Zobrazeno 1 - 10
of 17
pro vyhledávání: '"Nicolas Lentze"'
Publikováno v:
International Journal of Molecular Sciences, Vol 10, Iss 6, Pp 2763-2788 (2009)
A key property of complex biological systems is the presence of interaction networks formed by its different components, primarily proteins. These are crucial for all levels of cellular function, including architecture, metabolism and signalling, as
Externí odkaz:
https://doaj.org/article/ac50336d97f645fd8dce2c84035006d5
Autor:
Anna Klaus, Sarah Zorman, Alexandre Berthier, Cécile Polge, Sacnicte Ramirez, Sylvie Michelland, Michel Sève, Didier Vertommen, Mark Rider, Nicolas Lentze, Daniel Auerbach, Uwe Schlattner
Publikováno v:
PLoS ONE, Vol 8, Iss 5, p e62497 (2013)
AMP-activated protein kinase (AMPK) is a cellular and whole body energy sensor with manifold functions in regulating energy homeostasis, cell morphology and proliferation in health and disease. Here we apply multiple, complementary in vitro and in vi
Externí odkaz:
https://doaj.org/article/ecd29b6cc2694f8993a9151e2c81222c
A hallmark of alpha-crystallin-type small heat shock proteins (sHsps) is their highly dynamic oligomeric structure which promotes intermolecular interactions involved in subunit exchange and substrate binding (chaperone-like activity). We studied the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::76b61e77671bc49758e6d76b6f769978
https://doi.org/10.1111/j.1432-1033.2004.04180.x
https://doi.org/10.1111/j.1432-1033.2004.04180.x
Autor:
Joana Almaça, Rainer Schreiber, Karl Kunzelmann, Daniel Auerbach, Simão Luz, Nicolas Lentze, Diana Faria, Pedro Estilita Monteiro Da Cruz, Mandana Rezwan, Margarida D. Amaral, Luisa Alessio, Carlos M. Farinha, José Paulo Martins, Yuemin Tian
Publikováno v:
Pflügers Archiv - European Journal of Physiology. 463:819-827
Cystic fibrosis lung disease is caused by reduced Cl(-) secretion along with enhanced Na(+) absorption, leading to reduced airway surface liquid and compromised mucociliary clearance. Therapeutic strategies have been developed to activate cystic fibr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1847688b661b9e85b76fe867fd950234
https://doi.org/10.1007/s00424-012-1091-1
https://doi.org/10.1007/s00424-012-1091-1
Publikováno v:
International Journal of Molecular Sciences, Vol 10, Iss 6, Pp 2763-2788 (2009)
International Journal of Molecular Sciences
International Journal of Molecular Sciences, MDPI, 2009, 10 (6), pp.2763-88. ⟨10.3390/ijms10062763⟩
International Journal of Molecular Sciences
International Journal of Molecular Sciences, MDPI, 2009, 10 (6), pp.2763-88. ⟨10.3390/ijms10062763⟩
International audience; A key property of complex biological systems is the presence of interaction networks formed by its different components, primarily proteins. These are crucial for all levels of cellular function, including architecture, metabo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::125729827b4a52d6d8606a1a6f539c23
http://www.mdpi.com/1422-0067/10/6/2763/
http://www.mdpi.com/1422-0067/10/6/2763/
Autor:
Nicolas Lentze, Daniel Auerbach
Publikováno v:
Expert Opinion on Therapeutic Targets. 12:505-515
Background: The yeast two-hybrid system is the most widely used genetic assay to identify and characterize novel protein interactions. Over the past decade, the system has been adapted to cover an increasingly wide range of applications, including va
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::de8f21d14ccb77d58a20571b60f1ccf5
https://doi.org/10.1517/14728222.12.4.505
https://doi.org/10.1517/14728222.12.4.505
Autor:
Nicolas Lentze, Franz Narberhaus
Publikováno v:
Journal of Biological Sciences. 5:1-9
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e942d54410797195ed917bea3476297c
https://doi.org/10.3923/jbs.2005.1.9
https://doi.org/10.3923/jbs.2005.1.9
Autor:
Franz Narberhaus, Nicolas Lentze
Publikováno v:
Biochemical and Biophysical Research Communications. 325:401-407
Small heat shock proteins (sHsps) form large oligomers that are characterised by their dynamic behaviour, e.g., complex disassembly/reassembly and extensive subunit exchange. These processes are interrelated with sHsp/substrate interaction. sHsps bin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7bbf5e881f1b157078420e059f69bfd9
https://doi.org/10.1016/j.bbrc.2004.10.043
https://doi.org/10.1016/j.bbrc.2004.10.043
Publikováno v:
Journal of Molecular Biology. 328:927-937
The diverse family of alpha-crystallin-type small heat shock proteins (alpha-Hsps or sHsps) is characterised by a central, moderately conserved alpha-crystallin domain. Oligomerisation followed by dissociation of subparticles is thought to be a prere
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9f48400b9a6c5f1a88134444f5b47906
https://doi.org/10.1016/s0022-2836(03)00356-5
https://doi.org/10.1016/s0022-2836(03)00356-5
Publikováno v:
European Journal of Biochemistry. 269:3578-3586
Oligomerization into multimeric complexes is a prerequisite for the chaperone function of almost all alpha-crystallin type heat shock proteins (alpha-Hsp), but the molecular details of complex assembly are poorly understood. The alpha-Hsp proteins fr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d9b6f866bd3f090534759bfd3a8025c5
https://doi.org/10.1046/j.1432-1033.2002.03049.x
https://doi.org/10.1046/j.1432-1033.2002.03049.x