Zobrazeno 1 - 10
of 155
pro vyhledávání: '"PA clan"'
Publikováno v:
Biomolecules, Vol 12, Iss 6, p 793 (2022)
A conserved, 26-residue sequence [AA(X2)[A/G][G/L](X2)GDV[I/L](X2)[V/L]NGE(X1)V(X6)] and corresponding structure repeating module were identified within the HtrA protease family using a non-redundant set (N = 20) of publicly available structures. Whi
Externí odkaz:
https://doaj.org/article/4f357178b60548e1956304812f4d1cdd
Akademický článek
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Publikováno v:
Europe PubMed Central
Chembiochem
Chembiochem
© 2015 The Authors. Published by Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim. Mutation of the tobacco etch virus (TEV) protease nucleophile from cysteine to serine causes an approximately 104-fold loss in activity. Ten rounds of directed evolution of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::afd2aa2c29b3f791b8d8d18a49672ea4
Autor:
Karen dos Santos Charret, Luiz Filipe Gonçalves de Oliveira, Carlos Roberto Alves, Raquel Aparecida Souza, Luzia Monteiro de Castro Côrtes, Laura Barral-Veloso, Matheus Pereira de Sá-Silva, Franklin Souza da Silva
Publikováno v:
Experimental Parasitology. 184:67-81
Serine proteases have significant functions over a broad range of relevant biological processes to the Leishmania spp lifecycle. Data gathered here present an update on the Leishmania spp serine proteases and the status of these enzymes as part of th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6b095276c8c3e8ca09629ef77706e584
https://doi.org/10.1016/j.exppara.2017.11.008
https://doi.org/10.1016/j.exppara.2017.11.008
Publikováno v:
PLoS ONE, Vol 14, Iss 5, p e0216659 (2019)
PLOS ONE
PLoS ONE
PLOS ONE
PLoS ONE
Specific cleavage of proteins by proteases is essential for several cellular, physiological, and viral processes. Chymotrypsin-related proteases that form the PA clan in the MEROPS classification of proteases is one of the largest and most diverse gr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ef2eea35095a4e6a7917f06a09f821e5
http://hdl.handle.net/10138/303451
http://hdl.handle.net/10138/303451
Publikováno v:
BMC Research Notes, Vol 5, Iss 1, p 256 (2012)
Abstract Background Serine proteases account for over a third of all known proteolytic enzymes; they are involved in a variety of physiological processes and are classified into clans sharing structural homology. The PA clan of endopeptidases is the
Externí odkaz:
https://doaj.org/article/30bd4a6379164590a4e060dff11ef3f0
Autor:
Sonali B. Rohamare, Prathit Chatterjee, Jayanta K. Pal, Varsha Bhavnani, Ranu Sharma, Sushama M. Gaikwad, D. Dafydd Jones
Publikováno v:
Process Biochemistry. 50:378-387
A serine protease (N. protease), from Nocardiopsis sp., was cloned and expressed in Escherichia coli and investigated for its potential kinetic stability. Protein expression using two vectors, pET-22b (+) and pET-39b (+) was compared based on proper
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4b5d6b25e594e445a8f6e4f008c70a3c
https://doi.org/10.1016/j.procbio.2014.12.025
https://doi.org/10.1016/j.procbio.2014.12.025
Autor:
Xiao-xia Liu, Zhiliang Ji, Yu Yongfei, Yuan Ma, Xiang Gao, Yin-Bo Li, Yufen Zhao, Yan Liu, Yan-Mei Li
Publikováno v:
Amino acids. 50(1)
Seryl-histidine dipeptide (Ser-His) has been recognized as the shortest peptide with hydrolysis cleavage activity; however, its protein cleavage spectrum has not yet been fully explored. Here, four differently folded proteins were treated with Ser-Hi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2d6beaa2fd33297efa75b31760c619f5
https://pubmed.ncbi.nlm.nih.gov/29071530
https://pubmed.ncbi.nlm.nih.gov/29071530
Publikováno v:
Journal of Biological Chemistry. 289:8288-8298
The chymotrypsin subfamily A of serine proteases consists primarily of eukaryotic proteases, including only a few proteases of bacterial origin. VesB, a newly identified serine protease that is secreted by the type II secretion system in Vibrio chole
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::321bfc4ce79263b2c4b039d8431be2d4
https://doi.org/10.1074/jbc.m113.525261
https://doi.org/10.1074/jbc.m113.525261
Publikováno v:
Volume: 38, Issue: 2 168-176
Turkish Journal of Biology
Turkish Journal of Biology
Deg5 and Deg8 are chloroplastic proteases found in Arabidopsis thaliana. These proteases participate in the repair of photosystem II. However, little information exists on the structures of Deg5 and Deg8. Here, the Deg5 and Deg8 structures were model
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9f973ba8cafb9879035ae7ea8701ca01
https://doi.org/10.3906/biy-1306-74
https://doi.org/10.3906/biy-1306-74