853c540b96f10d36595de602f8ee91
https://doi.org/10.1021/bi100372h
https://doi.org/10.1021/bi100372h
Autor:
Allan Matte, Abdalin Asinas, Christine Munger, Erumbi S. Rangarajan, Pietro Iannuzzi, Miroslaw Cygler, Jason Baardsnes, A. Proteau
Hydrogenases are enzymes involved in hydrogen metabolism, utilizing H 2 as an electron source. [NiFe] hydrogenases are heterodimeric Fe-S proteins, with a large subunit containing the reaction center involving Fe and Ni metal ions and a small subunit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b3cbb588bdb81da848a9c1a4e6b5fd11
https://europepmc.org/articles/PMC2238214/
https://europepmc.org/articles/PMC2238214/
