Zobrazeno 1 - 10
of 95
pro vyhledávání: '"Jan Hofsteenge"'
The beta-chain of human interleukin 12 (IL-12) contains at position 319-322, the sequence Trp-x-x-Trp. In human RNase 2 this is the recognition motif for a new, recently discovered posttranslational modification, i.e., the C-glycosidic attachment of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b24f8c51bcf800d1adb3c07661cd7ce3
http://doc.rero.ch/record/304956/files/9-5-435.pdf
http://doc.rero.ch/record/304956/files/9-5-435.pdf
Autor:
Jan Hofsteenge, Stuart R. Stone
Recombinant hirudin variant-2(Lys47), was found to be a competitive inhibitor of human alpha-thrombin with respect to peptidyl p-nitroanilide substrates. These results contrast with those of Degryse and coworkers that suggest that recombinant hirudin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::62c43bff37a4609d4c29f995f3151d63
http://doc.rero.ch/record/290650/files/4-3-295.pdf
http://doc.rero.ch/record/290650/files/4-3-295.pdf
We have previously shown that DNA demethylation by chick embryo 5-methylcytosine (5-MeC)-DNA glycosylase needs both protein and RNA. RNA from enzyme purified by SDS-PAGE was isolated and cloned. The clones have an insert ranging from 240 to 670 bp an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e193b46755d4f300c047cae228cfe101
http://doc.rero.ch/record/304069/files/25-22-4545.pdf
http://doc.rero.ch/record/304069/files/25-22-4545.pdf
Autor:
Daniel Hess, Saskia A J Lesnik Oberstein, Jeremy J. Keusch, Jan Hofsteenge, Raoul C.M. Hennekam
Publikováno v:
Journal of biological chemistry, 283(12), 7354-7360. American Society for Biochemistry and Molecular Biology Inc.
Peters Plus syndrome is an autosomal recessive disorder characterized by anterior eye chamber defects, disproportionate short stature, developmental delay, and cleft lip and/or palate. It is caused by splice site mutations in what was thought to be a
Primary and Tertiary Structure Studies of p-Hydroxybenzoate Hydroxylase from Pseudomonas fluorescens
Autor:
W.J. Weijer, Jan Drenth, Rik K. Wierenga, Johan M. Vereijken, Jan Hofsteenge, Jaap J. Beintema
Publikováno v:
European Journal of Biochemistry. 113:141-150
p-Hydroxybenzoate hydroxylase from Pseudomonas fluorescens contains six methionine residues, one of which is N-terminal. After CNBr cleavage five peptides, ranging from 13 to 158 residues in length, and free homoserine were isolated and purified by r
Publikováno v:
International Journal of Mass Spectrometry. 234:11-21
The low energy dissociation technique electron capture dissociation has been applied to a series of thrombospondin and properdin derived O-fucosylated glycopeptides. Followed by capture of an electron by multiply protonated precursor ions [M+nH]n+ re
Publikováno v:
Phytochemistry, 63(5), 517-522. PERGAMON-ELSEVIER SCIENCE LTD
Upon centrifugation, rubber latex is divided into a layer of rubber particles, the cytosol, and the lutoid-body fraction, which is of vacuolar origin. One of the proteins isolated from the lutoid-body fraction is a protein with a molecular mass of 43
Autor:
Peter A. Jekel, Henk de Vries, Jan Hofsteenge, Jan Jacob Schuringa, Toto Subroto, Ukun M.S. Soedjanaatmadja, Jaap J. Beintema
Publikováno v:
Plant Physiology and Biochemistry. 39:1047-1055
The lutoid-body (bottom) fraction of latex from the rubber tree (Hevea brasiliensis) contains a limited number of major proteins. These are the chitin-binding protein hevein, its precursor and C-terminal fragment of the precursor, a basic chitinase/l
Publikováno v:
Protein Expression and Purification. 22:174-179
Ribonucleases can be cytotoxic if they retain their ribonucleolytic activity in the cytosol. The cytosolic ribonucleolytic activity of ribonuclease A (RNase A) and other pancreatic-type ribonucleases is limited by the presence of excess ribonuclease
Autor:
Jasna Peter-Katalinic, Kristin G. Huwiler, Boris Macek, Daniel Hess, Jan Hofsteenge, Deane F. Mosher, Jack Lawler
Publikováno v:
Journal of Biological Chemistry. 276:6485-6498
Thrombospondin-1 (TSP-1) is a multidomain protein that has been implicated in cell adhesion, motility, and growth. Some of these functions have been localized to the three thrombospondin type 1 repeats (TSRs), modules of approximately 60 amino acids