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1. Full Text The binding selectivity of vonoprazan (TAK‐438) to the gastric H+,K+‐ATPase
by Scott, D. R and Munson, K. B and Marcus, E. A and Lambrecht, N. W. G and Sachs, G
Alimentary pharmacology & therapeutics, ISSN 0269-2813, 12/2015, Volume 42, Issue 11-12, pp. 1315 - 1326
Gastroenterology & Hepatology | Pharmacology & Pharmacy | Life Sciences & Biomedicine | Science & Technology | Pyrroles - metabolism | Rabbits | Proton Pump Inhibitors - pharmacology | H(+)-K(+)-Exchanging ATPase - metabolism | Half-Life | Parietal Cells, Gastric - metabolism | Male | Stomach - metabolism | Gastric Mucosa - metabolism | Animals | Gastric Mucosa - drug effects | Sulfonamides - metabolism | Gastric Acid - metabolism | Proton pump inhibitors | Pyridine | Chemical properties | Adenosine triphosphatase | Index Medicus | H+,K+-ATPase | parietal cell | vonoprazan | molecular modeling | TAK-438
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2. Full Text Phosphorylation of the Na +,K +-ATPase and the H +,K +-ATPase
by Poulsen, Hanne and Morth, Preben and Egebjerg, Jan and Nissen, Poul
FEBS letters, ISSN 0014-5793, 2010, Volume 584, Issue 12, pp. 2589 - 2595
Phosphorylation | H +,K +-ATPase | Protein kinase C | cAMP activated protein kinase | Na +,K +-ATPase | Na+,K+-ATPase | H+,K+-ATPase | ATPase | CAMP activated protein kinase | Biochemistry & Molecular Biology | Biophysics | Life Sciences & Biomedicine | Science & Technology | Cell Biology | Amino Acid Sequence | Protein Subunits | Sodium-Potassium-Exchanging ATPase - genetics | H(+)-K(+)-Exchanging ATPase - metabolism | Mutagenesis, Site-Directed | Sodium-Potassium-Exchanging ATPase - chemistry | Humans | Models, Molecular | Molecular Sequence Data | Crystallography, X-Ray | H(+)-K(+)-Exchanging ATPase - genetics | Sequence Homology, Amino Acid | Sodium-Potassium-Exchanging ATPase - metabolism | Animals | H(+)-K(+)-Exchanging ATPase - chemistry | Models, Biological | Electrophysiological Phenomena | Binding Sites | Amino Acid Substitution | Index Medicus
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3. Full Text Circadian expression of H,K‐ATPase type 2 contributes to the stability of plasma K+ levels
by Salhi, Amel and Centeno, Gabriel and Firsov, Dmitri and Crambert, Gilles
The FASEB journal, ISSN 0892-6638, 07/2012, Volume 26, Issue 7, pp. 2859 - 2867
epithelial ion transport | electrolyte | diurnal variation | potassium balance | Epithelial ion transport | Potassium balance | Diurnal variation | Electrolyte | Biochemistry & Molecular Biology | Biology | Life Sciences & Biomedicine - Other Topics | Life Sciences & Biomedicine | Science & Technology | Cell Biology | H(+)-K(+)-Exchanging ATPase - metabolism | Mice, Inbred C57BL | Circadian Rhythm - genetics | Homeostasis | Potassium, Dietary - administration & dosage | CLOCK Proteins - genetics | Circadian Rhythm - physiology | H(+)-K(+)-Exchanging ATPase - genetics | H(+)-K(+)-Exchanging ATPase - classification | CLOCK Proteins - deficiency | Mice, Knockout | Gene Expression Regulation, Enzymologic | CLOCK Proteins - metabolism | Kidney - metabolism | Animals | NF-E2-Related Factor 2 - metabolism | Potassium - urine | Potassium - blood | Mice | H(+)-K(+)-Exchanging ATPase - deficiency | Index Medicus
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4. Full Text Phenylalanine and tryptophan stimulate gastrin and somatostatin secretion and H+-K+-ATPase activity in pigs through calcium-sensing receptor
by Xian, Yihan and Zhao, Xiuying and Wang, Chao and Kang, Cuicui and Ding, Liren and Zhu, Weiyun and Hang, Suqin
