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protein structure, tertiary (120) 120
proton pumps (117) 117
endocytosis (116) 116
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Journal Article
Proceedings of the National Academy of Sciences - PNAS, ISSN 0027-8424, 8/2012, Volume 109, Issue 35, pp. 13961 - 13965
We report the high-resolution (1.9 Å) crystal structure of oligomycin bound to the subunit c₁₀ ring of the yeast mitochondrial ATP synthase. Oligomycin binds... 
Protons | Molecules | Yeasts | Atomic interactions | Adenosine triphosphatases | Crystals | Atoms | Genetic mutation | Oligomycins | Binding sites | Proton pore | F1Fo ATP synthase | VENTURICIDIN | RESISTANT MUTANTS | ANTIBIOTICS | MULTIDISCIPLINARY SCIENCES | SENSITIVITY | AMINO-ACID SUBSTITUTIONS | MITOCHONDRIAL ATPASE | SUBUNIT-9 | PARTIAL RESOLUTION | proton pore | INHIBITORS | CATALYZING OXIDATIVE PHOSPHORYLATION | Mitochondria - enzymology | Humans | Crystallography, X-Ray | Vacuolar Proton-Translocating ATPases - metabolism | Proton-Translocating ATPases - metabolism | Oligomycins - pharmacology | Hydrogen Bonding - drug effects | ATP Synthetase Complexes - metabolism | Drug Design | ATP Synthetase Complexes - chemistry | Binding Sites - drug effects | Escherichia coli - enzymology | Protein Structure, Secondary | Bacterial Proton-Translocating ATPases - chemistry | Bacterial Proton-Translocating ATPases - metabolism | Escherichia coli Proteins - metabolism | Mitochondria - drug effects | Proton-Translocating ATPases - chemistry | Animals | Mycobacterium tuberculosis - enzymology | Vacuolar Proton-Translocating ATPases - chemistry | Saccharomyces cerevisiae Proteins - metabolism | Saccharomyces cerevisiae - enzymology | Anti-Bacterial Agents - pharmacology | Escherichia coli Proteins - chemistry | Saccharomyces cerevisiae Proteins - chemistry | Clinical chemistry | Antibiotics | Yeast fungi | Physiological aspects | Microbiological chemistry | Chemical properties | Research | Structure | Identification and classification | Adenosine triphosphate | Protein binding | Biological Sciences | Physical Sciences
Journal Article
PloS one, ISSN 1932-6203, 2019, Volume 14, Issue 1, p. e0210883
Vacuolar proton-translocating ATPase (V-ATPase) is located in fungal vacuolar membranes... 
YEAST | HOMEOSTASIS | EVOLUTION | MEMBRANE | MULTIDISCIPLINARY SCIENCES | CALCINEURIN | ACIDIFICATION | MECHANISMS | BAFILOMYCINS | ALBICANS | SACCHAROMYCES-CEREVISIAE | Virulence - drug effects | Vacuolar Proton-Translocating ATPases - genetics | Fluconazole - pharmacology | Voriconazole - pharmacology | Humans | Drug Resistance, Fungal - physiology | Fungal Proteins - antagonists & inhibitors | Drug Resistance, Multiple, Fungal - physiology | Candidiasis - microbiology | Vacuolar Proton-Translocating ATPases - metabolism | Virulence - genetics | Candidiasis - drug therapy | Gene Deletion | Macrolides - pharmacology | Female | Genes, Fungal | Antifungal Agents - pharmacology | Candida glabrata - pathogenicity | Drug Resistance, Fungal - genetics | Fungal Proteins - genetics | Drug Synergism | Vacuolar Proton-Translocating ATPases - antagonists & inhibitors | Animals | Vacuoles - metabolism | Virulence - physiology | Mice | Mice, Inbred BALB C | Candida glabrata - enzymology | Candida glabrata - drug effects | Fungal Proteins - metabolism | Drug resistance in microorganisms | Candida | Analysis | Physiological aspects | Genetic aspects | Research | Virulence (Microbiology) | Adenosine triphosphatase | Candidiasis | Membranes | Yeast | Fungicides | Calcium | Calcineurin | Virulence | Calcineurin inhibitors | Homeostasis | Iron | Genomes | Biochemistry | Gene deletion | pH effects | Manganese ions | Fungi | Cell growth | Clonal deletion | Heterocyclic compounds | Voriconazole | University graduates | H+-transporting ATPase | Fluconazole | Multidrug resistance | Antifungal agents | Zinc | Environmental stress | Medicine | Azoles | Hospitals | Infectious diseases | Inhibitors | Tacrolimus | Amphotericin B | Reagents | Synergistic effect | Laboratory animals | Calcium ions
Journal Article
Nature reviews. Molecular cell biology, ISSN 1471-0080, 2002, Volume 3, Issue 2, pp. 94 - 103
Journal Article
Journal Article
The Journal of biological chemistry, ISSN 1083-351X, 2018, Volume 293, Issue 8, pp. 2787 - 2800
...+-ATPase (V-ATPase) complex, where it functions in proton translocation. In mammals, this subunit has four paralogous isoforms, a1-a4, which may encode signals for targeting assembled V-ATPases to specific intracellular locations... 
