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of 10
pro vyhledávání: '"Christoph, Kluge"'
Publikováno v:
Biophysical Journal. 121:671-683
The (local) curvature of cellular membranes acts as a driving force for the targeting of membrane-associated proteins to specific membrane domains, as well as a sorting mechanism for transmembrane proteins, e.g., by accumulation in regions of matchin
Autor:
Kai Karin Baum, Christoph Kluge
Publikováno v:
E-Learning im digitalen Zeitalter ISBN: 9783658361129
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::13ec6c111ca554aeaf688f9878eb6123
https://doi.org/10.1007/978-3-658-36113-6_19
https://doi.org/10.1007/978-3-658-36113-6_19
Autor:
Dortje Golldack, Shanti S. Sharma, Karl-Josef Dietz, Tetsuro Mimura, Christoph Kluge, Gary C. Harris, A. N. Chardonnens, Nastaran Tavakoli
Publikováno v:
Journal of Experimental Botany. 52:1969-1980
Two electrogenic H(+)-pumps, the vacuolar type H(+)-ATPase (V-ATPase) and the vacuolar pyrophosphatase, coexist at membranes of the secretory pathway of plants. The V-ATPase is the dominant H(+)-pump at endomembranes of most plant cells, both in term
Autor:
Herve Bercovier, Gilles Marchal, Catherine Fitting, Antonio Bandeira, Mohammad Abolhassani, Micheline Lagranderie, Christoph Kluge, Helene Kiefer–Biasizzo, Michel Huerre, Marie Anne Nahori
Publikováno v:
Gastroenterology
Gastroenterology, WB Saunders, 2011, 141 (2), pp.642-52, 652.e1-4. ⟨10.1053/j.gastro.2011.05.002⟩
Gastroenterology, 2011, 141 (2), pp.642-52, 652.e1-4. ⟨10.1053/j.gastro.2011.05.002⟩
Gastroenterology, WB Saunders, 2011, 141 (2), pp.642-52, 652.e1-4. ⟨10.1053/j.gastro.2011.05.002⟩
Gastroenterology, 2011, 141 (2), pp.642-52, 652.e1-4. ⟨10.1053/j.gastro.2011.05.002⟩
International audience; BACKGROUND & AIMS: Mycobacterium bovis Bacillus Calmette-Guérin (BCG), killed by extended freeze-drying (EFD), induces secretion of interleukin-10 and reduces lung inflammation in a mouse model of asthma. We investigated the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::574990fbf25f6b17e59da0d859dc7752
https://hal-pasteur.archives-ouvertes.fr/pasteur-00627235
https://hal-pasteur.archives-ouvertes.fr/pasteur-00627235
Autor:
Christoph, Kluge, Thorsten, Seidel, Susanne, Bolte, Shanti S, Sharma, Miriam, Hanitzsch, Beatrice, Satiat-Jeunemaitre, Joachim, Ross, Markus, Sauer, Dortje, Golldack, Karl-Josef, Dietz
Publikováno v:
BMC Cell Biology, Vol 5, Iss 1, p 29 (2004)
BMC Cell Biology
BMC Cell Biology, BioMed Central, 2004, 5, pp.29. ⟨10.1186/1471-2121-5-29⟩
BMC Cell Biology
BMC Cell Biology, BioMed Central, 2004, 5, pp.29. ⟨10.1186/1471-2121-5-29⟩
Background Vacuolar H+-ATPases are large protein complexes of more than 700 kDa that acidify endomembrane compartments and are part of the secretory system of eukaryotic cells. They are built from 14 different (VHA)-subunits. The paper addresses the
Colocalization and FRET-analysis of subunits c and a of the vacuolar H+-ATPase in living plant cells
Autor:
Miriam Hanitzsch, Karl-Josef Dietz, Christoph Kluge, Dortje Golldack, Joachim Ross, Markus Sauer, Thorsten Seidel
Publikováno v:
Journal of biotechnology. 112(1-2)
The proton-translocating plant vacuolar H+-ATPase (VHA) is of prime importance for acidification of intracellular compartments and is essential for processes such as secondary activated transport, maintenance of ion homeostasis, and adaptation to env
Autor:
Petra Lamkemeyer, Dortje Golldack, Karl-Josef Dietz, Andrea Kandlbinder, Christoph Kluge, Nastaran Tavakoli
The vacuolar-type ATPase (V-ATPase) and the vacuolar H+-pyrophosphatase are electrogenic proton pumps at plant endomembranes that create the proton motive force required for secondary activated transport and metabolite accumulation during development
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b1bfb2361d885827eeda0164cd0330f2
https://doi.org/10.1080/0968768031000084154
https://doi.org/10.1080/0968768031000084154
Autor:
Igor A. Tikhonovich, Vera I. Safronova, Karl-Josef Dietz, Alexey Y. Borisov, Viktor E. Tsyganov, Andrei A. Belimov, Tatyana N. Egorova, Christoph Kluge, Tatyana A. Sergeyeva, Angelika Preisfeld, Vitaley V. Stepanok, Victoria A. Matveyeva
Fifteen bacterial strains containing 1-aminocyclopropane-1-carboxylate (ACC) deaminase were isolated from the rhizoplane of pea (Pisum sativum L.) and Indian mustard (Brassica juncea L.) grown in different soils and a long-standing sewage sludge cont
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::457cef801993d8a3d37eb4ae871378da
https://doi.org/10.1139/cjm-47-7-642
https://doi.org/10.1139/cjm-47-7-642
Autor:
Dortje Golldack, Béatrice Satiat-Jeunemaitre, Miriam Hanitzsch, Shanti S Sharma, Joachim Roß, Susanne Bolte, Karl-Josef Dietz, Christoph Kluge, Markus Sauer, Thorsten Seidel
Publikováno v:
BMC Cell Biology. 5:29
Vacuolar H+-ATPases are large protein complexes of more than 700 kDa that acidify endomembrane compartments and are part of the secretory system of eukaryotic cells. They are built from 14 different (VHA)-subunits. The paper addresses the question of
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Biomembranes. (1):105-110
A 1034 bp cDNA encoding the full length sequence of subunit D of the vacuolar H+-ATPase was cloned from Arabidopsis thaliana. The open reading frame of the cDNA clone vatpD contains 780 bp and codes for a protein of 29.1 kDa with a pI of 9.52. Struct