Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Emil Boonacker"'
Autor:
Emil Boonacker, Sjoerd Elferink, Abdennasser Bardai, Jan Wormmeester, Cornelis J.F. Van Noorden
Publikováno v:
BioTechniques, Vol 35, Iss 4, Pp 766-774 (2003)
Proteolysis is a regulatory step in many physiological processes, but which proteases in what cellular sites are involved in activation or degradation of which peptides is not well known. We developed a rapid assay consisting of living cells and fluo
Externí odkaz:
https://doaj.org/article/35c7eb6eb9fa4caba758562f5afeedfa
Publikováno v:
Acta histochemica, 106(2), 89-96. Urban und Fischer Verlag Jena
The ultimate activity of an enzyme depends on many regulatory steps from transcription of the gene up to complex formation of the enzyme. Therefore, gene expression (mRNA levels) or protein expression (protein levels) are not reliable parameters to p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4fcce37a9eec85fe71990d84abc2e96f
https://doi.org/10.1016/j.acthis.2004.01.002
https://doi.org/10.1016/j.acthis.2004.01.002
Autor:
Jan Wormmeester, Emil Boonacker, Sjoerd Elferink, Abdennasser Bardai, Cornelis J.F. Van Noorden
Publikováno v:
BioTechniques, 35(4), 766-+. Eaton Publishing Company
Proteolysis is a regulatory step in many physiological processes, but which proteases in what cellular sites are involved in activation or degradation of which peptides is not well known. We developed a rapid assay consisting of living cells and fluo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::432a50f38ba7e8dfe08783ddec764ba0
https://doi.org/10.2144/03354st07
https://doi.org/10.2144/03354st07
Autor:
Abdennasser Bardai, Cornelis J.F. Van Noorden, Bernard Fleischer, Emil Boonacker, Sjoerd Elferink
Publikováno v:
journal of histochemistry and cytochemistry, 51(7), 959-968. Histochemical Society Inc.
Fluorogenic substrates [Ala-Pro]2-cresyl violet and Ala-Pro-rhodamine 110 have been tested for microscopic detection of protease activity of dipeptidyl peptidase IV (DPPIV) in living cells. DPPIV activity is one of the many functions of the multifunc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1b5cc0e4c57f79c35f76231e77e6cb8d
https://doi.org/10.1177/002215540305100711
https://doi.org/10.1177/002215540305100711
Publikováno v:
Analytical biochemistry, 252(1), 71-77. Academic Press Inc.
A new type of fluorogenic substrates for proteases based on the leaving group cresyl violet has been synthesized. Cresyl violet is not fluorescent when amino acids or peptide groups are attached but becomes highly fluorescent after proteolytic libera
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::531d342170238c08414fd545a6b0b4d1
https://doi.org/10.1006/abio.1997.2312
https://doi.org/10.1006/abio.1997.2312
Publikováno v:
European journal of cell biology. 82(2)
CD26/DPPIV can be considered a moonlighting protein because it is a multifunctional protein that exerts its different functions depending on cell type and intra- or extracellular conditions in which it is expressed. In the present review, we summariz
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1a23f8ab5cfd60e4908c0362e147d2fe
https://pubmed.ncbi.nlm.nih.gov/12647932
https://pubmed.ncbi.nlm.nih.gov/12647932
Publikováno v:
journal of histochemistry and cytochemistry, 50(9), 1169-1177. Histochemical Society Inc.
CD26/DPPIV is a cell surface glycoprotein that functions both in signal transduction and as a proteolytic enzyme, dipeptidyl peptidase IV (DPPIV). To investigate how two separate functions of one molecule are regulated, we analyzed CD26 protein expre
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2253ece7fb63dd6be19fdfe49c92937d
https://pubmed.ncbi.nlm.nih.gov/12185194
https://pubmed.ncbi.nlm.nih.gov/12185194