Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Alexandra, Males"'
Publikováno v:
Israel Journal of Chemistry. 63
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::dae0a56dd22110e0e4dc7db198251915
https://doi.org/10.1002/ijch.202200067
https://doi.org/10.1002/ijch.202200067
Publikováno v:
Current Opinion in Structural Biology. 62:79-92
Mannosidases are a diverse group of enzymes that are important in the biological processing of mannose-containing polysaccharides and complex glycoconjugates. They are found in 12 of the >160 sequence-based glycosidase families. We discuss evidence t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d03a8cf095e20d406d13774b7ece6349
https://doi.org/10.1016/j.sbi.2019.11.008
https://doi.org/10.1016/j.sbi.2019.11.008
Autor:
Manuel González-Cuesta, Peter Sidhu, Roger A. Ashmus, Alexandra Males, Cameron Proceviat, Zarina Madden, Jason C. Rogalski, Jil A. Busmann, Leonard J. Foster, José M. García Fernández, Gideon J. Davies, Carmen Ortiz Mellet, David J. Vocadlo
Publikováno v:
Journal of the American Chemical Society. 144(2)
Owing to its roles in human health and disease, the modification of nuclear, cytoplasmic, and mitochondrial proteins with O-linked
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a3658ecaf8f20742f6ee3479a34644cc
https://pubmed.ncbi.nlm.nih.gov/34985906
https://pubmed.ncbi.nlm.nih.gov/34985906
Publikováno v:
Current Opinion in Chemical Biology. 53:131-144
The post-translational modification of proteins by O-linked N-acetylglucosamine (O-GlcNAc) dynamically programmes cellular physiology to maintain homoeostasis and tailor biochemical pathways to meet context-dependent cellular needs. Despite diverse r
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::43ce24e3fc8d052a38b87ce6b4d6c4fd
https://doi.org/10.1016/j.cbpa.2019.09.001
https://doi.org/10.1016/j.cbpa.2019.09.001
Publikováno v:
Organic & Biomolecular Chemistry. 17:7863-7869
Enzyme transition-state mimics can act as powerful inhibitors and allow structural studies that report on the conformation of the transition-state. Here, mannoimidazole, a mimic of the transition state of mannosidase catalyzed hydrolysis of mannoside
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::eabb1c168482689405e2bce3d4d82f8b
https://doi.org/10.1039/c9ob01161g
https://doi.org/10.1039/c9ob01161g
Autor:
Gideon J. Davies, Casper de Boer, Herman S. Overkleeft, Wendy A. Offen, Jacopo Enotarpi, Gijsbert A. van der Marel, Jeroen D. C. Codée, Sybrin P. Schröder, Laura Marino, Bogdan I. Florea, Alexandra Males, Yi Jin
Publikováno v:
CHEM-EUR J, 27(37), 9519-9523. WILEY-V C H VERLAG GMBH
Schröder, S P, Offen, W A, Males, A, Jin, Y, Boer, C, Enotarpi, J, Marino, L, Marel, G A, Florea, B I, Codée, J D C, Overkleeft, H S & Davies, G J 2021, ' Development of Non-Hydrolysable Oligosaccharide Activity-Based Inactivators for Endoglycanases: A Case Study on alpha-1,6 Mannanases ', Chemistry – A European Journal, vol. 27, no. 37, pp. 9519-9523 . https://doi.org/10.1002/chem.202101255
Chemistry (Weinheim an Der Bergstrasse, Germany)
Schröder, S P, Offen, W A, Males, A, Jin, Y, Boer, C, Enotarpi, J, Marino, L, Marel, G A, Florea, B I, Codée, J D C, Overkleeft, H S & Davies, G J 2021, ' Development of Non-Hydrolysable Oligosaccharide Activity-Based Inactivators for Endoglycanases: A Case Study on alpha-1,6 Mannanases ', Chemistry – A European Journal, vol. 27, no. 37, pp. 9519-9523 . https://doi.org/10.1002/chem.202101255
Chemistry (Weinheim an Der Bergstrasse, Germany)
There is a vast genomic resource for enzymes active on carbohydrates. Lagging far behind, however, are functional chemical tools for the rapid characterization of carbohydrate‐active enzymes. Activity‐based probes (ABPs) offer one chemical soluti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::503a40aafc1803d748abf9432d41357f
http://hdl.handle.net/1887/3205317
http://hdl.handle.net/1887/3205317
Publikováno v:
Organicbiomolecular chemistry. 17(34)
Enzyme transition-state mimics can act as powerful inhibitors and allow structural studies that report on the conformation of the transition-state. Here, mannoimidazole, a mimic of the transition state of mannosidase catalyzed hydrolysis of mannoside
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::6410959c99e455f4268f9e8e74ce60d4
https://pubmed.ncbi.nlm.nih.gov/31407758
https://pubmed.ncbi.nlm.nih.gov/31407758
Autor:
Tom Ward, M. Fleur Sernee, Eric Hanssen, Lauren Stanton, Laurence M. Bastidas, Tracy L. Nero, Spencer J. Williams, Lukasz F. Sobala, Michael W. Parker, David B. Ascher, Phillip L. van der Peet, Julie E. Ralton, Gideon J. Davies, Malcolm J. McConville, Joachim Kloehn, Simon A. Cobbold, Alexandra Males, Douglas E. V. Pires, Marcel A. Vieira-Lara
Publikováno v:
Trends Parasitol
Parasitic protists belonging to the genus Leishmania synthesize the non-canonical carbohydrate reserve, mannogen, which is composed of β-1,2-mannan oligosaccharides. Here, we identify a class of dual-activity mannosyltransferase/phosphorylases (MTPs
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5f8fa59bb71685990c8526200dba1360
https://pubmed.ncbi.nlm.nih.gov/31662278
https://pubmed.ncbi.nlm.nih.gov/31662278
Autor:
Gideon J. Davies, Alexandra Males
Publikováno v:
Acta Crystallographica. Section D, Structural Biology
The surface-entropy reduction method has been used to generate new crystal forms of human O-GlcNAcase.
The enzyme O-GlcNAcase catalyses the removal of the O-GlcNAc co/post-translational modification in multicellular eukaryotes. The enzyme has be
The enzyme O-GlcNAcase catalyses the removal of the O-GlcNAc co/post-translational modification in multicellular eukaryotes. The enzyme has be
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fb4125b949b024a5589c60dcf28d5bba
https://eprints.whiterose.ac.uk/141443/1/jc5018.pdf
https://eprints.whiterose.ac.uk/141443/1/jc5018.pdf
Autor:
David B. Ascher, Malcolm J. McConville, Tom Ward, Lauren Stanton, Douglas E. V. Pires, Fleur Sernee, Eric Hanssen, Lukasz F. Sobala, Simon A. Cobbold, Marcel Viera-Lara, Spencer J. Williams, Michael W. Parker, Alexandra Males, Tracy L. Nero, Joachim Kloehn, Gideon J. Davies, Phillip L. van der Peet, Julie E. Ralton, Laurence M. Bastidas
Publikováno v:
SSRN Electronic Journal.
Leishmania are medically important protozoan parasites that have replaced canonical pathways of reserve carbohydrate biosynthesis with a new pathway for synthesis of β-1,2-mannan oligosaccharides, termed mannogen. Here we describe a new class of enz
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::990384f7c95c3d8cf1fa9c5fff32b279
https://doi.org/10.2139/ssrn.3382549
https://doi.org/10.2139/ssrn.3382549