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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
Summary Background The gastric H+,K+‐ATPase is the preferred target for acid suppression. Until recently, the only drugs that effectively inhibited this ATPase... 
ESOMEPRAZOLE | INHIBITION | H+/K+-ATPASE | COMPETITIVE ACID BLOCKER | RANDOMIZED CLINICAL-TRIAL | H,K-ATPASE | HEALTHY MALE-SUBJECTS | PHARMACOLOGY & PHARMACY | SECRETION | MONOFUMARATE TAK-438 | GASTROENTEROLOGY & HEPATOLOGY | PROTON PUMP | 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 | 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 is a widely used, reversible means of regulating enzymatic activity. Among the important phosphorylation targets are the Na ,K - and H ,K... 
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 | PROTEIN-KINASE-C | DEPENDENT PHOSPHORYLATION | ALPHA-SUBUNIT | ALVEOLAR EPITHELIAL-CELLS | INDUCED ENDOCYTOSIS | BIOCHEMISTRY & MOLECULAR BIOLOGY | INTRACELLULAR NA+ | SODIUM-POTASSIUM PUMP | PLASMA-MEMBRANE | NA-K-ATPASE | CELL BIOLOGY | BIOPHYSICS | PKA PHOSPHORYLATION | 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 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
In rodents and humans, aromatic amino acids increase gut hormone secretion and H -K -ATPase activity by modulating calcium-sensing receptor (CaSR). However,... 
l-Tryptophan | Pig stomach | Gastrin | H+-K+-ATPase | Calcium-sensing receptor | Somatostatin | l-Phenylalanine | L-Phenylalanine | ATPase | L-Tryptophan | ENTEROENDOCRINE STC-1 CELLS | ACID-SECRETION | GASTROINTESTINAL-TRACT | GUT | RELEASE | PEPTIDE | CHOLECYSTOKININ SECRETION | AMINO-ACIDS | ENDOCRINOLOGY & METABOLISM | STOMACH | CA2+-SENSING RECEPTOR | Central Nervous System Stimulants | Animals | H(+)-K(+)-Exchanging ATPase - metabolism | Phenylalanine - metabolism | Swine | Humans | Gastrins - metabolism | Receptors, Calcium-Sensing - metabolism | Somatostatin - metabolism | Tryptophan - metabolism
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4. 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
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5. 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
Ghrelin is implicated in the regulation of gastric functional development. The octanoylation of ghrelin is critical for its physiological functions which... 
GOAT | H+–K+-ATPase activity | Total ghrelin | Acylated ghrelin | ATPase activity | ACID-SECRETION | H+-K+-ATPase activity | RATS | GLUCOSE | ENDOCRINOLOGY & METABOLISM | MICE | EXPRESSION | STOMACH | MOTILITY | ACTS | 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
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6. Full Text Airway acidification initiates host defense abnormalities in cystic fibrosis mice
by Shah, Viral S and Meyerholz, David K and Tang, Xiao Xiao and Reznikov, Leah and Alaiwa, Mahmoud Abou and Ernst, Sarah E and Karp, Philip H and Wohlford-Lenane, Christine L and Heilmann, Kristopher P and Leidinger, Mariah R and Allen, Patrick D and Zabner, Joseph and McCray, Paul B and Ostedgaard, Lynda S and Stoltz, David A and Randak, Christoph O and Welsh, Michael J
Science, ISSN 0036-8075, 01/2016, Volume 351, Issue 6272, pp. 503 - 507
Cystic fibrosis (CF) is caused by mutations in the gene that encodes the cystic fibrosis transmembrane conductance regulator (CFTR) anion channel. In humans... 
