Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Lucy Vandeputte-Rutten"'
Autor:
Piet Gros, Lucy Vandeputte-Rutten
Publikováno v:
Current Opinion in Structural Biology. 12:704-708
Proteases perform a wide variety of functions, inside and outside cells, regulating many biological processes. Recent years have witnessed a number of significant advances in the structural biology of proteases, including aspects of intracellular pro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::47dfc80d05e726690e81afcf7d2f0387
https://doi.org/10.1016/s0959-440x(02)00393-7
https://doi.org/10.1016/s0959-440x(02)00393-7
Autor:
Klaus Brandenburg, Niek Dekker, R.Arjen Kramer, Marjolein Werkhoven, Piet Gros, Maarten R. Egmond, Lucy Vandeputte-Rutten
Publikováno v:
European Journal of Biochemistry. 269:1746-1752
OmpT is an integral outer membrane protease of Escherichia coli. Overexpression of OmpT in E. coli and subsequent in vitro folding of the produced inclusion bodies yielded protein with a native-like structure. However, enzymatically active protease w
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b937a9eb5dcad6f8968dcc1c5453a74d
https://doi.org/10.1046/j.1432-1327.2002.02820.x
https://doi.org/10.1046/j.1432-1327.2002.02820.x
Publikováno v:
EMBO Journal, 20(18), 5033. European Molecular Biology Organization
OmpT from Escherichia coli belongs to a family of highly homologous outer membrane proteases, known as omptins, which are implicated in the virulence of several pathogenic Gram-negative bacteria. Here we present the crystal structure of OmpT, which s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::25b1e4d5f20963fcb14eed6f6409659c
https://doi.org/10.1093/emboj/20.18.5033
https://doi.org/10.1093/emboj/20.18.5033
Publikováno v:
Journal of Biological Chemistry. 274:1495-1501
MN12H2 is a bactericidal antibody directed against outer membrane protein PorA epitope P1.16 of Neisseria meningitidis. Binding of MN12H2 to PorA at the meningococcal surface activates the classical complement pathway resulting in bacterial lysis. We
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a14ba2ea84f8fd28afdf6c097c841b52
https://doi.org/10.1074/jbc.274.3.1495
https://doi.org/10.1074/jbc.274.3.1495
Autor:
R Arjen, Kramer, Klaus, Brandenburg, Lucy, Vandeputte-Rutten, Marjolein, Werkhoven, Piet, Gros, Niek, Dekker, Maarten R, Egmond
Publikováno v:
European journal of biochemistry. 269(6)
OmpT is an integral outer membrane protease of Escherichia coli. Overexpression of OmpT in E. coli and subsequent in vitro folding of the produced inclusion bodies yielded protein with a native-like structure. However, enzymatically active protease w
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::3c1cf5757a822064b298c330db9def2d
https://pubmed.ncbi.nlm.nih.gov/11895445
https://pubmed.ncbi.nlm.nih.gov/11895445
Autor:
Gerard Jan de Roon, Niek Dekker, R.Arjen Kramer, Lucy Vandeputte-Rutten, Piet Gros, Maarten R. Egmond
Publikováno v:
FEBS Letters. (3):426-430
Escherichia coli outer membrane protease OmpT has previously been classified as a serine protease with Ser(99) and His(212) as active site residues. The recently solved X-ray structure of the enzyme was inconsistent with this classification, and the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c3e919778bdd9be6575092f10f2531ef