Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Renata Filipek"'
Publikováno v:
Biochemistry. 47:4257-4265
The semisynthetic streptogramin antibiotic quinupristin/dalfopristin (trade name Synercid, Aventis Pharma) is a mixture of the A-type streptogramin dalfopristin and the B-type streptogramin quinupristin, a capped hexapeptide macrolactone. Quinupristi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d101257129b33249cdc8f85ba7fd8fa1
https://doi.org/10.1021/bi7015266
https://doi.org/10.1021/bi7015266
Publikováno v:
Molecular Microbiology. 57:605-610
Summary The genes encoding secreted, broad-spectrum activity cysteine proteases of Staphylococcus spp. (staphopains) and Streptococcus pyogenes (streptopain, SpeB) are genetically linked to genes encoding cytoplasmic inhibitors. While staphopain inhi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::868678b54e6b47dbb4ddcf227102e8cd
https://doi.org/10.1111/j.1365-2958.2005.04714.x
https://doi.org/10.1111/j.1365-2958.2005.04714.x
Publikováno v:
Journal of Biological Chemistry. 280:22006-22011
Protein ubiquitination requires the sequential activity of three enzymes: a ubiquitin-activating enzyme (E1), a ubiquitin-conjugating enzyme (E2), and a ubiquitin-ligase (E3). The ubiquitin-transfer machinery is hierarchically organized; for every ub
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a5118d99e5ccf56f301485a756bc8549
https://doi.org/10.1074/jbc.m502583200
https://doi.org/10.1074/jbc.m502583200
Publikováno v:
Biological Chemistry. 385:1059-1067
Staphylococcus aureus, a leading cause of bacterial infections in humans, is endowed with a wealth of virulence factors that contribute to the disease process. Several extracellular proteolytic enzymes, including cysteine proteinases referred to as t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::47039150aa8a2e13ef308ac767236945
https://doi.org/10.1515/bc.2004.137
https://doi.org/10.1515/bc.2004.137
Publikováno v:
Biochemistry. 43:14306-14315
Prostaphopain B is the precursor of staphopain B, a papain-type secreted cysteine protease from the pathogen Staphylococcus aureus. Here, we describe the 2.5 A crystal structure of the proenzyme. Its 21 kDa proregion is organized around a central hal
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::18a9a2b6c008fe037a250b69a0189284
https://doi.org/10.1021/bi048661m
https://doi.org/10.1021/bi048661m
Autor:
Matthias Bochtler, Aneta Oleksy, Renata Filipek, Malgorzata Rzychon, Jan Potempa, Milosz Gruca, Adam Dubin
Publikováno v:
Journal of Biological Chemistry. 278:40959-40966
Staphostatins are the endogenous inhibitors of the major secreted cysteine proteases of Staphylococcus aureus, the staphopains. Our recent crystal structure of staphostatin B has shown that this inhibitor forms a mixed, eight-stranded β-barrel with
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::bb7a734e9bba582ebecd0bd75d67fd0c
https://doi.org/10.1074/jbc.m302926200
https://doi.org/10.1074/jbc.m302926200
Publikováno v:
Molecular microbiology. 57(3)
The genes encoding secreted, broad-spectrum activity cysteine proteases of Staphylococcus spp. (staphopains) and Streptococcus pyogenes (streptopain, SpeB) are genetically linked to genes encoding cytoplasmic inhibitors. While staphopain inhibitors h
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::98cbd5cdac7b387ee4683ab72b4d59e4
https://pubmed.ncbi.nlm.nih.gov/16045606
https://pubmed.ncbi.nlm.nih.gov/16045606
Publikováno v:
The Journal of biological chemistry. 280(15)
Staphostatins are the endogenous, highly specific inhibitors of staphopains, the major secreted cysteine proteases from Staphylococcus aureus. We have previously shown that staphostatins A and B are competitive, active site-directed inhibitors that s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::94aa0afcbb2154001c95fa26c4bdb3e7
https://pubmed.ncbi.nlm.nih.gov/15644332
https://pubmed.ncbi.nlm.nih.gov/15644332
Autor:
Artur Sabat, Malgorzata Rzychon, Jan Potempa, Klaudia Kosowska, Renata Filipek, Matthias Bochtler, Adam Dubin
Staphostatins are the endogenous inhibitors of the major secreted cysteine proteases of Staphylococcus aureus, the staphopains. Here, we present the 1.4 A crystal structure of staphostatin B and show that the fold can be described as a fully closed,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ddadf0d697c838c1b5873c33780a6dfc
https://europepmc.org/articles/PMC2366914/
https://europepmc.org/articles/PMC2366914/
Autor:
Renata, Filipek, Malgorzata, Rzychon, Aneta, Oleksy, Milosz, Gruca, Adam, Dubin, Jan, Potempa, Matthias, Bochtler
Publikováno v:
The Journal of biological chemistry. 278(42)
Staphostatins are the endogenous inhibitors of the major secreted cysteine proteases of Staphylococcus aureus, the staphopains. Our recent crystal structure of staphostatin B has shown that this inhibitor forms a mixed, eight-stranded beta-barrel wit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::48769274c39f7f8e443955ac231a1735
https://pubmed.ncbi.nlm.nih.gov/12874290
https://pubmed.ncbi.nlm.nih.gov/12874290