Results 21 to 30 of about 2,525 (167)

Reconstitution in Vitro of the V1 Complex from the Yeast Vacuolar Proton-translocating ATPase [PDF]

Journal of Biological Chemistry, 1997
Oligomeric assembly is a fundamental aspect of many complex enzymes. Using our native gel technique for examining subcomplexes of the V-ATPase V1 sector, we have developed an in vitro reconstitution assay for assembly of this complex. Assembly of complex II, the soluble V1 complex observed in native gels, is dependent upon the presence of divalent ...
John J. Tomashek, Brian S. Garrison, Daniel J. Klionsky   +2 more
openaire   +2 more sources

Vacuolar proton-translocating ATPase is required for antifungal resistance and virulence of Candida glabrata

PLOS ONE, 2019
Vacuolar proton-translocating ATPase (V-ATPase) is located in fungal vacuolar membranes. It is involved in multiple cellular processes, including the maintenance of intracellular ion homeostasis by maintaining acidic pH within the cell. The importance of V-ATPase in virulence has been demonstrated in several pathogenic fungi, including Candida albicans.
Asuka Minematsu, Taiga Miyazaki, Shintaro Shimamura, Hiroshi Nishikawa, Hironobu Nakayama, Takahiro Takazono, Tomomi Saijo, Kazuko Yamamoto, Yoshifumi Imamura, Katsunori Yanagihara, Shigeru Kohno, Hiroshi Mukae, Koichi Izumikawa   +12 more
openaire   +5 more sources

Transmembrane Topography of the 100-kDa a Subunit (Vph1p) of the Yeast Vacuolar Proton-translocating ATPase [PDF]

Journal of Biological Chemistry, 1999
The membrane topography of the yeast vacuolar proton-translocating ATPase a subunit (Vph1p) has been investigated using cysteine-scanning mutagenesis. A Cys-less form of Vph1p lacking the seven endogenous cysteines was constructed and shown to have 80% of wild type activity.
X H, Leng, T, Nishi, M, Forgac
openaire   +2 more sources

Role of vacuolar acidification in protein sorting and zymogen activation: a genetic analysis of the yeast vacuolar proton-translocating ATPase. [PDF]

Molecular and Cellular Biology, 1990
Vacuolar acidification has been proposed to play a key role in a number of cellular processes, including protein sorting, zymogen activation, and maintenance of intracellular pH. We investigated the significance of vacuolar acidification by cloning and mutagenizing the gene for the yeast vacuolar proton-translocating ATPase 60-kilodalton subunit (VAT2).
C T, Yamashiro, P M, Kane, D F, Wolczyk, R A, Preston, T H, Stevens   +4 more
openaire   +2 more sources

The proton translocation domain of cellular vacuolar ATPase provides a target for the treatment of influenza A virus infections [PDF]

British Journal of Pharmacology, 2011
Cellular vacuolar ATPases (v-ATPase) play an important role in endosomal acidification, a critical step in influenza A virus (IAV) host cell infection. We investigated the antiviral activity of the v-ATPase inhibitor saliphenylhalamide (SaliPhe) and compared it with several older v-ATPase inhibitors concanamycin A, bafilomycin A1, (BafA) and archazolid
Konstantin H Müller, Denis E Kainov, Karim El Bakkouri, Xavier Saelens, Jef K De Brabander, Christian Kittel, Elisabeth Samm, Claude P Muller   +7 more
openaire   +2 more sources

Tissue specific expression of the splice variants of the mouse vacuolar proton-translocating ATPase a4 subunit [PDF]

Biochemical and Biophysical Research Communications, 2007
We have identified splicing variants of the mouse a4 subunit which have the same open reading frame but have a different 5'-noncoding sequence. Further determination of the 5'-upstream region of the a4 gene in mouse indicated the presence of two first exons (exon 1a and exon 1b) which include the 5'-noncoding sequence of each variant. The mRNAs of both
Shoko, Kawasaki-Nishi, Akihito, Yamaguchi, Michael, Forgac, Tsuyoshi, Nishi   +3 more
openaire   +2 more sources

Molecular Cloning and Expression of Three Isoforms of the 100-kDa a Subunit of the Mouse Vacuolar Proton-translocating ATPase [PDF]

Journal of Biological Chemistry, 2000
We have identified cDNAs encoding three isoforms (a1, a2, and a3) of the 100-kDa a subunit of the mouse vacuolar proton-translocating ATPase (V-ATPase). The predicted protein sequences of the three isoforms are 838, 856, and 834 amino acids, respectively, and they display approximately 50% identity between isoforms.
T, Nishi, M, Forgac
openaire   +2 more sources

Subcellular distribution of the V-ATPase complex in plant cells, and in vivo localisation of the 100 kDa subunit VHA-a within the complex

, 2004
Kluge C, Seidel T, Bolte S, et al. Subcellular distribution of the V-ATPase complex in plant cells, and in vivo localisation of the 100 kDa subunit VHA-a within the complex. BMC Cell Biology. 2004;5(1):29.Background: Vacuolar H+-ATPases are large protein
Thorsten Seidel, Bolte Susanne, Kluge Christoph, Sauer, Markus, Hanitzsch, M, Kluge, C, Shanti S Sharma, Hanitzsch Miriam, Markus Sauer, Karl-Josef Dietz, Ross, J, Dortje Golldack, Satiat-Jeunemaitre Beatrice, Sharma, S. S., Golldack, Dortje, Christoph Kluge, Joachim Roß, Satiat-Jeunemaitre, B, Sharma Shanti S, Golldack Dortje, Dietz Karl-Josef, Susanne Bolte, Dietz, Karl-Josef, Bolte, S, Seidel Thorsten, Sauer Markus, Miriam Hanitzsch, Seidel, Thorsten, Beatrice Satiat-Jeunemaitre, Roß Joachim   +29 more
core   +1 more source

Organelle-specific isoenzymes of plant V-ATPase as revealed by in vivo-FRET analysis

, 2008
Seidel T, Schnitzer D, Golldack D, Sauer M, Dietz K-J. Organelle-specific isoenzymes of plant V-ATPase as revealed by in vivo-FRET analysis. BMC Cell Biology. 2008;9(1): 28.BACKGROUND: The V-ATPase (VHA) is a protein complex of 13 different VHA-subunits.
Thorsten Seidel, Sauer, Markus, Golldack Dortje, Dietz Karl-Josef, Markus Sauer, Karl-Josef Dietz, Daniel Schnitzer, Dietz, Karl-Josef, Dortje Golldack, Schnitzer Daniel, Seidel Thorsten, Sauer Markus, Golldack, Dortje, Seidel, Thorsten, Schnitzer, Daniel   +14 more
core   +1 more source

Physiological and pharmacological characterizations of the larval Anopheles albimanus rectum support a change in protein distribution and/or function in varying salinities [PDF]

, 2010
Ion regulation is a biological process crucial to the survival of mosquito larvae and a major organ responsible for this regulation is the rectum. The recta of anopheline larvae are distinct from other subfamilies of mosquitoes in several ways, yet have ...
Valenti, Micheala L., Raymond, Steven L., Smith, Peter J.S., Linser, Paul J., Smith, Kristin E.   +4 more
core   +1 more source