Results 21 to 30 of about 3,484 (169)

Mutational Analysis of the Nucleotide Binding Sites of the Yeast Vacuolar Proton-translocating ATPase [PDF]

Journal of Biological Chemistry, 1998
To further define the structure of the nucleotide binding sites on the vacuolar proton-translocating ATPase (V-ATPase), the role of aromatic residues at the catalytic sites was probed using site-directed mutagenesis of the VMA1 gene that encodes the A subunit in yeast.
K J, MacLeod, E, Vasilyeva, J D, Baleja, M, Forgac   +3 more
openaire   +2 more sources

Resolution of Subunit Interactions and Cytoplasmic Subcomplexes of the Yeast Vacuolar Proton-translocating ATPase [PDF]

Journal of Biological Chemistry, 1996
The vacuolar proton-translocating ATPase is the principal energization mechanism that enables the yeast vacuole to perform most of its physiological functions. We have undertaken an examination of subunit-subunit interactions and assembly states of this enzyme.
J J, Tomashek, J L, Sonnenburg, J M, Artimovich, D J, Klionsky   +3 more
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

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

Vacuolar Acidification and Bafilomycin-Sensitive Proton Translocating ATPase in Human Epidermal Langerhans Cells

Journal of Investigative Dermatology, 1991
Langerhans cells (LC) are the principal antigen-presenting cells (APC) of squamous epithelia. We have previously shown that freshly isolated LC (fLC) are able to deliver endocytosed membrane MHC class II molecules into acidic environments, and that this capacity is lost when LC are placed in culture (cLC).
GIROLOMONI, Giampiero, Stone DK, Bergstresser PR, Cruz P.D.   +3 more
openaire   +3 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

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

British journal of pharmacology, 2012
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

Identification and Reconstitution of an Isoform of the 116-kDa Subunit of the Vacuolar Proton Translocating ATPase [PDF]

Journal of Biological Chemistry, 1999
We have identified a cDNA encoding an isoform of the 116-kDa subunit of the bovine vacuolar proton translocating ATPase. The predicted protein sequence of the new isoform, designated a2, consists of 854 amino acids with a calculated molecular mass of 98,010 Da; it has approximately 50% identity to the original isoform (a1) we described (Peng, S.-B ...
S B, Peng, X, Li, B P, Crider, Z, Zhou, P, Andersen, S J, Tsai, X S, Xie, D K, Stone   +7 more
openaire   +2 more sources

A thermo-physical analysis of the proton pump vacuolar-ATPase: the constructal approach [PDF]

, 2014
Pumping protons across a membrane was a critical step at the origin of life on earth, and it is still performed in all living organisms, including in human cells. Proton pumping is paramount to keep normal cells alive, e.g.
Deisboeck, Thomas S., Lucia, Umberto, Ponzetto, Antonio   +2 more
core   +2 more sources