X
Search Filters
Format Format
Format Format
X
Sort by Item Count (A-Z)
Filter by Count
Journal Article (92123) 92123
Book Review (8014) 8014
Publication (7146) 7146
Book Chapter (956) 956
Conference Proceeding (369) 369
Dissertation (345) 345
Reference (57) 57
Book / eBook (35) 35
Web Resource (17) 17
Magazine Article (11) 11
Journal / eJournal (9) 9
Data Set (4) 4
Government Document (4) 4
Paper (3) 3
Trade Publication Article (3) 3
Newspaper Article (2) 2
Streaming Video (1) 1
more...
Subjects Subjects
Subjects Subjects
X
Sort by Item Count (A-Z)
Filter by Count
index medicus (69978) 69978
animals (44856) 44856
biochemistry & molecular biology (21298) 21298
humans (21029) 21029
atpase (17037) 17037
male (15567) 15567
rats (15539) 15539
sodium-potassium-exchanging atpase - metabolism (13215) 13215
cell biology (11037) 11037
kinetics (9283) 9283
calcium - metabolism (8901) 8901
female (8424) 8424
proteins (7452) 7452
physiology (7314) 7314
mice (7117) 7117
molecular sequence data (7022) 7022
calcium-transporting atpases - metabolism (6816) 6816
adenosine triphosphatases - metabolism (6625) 6625
adenosine triphosphatase (6534) 6534
amino acid sequence (6490) 6490
adenosine triphosphate - metabolism (5944) 5944
biophysics (5857) 5857
phosphorylation (5147) 5147
calcium (5109) 5109
expression (4896) 4896
proton-translocating atpases - metabolism (4816) 4816
mutation (4804) 4804
research (4802) 4802
in vitro techniques (4787) 4787
cells (4700) 4700
rabbits (4664) 4664
physiological aspects (4501) 4501
hydrogen-ion concentration (4384) 4384
binding sites (4378) 4378
protein binding (4291) 4291
analysis (4250) 4250
atpase activity (4188) 4188
cells, cultured (4081) 4081
pharmacology & pharmacy (4073) 4073
transport (3995) 3995
sodium-potassium-exchanging atpase - antagonists & inhibitors (3959) 3959
sodium - metabolism (3896) 3896
neurosciences (3735) 3735
plant sciences (3675) 3675
enzyme inhibitors - pharmacology (3660) 3660
ouabain - pharmacology (3637) 3637
protein (3635) 3635
gene expression (3556) 3556
protein conformation (3531) 3531
rats, wistar (3485) 3485
base sequence (3420) 3420
ca mg (3418) 3418
cell membrane - enzymology (3408) 3408
h+-atpase (3404) 3404
multidisciplinary sciences (3360) 3360
cell membrane - metabolism (3227) 3227
escherichia-coli (3183) 3183
rats, sprague-dawley (3178) 3178
models, molecular (3146) 3146
time factors (3098) 3098
article (3087) 3087
binding (3038) 3038
saccharomyces-cerevisiae (3028) 3028
life sciences (2979) 2979
hydrolysis (2960) 2960
cell line (2948) 2948
adult (2932) 2932
adenosine triphosphatases - genetics (2861) 2861
inhibition (2808) 2808
plasma-membrane (2762) 2762
dose-response relationship, drug (2721) 2721
enzymes (2713) 2713
microbiology (2707) 2707
potassium - metabolism (2700) 2700
models, biological (2686) 2686
na,k-atpase (2622) 2622
activation (2612) 2612
oxidative stress (2578) 2578
biology (2547) 2547
biochemistry (2524) 2524
homeostasis (2517) 2517
signal transduction (2498) 2498
sodium (2498) 2498
biological transport (2494) 2494
cattle (2464) 2464
myocardium - metabolism (2446) 2446
calcium-transporting atpases - antagonists & inhibitors (2404) 2404
gene (2340) 2340
mitochondria (2339) 2339
sarcoplasmic reticulum - enzymology (2329) 2329
genes (2320) 2320
proton-translocating atpases - genetics (2319) 2319
sarcoplasmic-reticulum (2313) 2313
mechanism (2280) 2280
ouabain (2276) 2276
sodium-potassium-exchanging atpase - genetics (2272) 2272
cardiac & cardiovascular systems (2209) 2209
rats, inbred strains (2197) 2197
middle aged (2178) 2178
identification (2164) 2164
more...
