Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Gunnar I, Berglund"'
Autor:
Richard Neutze, Gergely Katona, Janos Hajdu, Gunnar I. Berglund, Penny A. Wright, Christopher J. Schofield, Rupert C. Wilmouth
Kinetic analyses led to the discovery that N-acetylated tripeptides with polar residues at P3 are inhibitors of porcine pancreatic elastase (PPE) that form unusually stable acyl-enzyme complexes. Peptides terminating in a C-terminal carboxylate were
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1564e03e41ba36d6612815706f2a5fcd
https://doi.org/10.1074/jbc.m200676200
https://doi.org/10.1074/jbc.m200676200
Autor:
Gunnar I. Berglund, Sharon Wing Tak Ho, Sherry L. Mowbray, CM Tang, Wimal Ubhayasekera, Terese Bergfors, Mee-Len Chye
Publikováno v:
The FEBS Journal. 274:3695-3703
Brassica juncea chitinase is an endo-acting, pathogenesis-related protein that is classified into glycoside hydrolase family 19, with highest homology (50–60%) in its catalytic domain to class I plant chitinases. Here we report X-ray structures of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a0dc019204cdcf5a4953bb5bbeeb1f63
https://doi.org/10.1111/j.1742-4658.2007.05906.x
https://doi.org/10.1111/j.1742-4658.2007.05906.x
Publikováno v:
Biochemistry. 44(2)
Carbon monoxide, formate, and acetate interact with horseradish peroxidase (HRP) by binding to subsites within the active site. These ligands also bind to catalases, but their interactions are different in the two types of enzymes. Formate (notionall
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9eae8649d652c761704f077082c38530
https://pubmed.ncbi.nlm.nih.gov/15641789
https://pubmed.ncbi.nlm.nih.gov/15641789
Autor:
Jerry Ståhlberg, Tom Desmet, Andrew Shaw, Gunnar I. Berglund, Mats Sandgren, Lennart Kenne, Colin Mitchinson
Publikováno v:
Journal of molecular biology. 342(5)
As part of an ongoing enzyme discovery program to investigate the properties and catalytic mechanism of glycoside hydrolase family 12 (GH 12) endoglucanases, a GH family that contains several cellulases that are of interest in industrial applications
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0109a6fd6a85f49e0e4e8bfe0f00a8d8
https://pubmed.ncbi.nlm.nih.gov/15364577
https://pubmed.ncbi.nlm.nih.gov/15364577
Autor:
Colin Mitchinson, Andrew Shaw, Mats Sandgren, Gunnar I. Berglund, Mae Saldajeno, Sigrid Paech, Laurie S. Gross, Peter Gualfetti, Christian Paech, T. Alwyn Jones
As part of a program to discover improved glycoside hydrolase family 12 (GH 12) endoglucanases, we have extended our previous work on the structural and biochemical diversity of GH 12 homologs to include the most stable fungal GH 12 found, Humicola g
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::24b92b89ae1a87a311788e46ed05df81
https://europepmc.org/articles/PMC2366986/
https://europepmc.org/articles/PMC2366986/
Publikováno v:
Methods in enzymology. 353
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::ddef99486fe431fff457a237386ea438
https://pubmed.ncbi.nlm.nih.gov/12078505
https://pubmed.ncbi.nlm.nih.gov/12078505
Publikováno v:
Journal of molecular biology. 315(5)
Severe neurodegradative brain diseases, like Alzheimer, are tightly linked with proteolytic activity in the human brain. Proteinases expressed in the brain, such as human trypsin IV, are likely to be involved in the pathomechanism of these diseases.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fbe7f5be74e2a64e6a354db757175783
https://pubmed.ncbi.nlm.nih.gov/11827488
https://pubmed.ncbi.nlm.nih.gov/11827488
The four-electron reduction of dioxygen to water is the most exothermic non-photochemical reaction available to biology. A detailed molecular description of this reaction is needed to understand oxygen-based redox processes. Horseradish peroxidase (H
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::247b407e1074a93d8a1767438513473a
https://doi.org/10.1016/s0076-6879(02)53057-3
https://doi.org/10.1016/s0076-6879(02)53057-3