Zobrazeno 1 - 10
of 104
pro vyhledávání: '"Wilbert C, Boelens"'
Autor:
Sanne M. M. Hensen, Wilbert C. Boelens, Kimberly M. Bonger, Remco T. P. van Cruchten, Floris L. van Delft, Ger J. M. Pruijn
Publikováno v:
Molecules, Vol 20, Iss 4, Pp 6592-6600 (2015)
Citrullination is the conversion of peptidylarginine to peptidylcitrulline, which is catalyzed by peptidylarginine deiminases. This conversion is involved in different physiological processes and is associated with several diseases, including cancer
Externí odkaz:
https://doaj.org/article/1c5529670b08481997779bfbf5f10434
Autor:
Toshiyuki Watanabe, Saaya Hayasaki, Yoriko Atomi, Eri Ohto-Fujita, Soichiro Fujiki, Aya Atomi, Miho Shimizu, Wilbert C. Boelens
Publikováno v:
Journal of Biochemistry, 168, 2, pp. 125-137
Journal of Biochemistry, 168, 125-137
Journal of Biochemistry, 168, 125-137
αB-crystallin is highly expressed in the heart and slow skeletal muscle; however, the roles of αB-crystallin in the muscle are obscure. Previously, we showed that αB-crystallin localizes at the sarcomere Z-bands, corresponding to the focal adhesio
Autor:
John den Engelsman, Chantal van de Schootbrugge, Jeongsik Yong, Ger J M Pruijn, Wilbert C Boelens
Publikováno v:
PLoS ONE, Vol 8, Iss 9, p e73489 (2013)
The human small heat shock protein αB-crystallin (HspB5) is a molecular chaperone which is mainly localized in the cytoplasm. A small fraction can also be found in nuclear speckles, of which the localization is mediated by successional phosphorylati
Externí odkaz:
https://doaj.org/article/e60e8e1673d845e69e80c0fa7d371aea
Publikováno v:
Scientific Reports, 10, pp. 1-12
Scientific Reports, Vol 10, Iss 1, Pp 1-12 (2020)
Scientific Reports, 10, 1-12
Scientific Reports
Scientific Reports, Vol 10, Iss 1, Pp 1-12 (2020)
Scientific Reports, 10, 1-12
Scientific Reports
Women with silicone gel-filled breast implants are exposed to organosilicon compounds, in particular methylsiloxanes, as a result of ‘gel bleed’ and implant rupture. Although these silicones were originally considered to be inert, increasing evid
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8180397ea9ad846f1f3f661ca7bd50d3
https://hdl.handle.net/2066/224930
https://hdl.handle.net/2066/224930
Autor:
Wilbert C. Boelens
Publikováno v:
Cell Stress & Chaperones, 25, 581-591
Cell Stress & Chaperones
Cell Stress & Chaperones, 25, 4, pp. 581-591
Cell Stress & Chaperones
Cell Stress & Chaperones, 25, 4, pp. 581-591
Small heat shock proteins function as chaperones by binding unfolding substrate proteins in an ATP-independent manner to keep them in a folding-competent state and to prevent irreversible aggregation. They play crucial roles in diseases that are char
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2ac9271db0c2278f274eeae4fe7baf17
http://hdl.handle.net/2066/219179
http://hdl.handle.net/2066/219179
Autor:
Wilbert C. Boelens, Cynthia M. de Bont, Priscilla Faas, Ger J. M. Pruijn, Marloes E.M. Stokman, Helen L. Wright, Rogier M Thurlings
Publikováno v:
Journal of Autoimmunity, 113
JOURNAL OF AUTOIMMUNITY
JOURNAL OF AUTOIMMUNITY
Neutrophil extracellular traps (NETs) are networks of extracellular chromatin decorated with antimicrobial proteins, formed by neutrophils to entrap pathogens. NETs have been implicated in the generation of autoimmune reactions. Here, we investigate
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::89511e94e176631cf0f117ee46ba5e0b
https://hdl.handle.net/2066/222128
https://hdl.handle.net/2066/222128
Autor:
Wilbert C. Boelens, Frances D.L. Kondrat, Nicholas J. Ray, Nicholas H. Keep, Ambrose R. Cole, Gillian R. Hilton, Christine Slingsby, Wilma Vree Egberts, Alice R. Clark, John A. Carver, Justin L. P. Benesch
Publikováno v:
Journal of Molecular Biology, 430, 3297-3310