General and comparative endocrinology, ISSN 0016-6480, 10/2018, Volume 267, pp. 1 - 8
l-Tryptophan | Pig stomach | Gastrin | H+-K+-ATPase | Calcium-sensing receptor | Somatostatin | l-Phenylalanine | L-Phenylalanine | ATPase | L-Tryptophan | Life Sciences & Biomedicine | Endocrinology & Metabolism | Science & Technology | Central Nervous System Stimulants | Animals | H(+)-K(+)-Exchanging ATPase - metabolism | Phenylalanine - metabolism | Swine | Humans | Gastrins - metabolism | Receptors, Calcium-Sensing - metabolism | Somatostatin - metabolism | Tryptophan - metabolism | Index Medicus
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5. Full Text H,K-ATPase type 2 contributes to salt-sensitive hypertension induced by K+ restriction
by Walter, Christine and Tanfous, Mariem Ben and Igoudjil, Katia and Salhi, Amel and Escher, Geneviève and Crambert, Gilles
Pflügers Archiv, ISSN 0031-6768, 10/2016, Volume 468, Issue 10, pp. 1673 - 1683
Biomedicine | Human Physiology | Low-K + diet | Na + /Cl − -cotransporter | Blood pressure | Extracellular volume | Vasopressin | Low-K | Na | Cl | diet | cotransporter | Life Sciences & Biomedicine | Physiology | Science & Technology | Blood Pressure | Potassium - metabolism | H(+)-K(+)-Exchanging ATPase - metabolism | Mice, Inbred C57BL | H(+)-K(+)-Exchanging ATPase - genetics | Vasopressins - blood | Hypertension - etiology | Hypertension - metabolism | Dinoprostone - metabolism | Kidney - metabolism | Animals | Potassium Deficiency - complications | Potassium Deficiency - metabolism | Potassium - blood | Mice | Solute Carrier Family 12, Member 3 - metabolism | Index Medicus
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6. Characterization of a novel potassium-competitive acid blocker of the gastric H,K-ATPase,1-[5-(2-fluorophenyl)-1-(pyridin-3-ylsulfonyl)-1H-pyrrol-3- yl]-N-methylmethanamine monofumarate (TAK-438)
by Shin, Jai Moo and Inatomi, Nobuhiro and Munson, Keith and Strugatsky, David and Tokhtaeva, Elmira and Vagin, Olga and Sachs, George
The Journal of pharmacology and experimental therapeutics, ISSN 0022-3565, 11/2011, Volume 339, Issue 2, pp. 412 - 420
Life Sciences & Biomedicine | Pharmacology & Pharmacy | Science & Technology | Acridine Orange - metabolism | Proton Pump Inhibitors - pharmacology | Stereoisomerism | Humans | Fluorescent Dyes - metabolism | Molecular Targeted Therapy | Proton Pump Inhibitors - analysis | H(+)-K(+)-Exchanging ATPase - chemistry | Swine | HEK293 Cells | Phosphorylation - drug effects | Gastroesophageal Reflux - drug therapy | Stomach - drug effects | Pyrroles - metabolism | H(+)-K(+)-Exchanging ATPase - metabolism | Sulfonamides - chemistry | Models, Molecular | Sulfonamides - pharmacology | Pyrroles - pharmacology | Animals | Proton Pump Inhibitors - chemistry | Stomach - enzymology | Sulfonamides - metabolism | Protein Binding | Pyrroles - chemistry | Software
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7. Full Text RNAi-mediated Ghrelin affects gastric H+ –K+ -ATPase activity and expression of GOAT–Ghrelin system in vitro
by Du, Gai M and Wu, Jie G and Luo, Bi P and Hu, Zhi H and Li, Liu A and Liu, Mao J
General and comparative endocrinology, ISSN 0016-6480, 2016, Volume 228, pp. 48 - 52
Endocrinology & Metabolism | shGhrelin | GOAT | H+–K+-ATPase activity | Acylated ghrelin | ShGhrelin | ATPase activity | Life Sciences & Biomedicine | Science & Technology | RNA, Small Interfering - genetics | H(+)-K(+)-Exchanging ATPase - metabolism | RNA, Messenger - genetics | Cells, Cultured | Gene Expression Regulation | Ghrelin - genetics | H(+)-K(+)-Exchanging ATPase - genetics | Acyltransferases - metabolism | Gastric Mucosa - metabolism | Reverse Transcriptase Polymerase Chain Reaction | Acyltransferases - genetics | Ghrelin - antagonists & inhibitors | Ghrelin - metabolism | Animals | RNA Interference | Swine | In Vitro Techniques | Real-Time Polymerase Chain Reaction | Index Medicus
