Zobrazeno 1 - 10
of 16
pro vyhledávání: '"Keya Zhang"'
Autor:
Bo Zhao, Keya Zhang, Karan Bhuripanyo, Chan Hee J Choi, Eric B Villhauer, Heng Li, Ning Zheng, Hiroaki Kiyokawa, Hermann Schindelin, Jun Yin
Publikováno v:
PLoS ONE, Vol 8, Iss 8, p e70312 (2013)
The C-terminal peptides of ubiquitin (UB) and UB-like proteins (UBLs) play a key role in their recognition by the specific activating enzymes (E1s) to launch their transfer through the respective enzymatic cascades thus modifying cellular proteins. U
Externí odkaz:
https://doaj.org/article/e98b3b659bb94f6f8d0f1bfa4bcaac2d
Autor:
Helong Hao, Frits Goedegebuur, Zhenghong Zhang, Keya Zhang, Xiaogang Gu, Lilia Maria Babe, Zhiyong Xie, Zhengzheng Zou, Zhongmei Tang
Publikováno v:
Journal of Microbiology and Biotechnology. 25:1281-1290
Thermolysin and its homologs are a group of metalloproteases that have been widely used in both therapeutic and biotechnological applications. We here report the identification and characterization of a novel thermolysin-like protease, BtsTLP1, from
Publikováno v:
ChemBioChem. 14:426-430
The β-propeller fold is a widespread structural module responsible for specific protein-protein interactions in the cell. [1] Typically β-propellers consist of four to eight blades that are made of antiparallel β-sheets twisting around a central t
Autor:
Karan Bhuripanyo, Hermann Schindelin, Bo Zhao, David L. Boone, Jun Yin, Keya Zhang, Jeffrey R. Schneider
Publikováno v:
ACS Chemical Biology. 7:2027-2035
Ubiquitin (UB) is a protein modifier that regulates many essential cellular processes. To initiate protein modification by UB, the E1 enzyme activates the C-terminal carboxylate of UB to launch its transfer through the E1-E2-E3 cascade onto target pr
Publikováno v:
Chemistry & Biology. 19:1265-1277
SummaryProtein modification by ubiquitin (UB) controls diverse cellular processes. UB is conjugated to cellular proteins by sequential transfer through an E1-E2-E3 enzymatic cascade. The cross-activities of 2 E1s, 50 E2s and thousands of E3s encoded
Publikováno v:
ChemBioChem. 10:2599-2606
Publikováno v:
Methods in Molecular Biology ISBN: 9781493927470
We find yeast cell surface display can be used to engineer enzymes by selecting the enzyme library for high affinity binding to reaction intermediates. Here we cover key steps of enzyme engineering on the yeast cell surface including library design,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::da2983a20fdef97b29a49e4d762c5fca
https://europepmc.org/articles/PMC4648535/
https://europepmc.org/articles/PMC4648535/
Publikováno v:
Site-Specific Protein Labeling ISBN: 9781493922710
Phosphopantetheinyl transferases (PPTase) Sfp and AcpS catalyze a highly efficient reaction that conjugates chemical probes of diverse structures to proteins. PPTases have been widely used for site-specific protein labeling and live cell imaging of t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bd87579880d1bc66d4cdf65cfc6d4906
https://doi.org/10.1007/978-1-4939-2272-7_11
https://doi.org/10.1007/978-1-4939-2272-7_11
Autor:
Jun Yin, Hermann Schindelin, Eric B. Villhauer, Keya Zhang, Hiroaki Kiyokawa, Karan Bhuripanyo, Ning Zheng, Heng Li, Chan Hee J. Choi, Bo Zhao
Publikováno v:
PLoS ONE, Vol 8, Iss 8, p e70312 (2013)
PLoS ONE
PLoS ONE
The C-terminal peptides of ubiquitin (UB) and UB-like proteins (UBLs) play a key role in their recognition by the specific activating enzymes (E1s) to launch their transfer through the respective enzymatic cascades thus modifying cellular proteins. U
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ba66079cd34e8ca6b07ea42ab3a73f1f
https://opus.bibliothek.uni-wuerzburg.de/files/12847/077_Zhao_Plos_One.pdf
https://opus.bibliothek.uni-wuerzburg.de/files/12847/077_Zhao_Plos_One.pdf
Publikováno v:
Methods in enzymology. 458
Phosphopantetheinyl transferases (PPTases) covalently attach the phosphopantetheinyl group derived from coenzyme A (CoA) to acyl carrier proteins or peptidyl carrier proteins as part of the enzymatic assembly lines of fatty acid synthases (FAS), poly