Library Location Library Location
Library Location Library Location
X
Sort by Item Count (A-Z)
Filter by Count
Gerstein Science - Stacks (19) 19
Online Resources - Online (9) 9
Earth Sciences (Noranda) - Stacks (3) 3
UTL at Downsview - May be requested (3) 3
UofT at Mississauga - Stacks (3) 3
Chemistry (A D Allen) - Stacks (1) 1
Collection Dvlpm't (Acquisitions) - Closed Orders (1) 1
Gerstein Science - Theses (1) 1
more...
Language Language
Language Language
X
Sort by Item Count (A-Z)
Filter by Count
English (89298) 89298
Russian (1394) 1394
Japanese (812) 812
Chinese (691) 691
French (254) 254
German (208) 208
Spanish (138) 138
Ukrainian (111) 111
Portuguese (93) 93
Korean (87) 87
Polish (61) 61
Italian (36) 36
Czech (28) 28
Slovak (21) 21
Dutch (15) 15
Hungarian (13) 13
Danish (9) 9
Finnish (5) 5
Serbian (5) 5
Bulgarian (4) 4
Croatian (4) 4
Norwegian (4) 4
Persian (3) 3
Romanian (3) 3
Turkish (3) 3
Afrikaans (1) 1
Arabic (1) 1
Hebrew (1) 1
Swedish (1) 1
more...
Publication Date Publication Date
Click on a bar to filter by decade
Slide to change publication date range


Journal of Experimental Biology, ISSN 0022-0949, 02/2017, Volume 220, Issue 3, pp. 425 - 436
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, 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 | MULTIDISCIPLINARY SCIENCES | AMINO-ACID SUBSTITUTIONS | ADENOSINE-TRIPHOSPHATASE | MITOCHONDRIAL ATPASE | SACCHAROMYCES-CEREVISIAE | 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 | Bacteria | Yeast | Adenosine triphosphatase | Crystal structure | Index Medicus | Biological Sciences | Physical Sciences
Journal Article
American Journal of Physiology - Regulatory, Integrative and Comparative Physiology, ISSN 0363-6119, 05/2007, Volume 292, Issue 5, pp. 2068 - 2076
Journal Article
Biochemical Journal, ISSN 0264-6021, 03/2006, Volume 394, Issue 3, pp. 605 - 615
The selective reversible S-glutathiolation of specific SERCA (sarcoplasmic/endoplasmic-reticulum Ca2+-ATPase) cysteine residues represents a novel physiologic... 
Sarcoplasmic/endoplasmic-reticulum Ca | ATPase (SERCA) | Cysteine oxidation | Sarcoplasmic reticulum | ATPase | Aging | Quantitative mapping | quantitative mapping | CALCIUM PUMPS | CANCER CELLS | sarcoplasmic/endoplasmic-reticulum | BIOCHEMISTRY & MOLECULAR BIOLOGY | S-GLUTATHIOLATION | Ca2+-ATPase | IDENTIFICATION | REACTIVE SULFHYDRYL-GROUPS | sarcoplasmic reticulum | SKELETAL-MUSCLE | CA2+-ATPASE SERCA | Ca2+-ATPase (SERCA) | CA-ATPASE | NITRIC-OXIDE | aging | cysteine oxidation | SARCOPLASMIC-RETICULUM ATPASE | Amino Acid Sequence | Calcium-Transporting ATPases - chemistry | Oxidation-Reduction | Rats | Chromatography, High Pressure Liquid | Cysteine - chemistry | Sarcoplasmic Reticulum Calcium-Transporting ATPases | Animals | Spectrometry, Mass, Electrospray Ionization | Time Factors | Staining and Labeling | Calcium-Transporting ATPases - metabolism | Cysteine - metabolism | Sarcoplasmic Reticulum - metabolism | Fluorescent Dyes | Aging - metabolism | Index Medicus | endoplasmic-reticulum Ca2+-ATPase (SERCA) | NAC, N-acetyl-L-cysteine | 3-NT, 3-nitrotyrosine | SR, sarcoplasmic reticulum | MS, tandem MS | CaM, calmodulin | ESI, electrospray ionization | SERCA, sarcoplasmic | a.m.u., atomic mass units | RP-HPLC, reversed-phase HPLC | 4-VP, 4-vinylpyridine | DTT, dithiothreitol | TG1, ThioGlo® 1 | endoplasmic-reticulum Ca2+-ATPase | sarcoplasmic | ER, endoplasmic reticulum
Journal Article
PLoS ONE, ISSN 1932-6203, 11/2013, Volume 8, Issue 11, pp. e78603 - e78603
The ATPase 6 accessory protein 2 (ATP6AP2)/(pro)renin receptor (PRR) is essential for the biogenesis of active vacuolar H+-ATPase (V-ATPase). Genetic deletion... 
