Zobrazeno 1 - 10 of 26 pro vyhledávání: '"van Jan Maarten Dijl"'
1
Potential antibiotic and anti-infective effects of rhodomyrtone from Rhodomyrtus tomentosa (Aiton) Hassk. on Streptococcus pyogenes as revealed by proteomics
Autor: Supayang Piyawan Voravuthikunchai, Oliver Kayser, Annie Hesseling-Meinders, van Jan Maarten Dijl, Surasak Limsuwan
Publikováno v: Phytomedicine, 18(11), 934-940
Rhodomyrtone from Rhodomyrtus tomentosa (Aiton) Hassk. leaf extract has a strong antibacterial activity against the bacterial pathogen Streptococcus pyogenes. Our previous studies indicated that the bactericidal activity of rhodomyrtone might involve
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1c2677443e5b56257cee2f10b1d010d6
https://doi.org/10.1016/j.phymed.2011.02.007
Zobrazit plný text záznamu
2
The Bacillus secretion stress response is an indicator for alpha-amylase production levels
Autor: Helga Westers, Oscar P. Kuipers, Geeske Zanen, van Jan Maarten Dijl, Wim J. Quax, Sierd Bron, Elise Darmon, Jan-Willem Veening
Publikováno v: Letters in Applied Microbiology, 39(1), 65-73. WILEY-BLACKWELL
H. W ESTERS, E . D ARMON, G . Z ANEN, J .-W. V EENING, O .P. K UIPERS, S . B RON, W .J. Q UAX A N D J . M . V A N D I J L . 2004. Aims: Overproduced a-amylases in Bacillus subtilis provoke a specific stress response involving the CssRS twocomponent s
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2ffcfd6a0a9928901b91b69821a4566b
https://doi.org/10.1111/j.1472-765x.2004.01539.x
Zobrazit plný text záznamu
3
Proteomics of protein secretion by Bacillus subtilis: separating the 'secrets' of the secretome
Autor: Geeske Zanen, Peter Braun, Ronald Dorenbos, Michael Hecker, Jean-Yves F. Dubois, Haike Antelmann, S Bron, Wim J. Quax, Elise Darmon, Helga Westers, Jan D. H. Jongbloed, Harold Tjalsma, Oscar P. Kuipers, van Jan Maarten Dijl
Publikováno v: Microbiology and Molecular Biology Reviews, 68, 2, pp. 207-33
Microbiology and Molecular Biology Reviews, 68, 207-33
Microbiology and Molecular Biology Reviews, 68(2), 207-233. AMER SOC MICROBIOLOGY
SUMMARY Secretory proteins perform a variety of important“ remote-control” functions for bacterial survival in the environment. The availability of complete genome sequences has allowed us to make predictions about the composition of bacterial ma
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cb3f3dbb212525795b88a73e544a4fc1
https://hdl.handle.net/2066/58005
Zobrazit plný text záznamu
4
A Truncated Soluble Bacillus Signal Peptidase Produced in Escherichia coli Is Subject to Self-Cleavage at Its Active Site
Autor: Anneke Kuipers, Jan D. H. Jongbloed, Sierd Bron, ML van Roosmalen, van Jan Maarten Dijl, Gerhardus Venema
Publikováno v: Journal of Bacteriology. 182:5765-5770
Soluble forms of Bacillus signal peptidases which lack their unique amino-terminal membrane anchor are prone to degradation, which precludes their high-level production in the cytoplasm of Escherichia coli. Here, we show that the degradation of solub
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bb68922adebecdce4f1597e6eab24db2
https://doi.org/10.1128/jb.182.20.5765-5770.2000
Zobrazit plný text záznamu
5
Chaperone-like activities of the CsaA protein of Bacillus subtilis
Autor: Jörg P. Müller, Sierd Bron, Gerhardus Venema, van Jan Maarten Dijl
Publikováno v: Microbiology-Reading, 146, 77-88. AMER SOC MICROBIOLOGY
The growth and protein export defects of Escherichia coli secA51(Ts) strains can be suppressed by the CsaA protein of Bacillus subtilis. The present studies indicate that this effect can be attributed to chaperone-like activities of CsaA. First. CsaA
