Zobrazeno 1 - 10
of 60
pro vyhledávání: '"R. Antony J. Warren"'
Publikováno v:
Journal of Proteome Research. 7:3282-3292
An activity-based isotope-coded affinity tagging (AB-ICAT) strategy for proteome-wide quantitation of active retaining endoglycosidases has been developed. Two pairs of biotinylated, cleavable, AB-ICAT reagents (light H(8) and heavy D(8)) have been s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::96164effbb02cfa59cc6e9dd84827c79
https://doi.org/10.1021/pr7008302
https://doi.org/10.1021/pr7008302
Autor:
Lindsay D. Eltis, R. Antony J. Warren, Omid Hekmat, Stephen G. Withers, Christine Florizone, Young-Wan Kim
Publikováno v:
ChemBioChem. 8:2125-2132
Functional proteomics methods are crucial for activity- and mechanism-based investigation of enzymes in biological systems at a post-translational stage. Glycosidases have central roles in cellular metabolism and its regulation, and their dysfunction
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2130e964667a5e2469522aff97a296ba
https://doi.org/10.1002/cbic.200700481
https://doi.org/10.1002/cbic.200700481
Publikováno v:
Angewandte Chemie. 118:2647-2650
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::06815ee0e337071de09751e034d69968
https://doi.org/10.1002/ange.200503900
https://doi.org/10.1002/ange.200503900
Autor:
Jiyoung Hwang, Johannes Müllegger, Hamzah Mohd. Salleh, R. Antony J. Warren, Stephen G. Withers, Stephen P. Reid, Wing Yiu Chan
Publikováno v:
Carbohydrate Research. 341:49-59
The putative β-glucuronidase from Thermotoga maritima , comprising 563 amino acid residues conjugated with a Hisx6 tag, was cloned and expressed in Escherichia coli . The enzyme has a moderately broad specificity, hydrolysing a range of p -nitrophen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::437a07b77a8a8491b3fce608a292d76e
https://doi.org/10.1016/j.carres.2005.10.005
https://doi.org/10.1016/j.carres.2005.10.005
Publikováno v:
Protein Engineering, Design and Selection. 18:497-501
A carbohydrate-binding module (CBM) was fused to the N-termini of mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase (EndoF1) and peptide N-glycosidase F (PNGaseF), two glycosidases from Chryseobacterium meningosepticum that are used to remove N
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::17d9ffc2132dacb9089aeee4b419e7e4
https://doi.org/10.1093/protein/gzi055
https://doi.org/10.1093/protein/gzi055
Publikováno v:
Journal of Biological Chemistry. 279:42787-42793
The Agrobacterium sp. beta-glucosidase (Abg) is a retaining beta-glycosidase and its nucleophile mutants, termed Abg glycosynthases, catalyze the formation of glycosidic bonds using alpha-glycosyl fluorides as donor sugars and various aryl glycosides
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6eb23fccb530e49a5e38bdad728b227a
https://doi.org/10.1074/jbc.m406890200
https://doi.org/10.1074/jbc.m406890200
Autor:
Stephen P. Reid, Stephen G. Withers, Dominik Stoll, Oyekanmi Nashiru, and R. Antony J. Warren, David L. Zechel
Publikováno v:
Biochemistry. 42:7195-7204
The chemical mechanism of a retaining beta-mannosidase from Cellulomonas fimi has been characterized through steady-state kinetic analyses with a range of substrates, coupled with chemical rescue studies on both the wild-type enzyme and mutants in wh
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::02058694df310b50192a694a6b9a81c8
https://doi.org/10.1021/bi034329j
https://doi.org/10.1021/bi034329j
Autor:
David R. Rose, Douglas G. Kilburn, R. Antony J. Warren, Gideon J. Davies, A.B. Boraston, V. Notenboom
Publikováno v:
Journal of Molecular Biology. 327:659-669
Carbohydrate-binding polypeptides, including carbohydrate-binding modules (CBMs) from polysaccharidases, and lectins, are widespread in nature. Whilst CBMs are classically considered distinct from lectins, in that they are found appended to polysacch
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8e17f287c18b427314ff8700f50ff3a5
https://doi.org/10.1016/s0022-2836(03)00152-9
https://doi.org/10.1016/s0022-2836(03)00152-9
Publikováno v:
Journal of Biological Chemistry. 278:6120-6127
Cellulase Cel5A from alkalophilic Bacillus sp. 1139 contains a family 17 carbohydrate-binding module (BspCBM17) and a family 28 CBM (BspCBM28) in tandem. The two modules have significantly similar amino acid sequences, but amino acid residues essenti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bad121ae46201aa5c240edbeea5bcf3f
https://doi.org/10.1074/jbc.m209554200
https://doi.org/10.1074/jbc.m209554200
Autor:
R. Antony J. Warren, M. Marta Guarna, Douglas G. Kilburn, Emily Kwan, Charles A. Haynes, Alisdair B. Boraston, Neil R. Gilkes
Publikováno v:
Biotechnology and Bioengineering. 79:724-732
In this work, a new derivative of FX was engineered. It comprises a cellulose-binding module (CBM) fused to the N-terminus of the truncated light chain (E2FX) of FX and a hexahistidine tag (H6) fused to the C-terminus of the heavy chain. The sequence
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::966b771364dab04c9a6953528f0eded6
https://doi.org/10.1002/bit.10312
https://doi.org/10.1002/bit.10312