TOPOLOGY | TRANSPORT | ISOFORMS | N-LINKED GLYCOSYLATION | MEMBRANE | BIOCHEMISTRY & MOLECULAR BIOLOGY | COMPLEXES | ACIDIFICATION | OSTEOPETROSIS | VACUOLAR H+-ATPASE | Golgi Apparatus - enzymology | Vacuolar Proton-Translocating ATPases - genetics | Kidney - pathology | Humans | Kidney - enzymology | Protein Multimerization | Acidosis, Renal Tubular - genetics | Endoplasmic Reticulum - metabolism | Golgi Apparatus - pathology | Mutation, Missense | Recombinant Fusion Proteins - metabolism | Vacuolar Proton-Translocating ATPases - metabolism | Proton-Translocating ATPases - metabolism | Endoplasmic Reticulum - pathology | Kidney - metabolism | Proton-Translocating ATPases - genetics | Proteolysis | Acidosis, Renal Tubular - pathology | Cell Membrane - pathology | HEK293 Cells | Cell Membrane - metabolism | Protein Interaction Domains and Motifs | Cutis Laxa - metabolism | Endoplasmic Reticulum - enzymology | Enzyme Stability | Models, Molecular | Cutis Laxa - genetics | Glycosylation | Recombinant Fusion Proteins - chemistry | Acidosis, Renal Tubular - metabolism | Protein Transport | Proton-Translocating ATPases - chemistry | Cell Membrane - enzymology | Vacuolar Proton-Translocating ATPases - chemistry | Golgi Apparatus - metabolism | Protein Processing, Post-Translational | Proteasome Endopeptidase Complex - metabolism | Cutis Laxa - pathology | Amino Acid Substitution | Molecular Bases of Disease | 3D modeling | proton pump | ATPase | ER-associated degradation | membrane protein | trafficking | N-glycosylation | protein degradation
Journal Article
The Journal of experimental medicine, ISSN 1540-9538, 2017, Volume 214, Issue 12, pp. 3707 - 3729
The biogenesis of the multi-subunit vacuolar-type H+-ATPase (V-ATPase) is initiated in the endoplasmic reticulum with the assembly of the proton pore V0, which is controlled by a group of assembly factors... 
MEDICINE, RESEARCH & EXPERIMENTAL | RENIN/PRORENIN RECEPTOR | ENDOSOMAL TRAFFICKING | PRORENIN RECEPTOR | DROSOPHILA OPTIC LOBE | ABNORMAL PROTEIN GLYCOSYLATION | CONGENITAL DISORDERS | COGNITIVE IMPAIRMENT | ENDOPLASMIC-RETICULUM | IMMUNOLOGY | VACUOLAR H+-ATPASE | DEFICIENCY CAUSES | Endoplasmic Reticulum-Associated Degradation | Vacuolar Proton-Translocating ATPases - genetics | Brain - embryology | Liver - pathology | Humans | Liver Diseases - pathology | Infant | Male | Psychomotor Disorders - complications | Blood Proteins - metabolism | Drosophila Proteins - metabolism | Neural Stem Cells - cytology | Autophagy | Drosophila melanogaster - metabolism | Proton-Translocating ATPases - metabolism | Young Adult | Lipids - chemistry | Genes, X-Linked | Proton-Translocating ATPases - genetics | Base Sequence | Cutis Laxa - complications | Liver Diseases - complications | Receptors, Cell Surface - chemistry | Membrane Proteins - metabolism | Amino Acid Sequence | Membrane Proteins - genetics | Proton-Translocating ATPases - deficiency | Psychomotor Disorders - pathology | Receptors, Cell Surface - metabolism | Glycosylation | Fibroblasts - pathology | Mutation - genetics | Animals | Receptors, Cell Surface - deficiency | Vacuolar Proton-Translocating ATPases - chemistry | Adolescent | Brain - pathology | Protein Binding | Mice | Protein Processing, Post-Translational | Drosophila Proteins - genetics | Vacuolar Proton-Translocating ATPases - deficiency | Cutis Laxa - pathology | Neural Stem Cells - metabolism | Receptors, Cell Surface - genetics | TOR protein | Liver | Impairment | Acidification | Serum proteins | Defects | Proteins | Missense mutation | Renin | Rodents | Evolution | Lipid metabolism | Fat body | Assembly | H+-transporting ATPase | Liver diseases | Drosophila | Immunodeficiency | Rapamycin | Metabolism | Signaling | Skin | Mutation | Auditory defects | Endoplasmic reticulum | Adenosine triphosphatase | Phagocytosis | 316 | 310 | 321
Journal Article
Journal Article
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 10/2015, Volume 290, Issue 41, pp. 25045 - 25061
Journal Article