Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Marion Gehrmann"'
Publikováno v:
Biochemistry. 41:3302-3310
The two-domain fragment N+K1 (rNK1) [Glu(1)-Glu(163)] of human plasminogen was expressed in E. coli as a hexahistidine-tagged fusion protein and chromatographically purified. The (1)H NMR spectrum supports proper folding of the K1 component within th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f1056dd12d8f0a9c4ecae5a01fb5e3a7
https://doi.org/10.1021/bi016018j
https://doi.org/10.1021/bi016018j
Autor:
László Bányai, László Patthy, Hedvig Tordai, Marion Gehrmann, Klára Briknarová, Miguel Llinás
Publikováno v:
Journal of Biological Chemistry. 276:27613-27621
Human matrix metalloproteinase-2 (MMP-2) contains an array of three fibronectin type II (FII) modules postulated to interact with gelatin (denatured collagen). Here, we verify that the NMR solution structure of the third FII repeat (COL-3) is similar
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8ecdd3b27c9f9ba32450bee0698dadb4
https://doi.org/10.1074/jbc.m101105200
https://doi.org/10.1074/jbc.m101105200
Autor:
Miguel Llinás, László Bányai, Marion Gehrmann, Justin T. Douglas, Hedvig Tordai, László Patthy
Publikováno v:
The Journal of biological chemistry. 279(45)
Matrix metalloproteinase 2 (MMP-2) contains three fibronectin type II (col) modules that contribute to its collagen specificity. We observed that the CD spectra of the separate col modules account for the CD and temperature profiles of the in-tandem
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fd32af2ec7ae5b1e77091de5de5f986e
https://pubmed.ncbi.nlm.nih.gov/15317806
https://pubmed.ncbi.nlm.nih.gov/15317806
Publikováno v:
The Journal of biological chemistry. 278(14)
The interaction of matrix metalloproteinase 2 (MMP-2) with gelatin is mediated by three repeats homologous to fibronectin type II (FN2) modules, which are inserted in the catalytic domain in proximity of the active site. We screened a random 15-mer p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9c834cb6127cd579a3ccaa52fce6b452
https://pubmed.ncbi.nlm.nih.gov/12486137
https://pubmed.ncbi.nlm.nih.gov/12486137
Publikováno v:
Biological Chemistry. 383
Human matrix metalloproteinase-2 (MMP-2) contains three in-tandem fibronectin type II (FII) repeats that bind gelatin. Here, we report the NMR solution structure of the first FII module of MMP-2 (col-1). The latter is described as a characteristic, g
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b246624bb4155735e5a84dffb1b6135c
https://doi.org/10.1515/bc.2002.014
https://doi.org/10.1515/bc.2002.014
Autor:
Johann Schaller, Valerae O. Lewis, Miguel Llinás, Joshua E. Hyman, Lawrence Weissbach, Deryk G. Jones, Marion Gehrmann, Al Rielly
Publikováno v:
European journal of biochemistry. 259(3)
The cDNA corresponding to exons 2-4 of the processed human plasminogen (Pgn) gene, encoding the N-terminal peptide domain (NTP), has been cloned, expressed in Escherichia coli as a recombinant protein (r-NTP) containing a hexahistidine tag, and refol
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ef68566a37317a5abc21cf8ec3f3ae8e
https://pubmed.ncbi.nlm.nih.gov/10092845
https://pubmed.ncbi.nlm.nih.gov/10092845
Autor:
Veenstra, Timothy D., Yates, John R.
Publikováno v:
Proteomics for Biological Discovery; 2006, p47-61, 15p
Written by recognized experts in the study of proteins,Proteomics for Biological Discovery begins bydiscussing the emergence of proteomics from genome sequencingprojects and a summary of potential answers to be gained fromproteome-level research. The
