Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Wolfgang M J, Obermann"'
Publikováno v:
Molecules, Vol 27, Iss 15, p 4976 (2022)
(1) Background: The amino acid sequence elucidation of peptides from the gas phase fragmentation mass spectra, de novo sequencing, is a valuable method for the identification of unknown proteins complementary to Edman sequencing. It is increasingly u
Externí odkaz:
https://doaj.org/article/3acf8b963f064e1f912bd51279ffa91c
Publikováno v:
Frontiers in Cell and Developmental Biology, Vol 9 (2021)
Although platelets and the coagulation factors are components of the blood system, they become part of and contribute to the tumor microenvironment (TME) not only within a solid tumor mass, but also within a hematogenous micrometastasis on its way th
Externí odkaz:
https://doaj.org/article/2b7b0e3d90ff4681b2963e63334c5466
Publikováno v:
PLoS ONE, Vol 8, Iss 8, p e71856 (2013)
Hsp90 (heat shock protein 90) is an essential molecular chaperone that mediates folding and quality control of client proteins. Many of them such as protein kinases, steroid receptors and transcription factors are involved in cellular signaling proce
Externí odkaz:
https://doaj.org/article/2ad1e8c45cba4bc982c5cf6a02bb1cab
Autor:
Wolfgang M. J. Obermann
Heat shock protein 90 (HSP90) is a molecular chaperone that supervises folding of cellular signaling proteins such as steroid receptors and many protein kinases. HSP90 relies on ATP hydrolysis for powering a conformational circuit that helps fold the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::352ba3219d31c179b85616ec197aaa08
https://europepmc.org/articles/PMC6200951/
https://europepmc.org/articles/PMC6200951/
Autor:
Wolfgang M. J. Obermann, Verena Ihrig
Publikováno v:
SLAS discovery : advancing life sciences RD. 22(7)
Deletion of a single phenylalanine residue at position 508 of the protein CFTR (cystic fibrosis transmembrane conductance regulator), a chloride channel in lung epithelium, is the most common cause for cystic fibrosis. As a consequence, folding of th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2fe2fb02f1b57ae87bdd7e1003d37f4d
https://pubmed.ncbi.nlm.nih.gov/28346090
https://pubmed.ncbi.nlm.nih.gov/28346090
Publikováno v:
Journal of Biological Chemistry. 289:36220-36228
Aha1 (activator of Hsp90 ATPase) stimulates the ATPase activity of the molecular chaperone Hsp90 to accelerate the conformational cycle during which client proteins attain their final shape. Thereby, Aha1 promotes effective folding of Hsp90-dependent
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1daecf00d07d3204376ca6cbe203a29d
https://doi.org/10.1074/jbc.m114.590141
https://doi.org/10.1074/jbc.m114.590141
Publikováno v:
International Journal of Biological Macromolecules. 45:310-314
The activity of many oncogenic proteins depends on the molecular chaperone Hsp90. Recent studies indicate that tumorigenesis is associated with increased expression of chaperones, such as Hsp90. However, little is known about the isoform dependence a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6acfa1306878fcccf6b1b66a85f0d547
https://doi.org/10.1016/j.ijbiomac.2009.06.012
https://doi.org/10.1016/j.ijbiomac.2009.06.012
Publikováno v:
International journal of biological macromolecules. 45(3)
The activity of many oncogenic proteins depends on the molecular chaperone Hsp90. Recent studies indicate that tumorigenesis is associated with increased expression of chaperones, such as Hsp90. However, little is known about the isoform dependence a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::f58b858837ad724b5a207e1088238c3d
https://pubmed.ncbi.nlm.nih.gov/19576239
https://pubmed.ncbi.nlm.nih.gov/19576239
Publikováno v:
Biochemistry. 47(31)
rhe molecular chaperones Hsp90 and Hsp70 are highly regulated by various cochaperones that participate in the activation of steroid receptors. Here we study Tpr2 (also called DjC7), a TPR domain-containing type III J protein implicated in steroid rec
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f4b8e28fbc6aa603d5b606d7317051cf
https://pubmed.ncbi.nlm.nih.gov/18620420
https://pubmed.ncbi.nlm.nih.gov/18620420
Publikováno v:
Journal of cell science. 121(Pt 5)
Heat shock protein 90 (HSP90) is considered a specialized molecular chaperone that controls the folding of cell-regulatory proteins such as steroid receptors and kinases. However, its high abundance is suggestive of a more general function in other f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e488f348d6a5ebde77b39a06cacd1183
https://pubmed.ncbi.nlm.nih.gov/18270269
https://pubmed.ncbi.nlm.nih.gov/18270269