'Journal of Molecular Biology ', vol: 430, pages: 3297-3310 (2018)
Journal of Molecular Biology
Journal of Molecular Biology, 430, 18, pp. 3297-3310
'Journal of Molecular Biology ', vol: 430, pages: 3297-3310 (2018)
Journal of Molecular Biology
Journal of Molecular Biology, 430, 18, pp. 3297-3310
Heterogeneity in small heat shock proteins (sHsps) spans multiple spatiotemporal regimes—from fast fluctuations of part of the protein, to conformational variability of tertiary structure, plasticity of the interfaces, and polydispersity of the int
Autor:
Jeroen van den Akker, Ed VanBavel, Remon van Geel, Hanke L Matlung, Bilge Guvenc Tuna, George M C Janssen, Peter A van Veelen, Wilbert C Boelens, Jo G R De Mey, Erik N T P Bakker
Publikováno v:
PLoS ONE, Vol 6, Iss 8, p e23067 (2011)
While inward remodeling of small arteries in response to low blood flow, hypertension, and chronic vasoconstriction depends on type 2 transglutaminase (TG2), the mechanisms of action have remained unresolved. We studied the regulation of TG2 activity
Externí odkaz:
https://doaj.org/article/25f4718461c746d789739fa08ef99995
Autor:
Nelson Arispe, Ivan Bello, Ricardo Capone, Wilbert C. Boelens, Wilma Vree Egberts, Antonio De Maio, David M. Cauvi
Publikováno v:
Cell stress & chaperones, vol 24, iss 5
Increasing evidence shows that heat shock proteins (hsp) escape the cytosol gaining access to the extracellular environment, acting as signaling agents. Since the majority of these proteins lack the information necessary for their export via the clas
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::968ab03279508bf97daa4518e6772ed2
https://europepmc.org/articles/PMC6717221/
https://europepmc.org/articles/PMC6717221/
Autor:
Johannes Buchner, Justin L. P. Benesch, Krzysztof Liberek, Ciro Cecconi, Lawrence E. Hightower, Nikolai B. Gusev, Vincent Timmerman, Brent L. Lockwood, Tangchun Wu, John A. Carver, Simon Alberti, Hyun O Lee, Serena Carra, Angelo Poletti, Elizabeth Vierling, Wilbert C. Boelens, Melinda E. Tóth, Robert M. Tanguay, Heath Ecroyd, Rachel E. Klevit
Publikováno v:
Cell stress & chaperones (Online) 24 (2019): 295–308. doi:10.1007/s12192-019-00979-z
info:cnr-pdr/source/autori:Carra S.; Alberti S.; Benesch J.L.P.; Boelens W.; Buchner J.; Carver J.A.; Cecconi C.; Ecroyd H.; Gusev N.; Hightower L.E.; Klevit R.E.; Lee H.O.; Liberek K.; Lockwood B.; Poletti A.; Timmerman V.; Toth M.E.; Vierling E.; Wu T.; Tanguay R.M./titolo:Small heat shock proteins: multifaceted proteins with important implications for life/doi:10.1007%2Fs12192-019-00979-z/rivista:Cell stress & chaperones (Online)/anno:2019/pagina_da:295/pagina_a:308/intervallo_pagine:295–308/volume:24
Cell stress and chaperones
Cell Stress & Chaperones, 24, 2, pp. 295-308
Cell Stress & Chaperones, 24, 295-308
info:cnr-pdr/source/autori:Carra S.; Alberti S.; Benesch J.L.P.; Boelens W.; Buchner J.; Carver J.A.; Cecconi C.; Ecroyd H.; Gusev N.; Hightower L.E.; Klevit R.E.; Lee H.O.; Liberek K.; Lockwood B.; Poletti A.; Timmerman V.; Toth M.E.; Vierling E.; Wu T.; Tanguay R.M./titolo:Small heat shock proteins: multifaceted proteins with important implications for life/doi:10.1007%2Fs12192-019-00979-z/rivista:Cell stress & chaperones (Online)/anno:2019/pagina_da:295/pagina_a:308/intervallo_pagine:295–308/volume:24
Cell stress and chaperones
Cell Stress & Chaperones, 24, 2, pp. 295-308
Cell Stress & Chaperones, 24, 295-308
Small Heat Shock Proteins (sHSPs) evolved early in the history of life; they are present in archaea, bacteria, and eukaryota. sHSPs belong to the superfamily of molecular chaperones: they are components of the cellular protein quality control machine
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8b4ce67723859ffa9a82f27c15e369ae
https://hdl.handle.net/11380/1172557
https://hdl.handle.net/11380/1172557