Involvement of the H3O+-Lys-164 -Gln-161-Glu-345 Charge Transfer Pathway in Proton Transport of Gastric H+,K+-ATPase-Reference-Cited by-同舟云学术

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Involvement of the H3O+-Lys-164 -Gln-161-Glu-345 Charge Transfer Pathway in Proton Transport of Gastric H+,K+-ATPase

Published:2008-06 Issue:24 Volume:283 Page:16876-16884
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Morii Magotoshi,Yamauchi Masashi,Ichikawa Tomohiko,Fujii Takuto,Takahashi Yuji,Asano Shinji,Takeguchi Noriaki,Sakai Hideki

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference38 articles.

1. Structural basis for E1–E2 conformational transitions in Na, K-pump and Ca-pump proteins

2. Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 Å resolution

3. Lumenal gating mechanism revealed in calcium pump crystal structures with phosphate analogues

4. Crystal structure of the sodium–potassium pump

5. Crystal structure of the plasma membrane proton pump

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1. Effects of Proton Pump Inhibitors on Serum Calcium Level: A Study on Rabbit Model;Journal of Pharmaceutical Research International;2021-09-07

2. Paradoxical relationship between proton pump inhibitors and COVID-19: A systematic review and meta-analysis;World Journal of Clinical Cases;2021-04-26

3. Positive regulation of the enzymatic activity of gastric H + ,K + -ATPase by sialylation of its β-subunit;Biochimica et Biophysica Acta (BBA) - Biomembranes;2016-06

4. Long-Range Electrostatics-Induced Two-Proton Transfer Captured by Neutron Crystallography in an Enzyme Catalytic Site;Angewandte Chemie International Edition;2016-03-09

5. Long-Range Electrostatics-Induced Two-Proton Transfer Captured by Neutron Crystallography in an Enzyme Catalytic Site;Angewandte Chemie;2016-03-09

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