Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Stephanie A Misquitta"'
Publikováno v:
Journal of Biological Chemistry. 283:32880-32888
Human glutathione transferase pi (GST pi) has been crystallized as a homodimer, with a subunit molecular mass of approximately 23 kDa; however, in solution the average molecular mass depends on protein concentration, approaching that of monomer at
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4588c254b6a530e6a5a76b57fab3b478
https://doi.org/10.1074/jbc.m805484200
https://doi.org/10.1074/jbc.m805484200
Publikováno v:
Biochemistry. 44:8608-8619
To study the communication between the two active sites of dimeric glutathione S-transferase A1-1, we used heterodimers containing one wild-type (WT) active site and one active site with a single mutation at either Tyr9, Arg15, or Arg131. Tyr9 and Ar
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::80865ae07d00eba37f6885d6a064b3cb
https://doi.org/10.1021/bi050449a
https://doi.org/10.1021/bi050449a
Publikováno v:
Protein Expression and Purification. 32:141-146
Human pituitary glutaminyl cyclase (hQC) was expressed in Drosophila S2 cells under the control of an inducible metallothionene promoter and fused to the Drosophila immunoglobulin-binding protein signal sequence to enable secretion into the culture m
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1a56f2d1369d309dadfda202aa4c495a
https://doi.org/10.1016/s1046-5928(03)00226-2
https://doi.org/10.1016/s1046-5928(03)00226-2
Publikováno v:
Biochemistry. 40:11246-11250
Glutaminyl cyclase (QC, EC 2.3.2.5) catalyzes the formation of the pyroglutamyl residue present at the amino terminus of numerous secretory peptides and proteins. Treatment with diethyl pyrocarbonate inactivated recombinant human QC with the apparent
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f44397da534e1c48893cb5fcfaee5bc5
https://doi.org/10.1021/bi011177o
https://doi.org/10.1021/bi011177o
Glutathione S-transferase pi has been shown to reactivate 1-cysteine peroxiredoxin (1-Cys Prx) by formation of a complex [L.A. Ralat, Y. Manevich, A.B. Fisher, R.F. Colman, Biochemistry 45 (2006) 360–372]. A model of the complex was proposed based
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::42bea1bc151f6cc9c1bffa202d56362b
https://europepmc.org/articles/PMC4939725/
https://europepmc.org/articles/PMC4939725/
Autor:
Stephanie A. Misquitta, Viktoria Hozjan, Xiaoqiu Wu, Udo Oppermann, Stuart Smith, Gabor Bunkoczi, Kathryn L. Kavanagh
Publikováno v:
The FASEB Journal. 22
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::05610d84e283fe9141cc8fd77d7f22fc
https://doi.org/10.1096/fasebj.22.1_supplement.1012.1
https://doi.org/10.1096/fasebj.22.1_supplement.1012.1
Autor:
Roberta F. Colman, Yefim Manevich, Luis A. Ralat, C. Lum Zony, Stephanie A. Misquitta, Aron B. Fisher
Publikováno v:
The FASEB Journal. 21
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::787b07f88c9fad28be5a401e29e825dd
https://doi.org/10.1096/fasebj.21.5.a644-a
https://doi.org/10.1096/fasebj.21.5.a644-a
Publikováno v:
BMC Biology, Vol 2, Iss 1, p 2 (2004)
BMC Biology
BMC Biology
Background Glutaminyl cyclase (QC) forms the pyroglutamyl residue at the amino terminus of numerous secretory peptides and proteins. We previously proposed the mammalian QC has some features in common with zinc aminopeptidases. We now have generated
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::22795a858f992abbb3aceb3ca984f4e1
https://doi.org/10.1186/1741-7007-2-2
https://doi.org/10.1186/1741-7007-2-2