CELLS | TRANSPORT | SURFACE PH | LIQUID PH | EPITHELIUM | CHANNEL | MULTIDISCIPLINARY SCIENCES | DISEASE | BASE SECRETION | MODEL | BICARBONATE SECRETION | Lung - microbiology | H(+)-K(+)-Exchanging ATPase - metabolism | Mice, Inbred CFTR - genetics | Cystic Fibrosis - metabolism | Cystic Fibrosis - microbiology | Mice, Inbred CFTR - metabolism | Humans | Mice, Transgenic | H(+)-K(+)-Exchanging ATPase - genetics | Acids - metabolism | Animals | Swine | Bicarbonates - metabolism | Lung - metabolism | Mice | Hydrogen-Ion Concentration | Cystic fibrosis | Genetic aspects | Gene expression | Observations | Health aspects | Airway (Medicine) | Acidification | Mutation | Pathogenesis | Rodents
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7. Full Text Letter: vonoprazan, a long‐lasting acid suppressor of the gastric H+, K+‐ATPases with ‐ implications for renal H+, K+‐ATPases; authors' reply
by Sachs, G and Scott, D. R
Alimentary Pharmacology & Therapeutics, ISSN 0269-2813, 02/2016, Volume 43, Issue 3, pp. 443 - 443
Pyrroles - metabolism | Proton Pump Inhibitors - pharmacology | Animals | H(+)-K(+)-Exchanging ATPase - metabolism | Sulfonamides - metabolism | Male | Stomach - metabolism | Adenosine triphosphatase
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8. 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
Journal of Pharmacology and Experimental Therapeutics, ISSN 0022-3565, 11/2011, Volume 339, Issue 2, pp. 412 - 420
Inhibition of the gastric H, K-ATPase by the potassium-competitive acid blocker (P-CAB)... 
ESOMEPRAZOLE | LANSOPRAZOLE | GASTROESOPHAGEAL-REFLUX DISEASE | VESICLES | ATPASE | PROTON PUMP INHIBITOR | MEMBRANES | PHARMACOLOGY & PHARMACY | SECRETION | BINDING-SITES | H+,K+-ATPASE | 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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9. Full Text KFP-H008 blocks gastric acid secretion through inhibiting H+-K+-ATPase
by Li, Cheng-yuan and Li, Yun-man and Su, Mei and Yan, Yun-yi and Zhou, Lin and Ao, Lu-yao and Fang, Wei-rong
European Journal of Pharmacology, ISSN 0014-2999, 09/2017, Volume 810, pp. 112 - 119
1-(5-(1H-indol-5-yl)-1-(pyridin-3-ylsulfonyl)-1H-pyrrol-3-yl)-N-methylmethanamine (KFP-H008)，a novel and potent potassium-competitive acid blocker for the... 
H+-K+-ATPase | Gastric acid secretion | Potassium-competitive acid blocker | Proton pump inhibitor | ATPase | Potassium - metabolism | Gastric Acid - secretion | Proton Pump Inhibitors - pharmacology | Pyrroles - pharmacology | Animals | H(+)-K(+)-Exchanging ATPase - metabolism | Histamine - pharmacology | Rats | Male | Rats, Sprague-Dawley
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10. 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
Highlights • shGhrelin inhibited ghrelin mRNA expression via an RNAi mechanism. • shGhrelin reduced total and acylated ghrelin production and secretion ( P <... 
Endocrinology & Metabolism | shGhrelin | GOAT | H+–K+-ATPase activity | Acylated ghrelin | ShGhrelin | ATPase activity | ACID-SECRETION | H+-K+-ATPase activity | RATS | O-ACYLTRANSFERASE GOAT | PEPTIDE | MUCOSAL CELLS | HORMONE | ENDOCRINOLOGY & METABOLISM | MICE | STOMACH | MOTILITY | ACTS | 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
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11. Full Text Modulations in extracellular calcium lead to H+-atpase-dependent acid secretion: A clarification of PPI failure
by Kitay, Alice Miriam and Schneebacher, Marie-Therese and Schmitt, Anne and Heschl, Katharina and Kopic, Sascha and Alfadda, Tariq and Alsaihati, Abrar and Link, Alexander and Geibel, John Peter
American Journal of Physiology - Gastrointestinal and Liver Physiology, ISSN 0193-1857, 07/2018, Volume 315, Issue 1, pp. G36 - G42
The H+, K+-ATPase was identified as the primary proton secretory pathway in the gastric parietal cell and is the pharmacological target of agents suppressing... 
