Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Matthew G. Hicks"'
Autor:
Charlotte A. Green, Nitin S. Kamble, Elizabeth K. Court, Owain J. Bryant, Matthew G. Hicks, Christopher Lennon, Gillian M. Fraser, Phillip C. Wright, Graham P. Stafford
Publikováno v:
Microbial Cell Factories, Vol 18, Iss 1, Pp 1-17 (2019)
Abstract Background Many valuable biopharmaceutical and biotechnological proteins have been produced in Escherichia coli, however these proteins are almost exclusively localised in the cytoplasm or periplasm. This presents challenges for purification
Externí odkaz:
https://doaj.org/article/e452668ad75543f096a42f8f752f7056
Autor:
Christopher Lennon, Elizabeth K. Court, Nitin S. Kamble, Owain J. Bryant, Charlotte A. Green, Gillian M. Fraser, Phillip C. Wright, Matthew G. Hicks, Graham P. Stafford
Publikováno v:
Microbial Cell Factories, Vol 18, Iss 1, Pp 1-17 (2019)
Microbial Cell Factories
Microbial Cell Factories
Background Many valuable biopharmaceutical and biotechnological proteins have been produced in Escherichia coli, however these proteins are almost exclusively localised in the cytoplasm or periplasm. This presents challenges for purification, i.e. th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::623aa99a7161557f17f66565dc4667bb
https://www.repository.cam.ac.uk/handle/1810/288217
https://www.repository.cam.ac.uk/handle/1810/288217
Autor:
Peter Sander, Matthew G. Hicks, Juliane K. Brülle, Benjamin J. Thompson, Govind Chandra, David A. Widdick, Iain C. Sutcliffe, Matthew I. Hutchings, Andreas Tschumi, Tracy Palmer
Publikováno v:
Molecular Microbiology. 80:1395-1412
Following translocation, bacterial lipoproteins are lipidated by lipoprotein diacylglycerol transferase (Lgt) and cleaved of their signal peptides by lipoprotein signal peptidase (Lsp). In Gram-negative bacteria and mycobacteria, lipoproteins are fur
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ca832f5bf54115aa5e3a93b8048635c8
https://doi.org/10.1111/j.1365-2958.2011.07656.x
https://doi.org/10.1111/j.1365-2958.2011.07656.x
Autor:
David A, Widdick, Matthew G, Hicks, Benjamin J, Thompson, Andreas, Tschumi, Govind, Chandra, Iain C, Sutcliffe, Juliane K, Brülle, Peter, Sander, Tracy, Palmer, Matthew I, Hutchings
Publikováno v:
MOLECULAR MICROBIOLOGY
Following translocation, bacterial lipoproteins are lipidated by lipoprotein diacylglycerol transferase (Lgt) and cleaved of their signal peptides by lipoprotein signal peptidase (Lsp). In Gram-negative bacteria and mycobacteria, lipoproteins are fur
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::370d6b6f29b326d9a1b7b40f35d2ed3b
Wiley Online Library
Wiley Online Library
Publikováno v:
Journal of Bacteriology. 190:5127-5131
We have functionally produced the outer membrane cytochrome OmcA from Shewanella oneidensis in Escherichia coli . Substrate accessibility experiments indicate that OmcA is surface exposed in an E. coli B strain but not in a K-12 strain. We show that
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a9353bfcf44e8858d2d7bfc125ea5e88
https://doi.org/10.1128/jb.00395-08
https://doi.org/10.1128/jb.00395-08
Autor:
Grant Buchanan, Matthew G. Hicks, Ben C. Berks, Tracy Palmer, Ida Porcelli, Nicholas P. Greene, Sonya M. Schermann
Publikováno v:
Journal of Biological Chemistry. 282:23937-23945
The Tat (twin arginine translocation) system transports folded proteins across the bacterial cytoplasmic membrane and the thylakoid membrane of plant chloroplasts. The integral membrane proteins TatA, TatB, and TatC are essential components of the Ta
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d87e859f6003afd64d097e4807e95d91
https://doi.org/10.1074/jbc.m702972200
https://doi.org/10.1074/jbc.m702972200
Autor:
Matthew P. DeLisa, Adam C. Fisher, Angélique Chanal, Long-Fei Wu, Matthew G. Hicks, Claire-Lise Santini, Ritsdeliz Perez-Rodriguez, Jason D. Perlmutter, Tracy Palmer
Publikováno v:
Journal of Molecular Biology. 367:715-730
All secreted proteins in Escherichia coli must be maintained in an export-competent state before translocation across the inner membrane. In the case of the Sec pathway, this function is carried out by the dedicated SecB chaperone and the general cha
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b8bbcd0d2ff4b589b971c741e541ffad
https://doi.org/10.1016/j.jmb.2007.01.027
https://doi.org/10.1016/j.jmb.2007.01.027
Autor:
Iain C. Sutcliffe, Govind Chandra, Benjamin J. Thompson, David A. Widdick, Tracy Palmer, Matthew G. Hicks, Matthew I. Hutchings
Publikováno v:
Molecular Microbiology.
Lipoproteins are a distinct class of bacterial membrane proteins that are translocated across the cytoplasmic membrane primarily by the Sec general secretory pathway and then lipidated on a conserved cysteine by the enzyme lipoprotein diacylglycerol
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::68d4602e50c53c78e5c68b63287b1c49
https://doi.org/10.1111/j.1365-2958.2010.07261.x
https://doi.org/10.1111/j.1365-2958.2010.07261.x
Autor:
Benjamin J, Thompson, David A, Widdick, Matthew G, Hicks, Govind, Chandra, Iain C, Sutcliffe, Tracy, Palmer, Matthew I, Hutchings
Publikováno v:
Molecular microbiology. 77(4)
Lipoproteins are a distinct class of bacterial membrane proteins that are translocated across the cytoplasmic membrane primarily by the Sec general secretory pathway and then lipidated on a conserved cysteine by the enzyme lipoprotein diacylglycerol
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::e75ff3e6447509ff18416e46e91173fc
https://pubmed.ncbi.nlm.nih.gov/20572939
https://pubmed.ncbi.nlm.nih.gov/20572939
Autor:
Tracy Palmer, So Iwata, Juni Andréll, Megan J. Maher, Matthew G. Hicks, Elisabeth P. Carpenter
Publikováno v:
Biochemistry. 48(18)
The acid-induced arginine decarboxylase is part of an enzymatic system in Escherichia coli that contributes to making this organism acid resistant. The arginine decarboxylase is a vitamin B(6)-dependent enzyme that is active at acidic pH. It consumes
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2edbb489510fdd43691565160a03ca4e
https://pubmed.ncbi.nlm.nih.gov/19298070
https://pubmed.ncbi.nlm.nih.gov/19298070