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8fd1a47ac99a024407e1cd363f485a0b
https://doi.org/10.1099/00221287-146-1-77
Zobrazit plný text záznamu
6
The Potential Active Site of the Lipoprotein-specific (Type II) Signal Peptidase of Bacillus subtilis
Autor: Geeske Zanen, Sierd Bron, Gerhardus Venema, van Jan Maarten Dijl, H Tjalsma
Publikováno v: The Journal of Biological Chemistry, 274(40), 28191-28197. AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
Type II signal peptidases (SPase II) remove signal peptides from lipid-modified preproteins of eubacteria. As the catalytic mechanism employed by type II SPases was not known, the present studies were aimed at the identification of their potential ac
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f75e4137b1beda1f12a6709e08c2c268
https://doi.org/10.1074/jbc.274.40.28191
Zobrazit plný text záznamu
7
The Plasmid-Encoded Signal Peptidase SipP Can Functionally Replace the Major Signal Peptidases SipS and SipT of Bacillus subtilis
Autor: van Jan Maarten Dijl, J van den Dolder, Gerhardus Venema, H Tjalsma, Sierd Bron, Wilfried J. J. Meijer
Publikováno v: Journal of Bacteriology, 181(8), 2448-2454. AMER SOC MICROBIOLOGY
The gram-positive eubacterium Bacillus subtilis is the organism with the largest number of paralogous type I signal peptidases (SPases) known. These are specified both by chromosomal and plasmid-borne genes. The chromosomally encoded SPases SipS and
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f0af77b16dd27a67b23ecbfa9d7e1b96
https://doi.org/10.1128/jb.181.8.2448-2454.1999
Zobrazit plný text záznamu
8
Protein secretion and possible roles for multiple signal peptidases for precursor processing in Bacilli
Autor: Harold Tjalsma, van Jan Maarten Dijl, Albert Bolhuis, Siger Holsappel, Sierd Bron, Gerhardus Venema
Publikováno v: Journal of Biotechnology. 64:3-13
Bacillus subtilis is one of the best known Gram-positive bacteria at both the genetic and physiological level. The entire sequence of its chromosome is known and efficient tools for the genetic modification of this bacterium are available. Moreover,
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::88848e8f241a4e72b26755444a055a4c
https://doi.org/10.1016/s0168-1656(98)00099-6
Zobrazit plný text záznamu
9
TheSip(Sli)Gene ofStreptomyces LividansTK24 Specifies an Unusual Signal Peptidase with a Putative C-Terminal Transmembrane Anchor
Autor: S Schacht, van Jan Maarten Dijl, Sierd Bron, Jozef Anné, Harold Tjalsma, L. Van Mellaert, Elke Lammertyn
Publikováno v: DNA Sequence. 9:79-88
Type I signal peptidases (SPases) are a widespread family of enzymes which remove signal peptides from proteins translocated across cellular membranes. Here, we report the first isolation of a gene coding for type I signal peptidase of Streptomyces,
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c6c67f20e2da3d8dae53cfd067cb0fed
https://doi.org/10.3109/10425179809086432
Zobrazit plný text záznamu
10
The chemistry and enzymology of the type I signal peptidases
Autor: MO Lively, Sierd Bron, Ross E. Dalbey, van Jan Maarten Dijl
Publikováno v: Protein Science. 6:1129-1138
The discovery that proteins exported from the cytoplasm are typically synthesized as larger precursors with cleavable signal peptides has focused interest on the peptidases that remove the signal peptides. Here, we review the membrane-bound peptidase
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::b0fc3da4ff8a2215e5345bdc033dddff
https://doi.org/10.1002/pro.5560060601
Zobrazit plný text záznamu

Vyhledávací nástroje:

Upřesnit hledání

Omezení vyhledávání
Plný text Recenzováno Digitální knihovna AV ČR
Zdroje