CELLS | RABEPRAZOLE | gastric gland | PHYSIOLOGY | BREAKTHROUGH | SENSING RECEPTOR | proton pumps | GASTROINTESTINAL-TRACT | PARIETAL | stomach | PEPTIC-ULCER DISEASE | parietal cells | GASTRIC GLANDS | GASTROESOPHAGEAL-REFLUX | acid secretion | PUMP INHIBITOR THERAPY | GASTROENTEROLOGY & HEPATOLOGY | Proton Pump Inhibitors - pharmacology | H(+)-K(+)-Exchanging ATPase - metabolism | Calcium - metabolism | Rats | Enzyme Activation - drug effects | Receptors, Calcium-Sensing - metabolism | Rats, Sprague-Dawley | Proton Pumps - metabolism | Calcium - blood | Carbachol - pharmacology | Histamine - metabolism | Proton Pumps - drug effects | Secretory Pathway - drug effects | Secretory Pathway - physiology | Animals | Parietal Cells, Gastric - drug effects | Ion Transport - drug effects | Parietal Cells, Gastric - physiology | Gastric Acid - metabolism | Ion Transport - physiology | Enzyme Activation - physiology | Cholinergic Agonists - pharmacology
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12. 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
P-type ATPases are ATP-powered ion pumps, classified into five subfamilies (PI–PV). Of these, PII-type ATPases, including Ca -ATPase, Na ,K -ATPase and gastric... 
COARSE-GRAINED SIMULATIONS | P-TYPE ATPASES | GASTRIC H+,K+-ATPASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | CATION-BINDING | NA+/K+-ATPASE | CALCIUM-PUMP | CARDIOTONIC STEROIDS | BINDING-SITES | SODIUM-POTASSIUM PUMP | SARCOPLASMIC-RETICULUM ATPASE | 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
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13. 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 - European Journal of Physiology, ISSN 0031-6768, 10/2016, Volume 468, Issue 10, pp. 1673 - 1683
In industrialized countries, a large part of the population is daily exposed to low K+ intake, a situation correlated with the development of salt-sensitive... 
Biomedicine | Human Physiology | Low-K + diet | Na + /Cl − -cotransporter | Blood pressure | Extracellular volume | Vasopressin | Low-K | Cl | diet | cotransporter | HOSPITALIZED-PATIENTS | HOMEOSTASIS | PHYSIOLOGY | TRANSPORTERS | BLOOD-PRESSURE | HYPOKALEMIA | POTASSIUM-DEPLETION | MICE | Low-K+ diet | DIETARY K | Na+/Cl--cotransporter | SODIUM-CHLORIDE COTRANSPORTER | 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
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14. Full Text Substituted methoxybenzyl-sulfonyl-1H-benzo[d]imidazoles evaluated as effective H+/K+-ATPase inhibitors and anti-ulcer therapeutics
by Rajesh, R and Manikandan, A and Sivakumar, A and Ramasubbu, C and Nagaraju, N
European Journal of Medicinal Chemistry, ISSN 0223-5234, 10/2017, Volume 139, pp. 454 - 460
Efforts were made to synthesize a series of substituted methoxybenzyl-sulfonyl- -benzo[d]imidazole derivatives ( ) and investigate their anti-ulcer... 
H+/K+-ATPase | SAR | Benzimidazole | Molecular docking | Anti-ulcer | ATPase | DESIGN | CHEMISTRY, MEDICINAL | BENZIMIDAZOLE DERIVATIVES | OMEPRAZOLE | ANTICONVULSANT | PUMP | ANTICANCER | AGENTS | PHARMACOLOGICAL EVALUATION | Proton Pump Inhibitors - pharmacology | Stomach Ulcer - metabolism | H(+)-K(+)-Exchanging ATPase - metabolism | Goats | Benzimidazoles - chemical synthesis | Stomach Ulcer - drug therapy | Structure-Activity Relationship | Benzimidazoles - chemistry | Dose-Response Relationship, Drug | Animals | Anti-Ulcer Agents - chemistry | Proton Pump Inhibitors - chemistry | Anti-Ulcer Agents - chemical synthesis | Anti-Ulcer Agents - pharmacology | Benzimidazoles - pharmacology | Proton Pump Inhibitors - chemical synthesis | Molecular Structure | Index Medicus
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