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8. Full Text The effect of ghrelin O-acyltransferase inhibitor on gastric H+–K+-ATPase activity and GOAT/ghrelin system in gastric mucosal cells in vitro
by Du, Gai Mei and Luo, Bi Ping and Hu, Zhi Hua and Wu, Jie Ge and Yan, Wen Mei and Han, Zheng Qiang and Zhang, Yu Hong and Liu, Mao Jun
General and comparative endocrinology, ISSN 0016-6480, 10/2018, Volume 267, pp. 167 - 171
GOAT | H+–K+-ATPase activity | Total ghrelin | Acylated ghrelin | ATPase activity | Life Sciences & Biomedicine | Endocrinology & Metabolism | Science & Technology | Acyltransferases - antagonists & inhibitors | Cell Line | H(+)-K(+)-Exchanging ATPase - metabolism | RNA, Messenger - genetics | Enzyme Inhibitors - pharmacology | Gastric Mucosa - enzymology | Gastric Mucosa - cytology | Acyltransferases - metabolism | RNA, Messenger - metabolism | Acyltransferases - genetics | Peptides - pharmacology | Ghrelin - metabolism | Animals | Culture Media | Mice | Index Medicus
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9. Full Text Positive regulation of the enzymatic activity of gastric H+,K+-ATPase by sialylation of its β-subunit
by Fujii, Takuto and Watanabe, Midori and Shimizu, Takahiro and Takeshima, Hiroshi and Kushiro, Keiichiro and Takai, Madoka and Sakai, Hideki
Biochimica et biophysica acta. Biomembranes, ISSN 0005-2736, 06/2016, Volume 1858, Issue 6, pp. 1228 - 1235
H+,K+-ATPase | Sialic acid | Glycosylation | Gastric acid | Neuraminidase | Biochemistry & Molecular Biology | Biophysics | Life Sciences & Biomedicine | Science & Technology | LLC-PK1 Cells | Animals | H(+)-K(+)-Exchanging ATPase - chemistry | H(+)-K(+)-Exchanging ATPase - metabolism | Swine | Stomach - enzymology | Famotidine - pharmacology | Stomach - drug effects | N-Acetylneuraminic Acid - metabolism
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10. Full Text Letter: vonoprazan, a long‐lasting acid suppressor of the gastric H+, K+‐ATPases with ‐ implications for renal H+, K+‐ATPases
by Srinivas, N. R
Alimentary pharmacology & therapeutics, ISSN 0269-2813, 02/2016, Volume 43, Issue 3, pp. 442 - 443
Pyrroles - metabolism | Proton Pump Inhibitors - pharmacology | Animals | H(+)-K(+)-Exchanging ATPase - metabolism | Sulfonamides - metabolism | Male | Stomach - metabolism | Adenosine triphosphatase | Index Medicus
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11. Full Text New crystal structures of PII-type ATPases: excitement continues
by Toyoshima, Chikashi and Cornelius, Flemming
Current opinion in structural biology, ISSN 0959-440X, 08/2013, Volume 23, Issue 4, pp. 507 - 514
Biochemistry & Molecular Biology | Life Sciences & Biomedicine | Science & Technology | Cell Biology | Calcium-Binding Proteins - metabolism | Sarcoplasmic Reticulum Calcium-Transporting ATPases - metabolism | H(+)-K(+)-Exchanging ATPase - metabolism | Proteolipids - metabolism | Crystallography, X-Ray | H(+)-K(+)-Exchanging ATPase - ultrastructure | Sodium-Potassium-Exchanging ATPase - ultrastructure | Sarcoplasmic Reticulum - enzymology | Sarcoplasmic Reticulum Calcium-Transporting ATPases - ultrastructure | Sodium-Potassium-Exchanging ATPase - metabolism | Animals | Muscle Proteins - metabolism | Protein Binding | Sarcoplasmic Reticulum - metabolism | Binding Sites | Structure | Adenosine triphosphatase | Crystals | Index Medicus
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