V-ATPASE | MEMBRANE SECTOR | PRORENIN RECEPTOR | NONPROTEOLYTIC ACTIVATION | MULTIDISCIPLINARY SCIENCES | PRO RENIN RECEPTOR | ENDOPLASMIC-RETICULUM | ANGIOTENSIN-II | (PRO)RENIN RECEPTOR | OSTEOCLAST DIFFERENTIATION | SACCHAROMYCES-CEREVISIAE | RNA, Small Interfering - genetics | Vacuolar Proton-Translocating ATPases - genetics | Embryo, Mammalian | Humans | Receptors, Cell Surface - antagonists & inhibitors | Vacuolar Proton-Translocating ATPases - metabolism | Proton-Translocating ATPases - metabolism | trans-Golgi Network - metabolism | Protein Isoforms - metabolism | Proton-Translocating ATPases - genetics | Transfection | Protein Isoforms - chemistry | Adenoviridae - genetics | Receptors, Cell Surface - chemistry | Autophagy - genetics | Proton-Translocating ATPases - antagonists & inhibitors | Fibroblasts - metabolism | Furin - metabolism | Protein Structure, Tertiary | Recombinant Proteins - metabolism | Gene Expression | Receptors, Cell Surface - metabolism | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Proton-Translocating ATPases - chemistry | Vacuolar Proton-Translocating ATPases - antagonists & inhibitors | Animals | Vacuolar Proton-Translocating ATPases - chemistry | Fibroblasts - cytology | Mice | Adenoviridae - metabolism | Mutation | Primary Cell Culture | Genetic Vectors | Protein Isoforms - genetics | RNA, Small Interfering - metabolism | Receptors, Cell Surface - genetics | Shedding | Basal ganglia | Nephrology | Hydrogen | Acidification | Amino acids | Biosynthesis | Kinases | Deletion mutant | Proteins | Renin | Clonal deletion | Deletion | Furin | Cleavage | Cardiology | Movement disorders | H+-transporting ATPase | Hypertension | Internal medicine | Spasticity | Central nervous system diseases | Metabolism | Golgi apparatus | Medicine | Endoplasmic reticulum | Adenosine triphosphatase | Endocrinology | Index Medicus
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 09/2012, Volume 287, Issue 39, pp. 32717 - 32727
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 2018, Volume 293, Issue 8, pp. 2787 - 2800
The a subunit is the largest of 15 different subunits that make up the vacuolar H+-ATPase (V-ATPase) complex, where it functions in proton translocation. In... 
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 | Index Medicus | Molecular Bases of Disease | 3D modeling | proton pump | ATPase | ER-associated degradation | membrane protein | trafficking | N-glycosylation | protein degradation
Journal Article
Toxicon, ISSN 0041-0101, 09/2015, Volume 103, pp. 80 - 84
Journal Article
Journal of Experimental Medicine, ISSN 0022-1007, 12/2017, 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... 
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 | Index Medicus | 316 | 310 | 321
Journal Article