Boric acid transport activity of human aquaporins expressed in <i>Xenopus</i> oocytes-Reference-Cited by-同舟云学术

Boric acid transport activity of human aquaporins expressed in Xenopus oocytes

Published:2022-01 Issue:1 Volume:10 Page:
ISSN:2051-817X
Container-title:Physiological Reports
language:en
Short-container-title:Physiological Reports

Author:

Ushio Kazutaka¹^ORCID,Watanabe Erika¹,Kamiya Takehiro²,Nagashima Ayumi¹^ORCID,Furuta Tadaomi¹^ORCID,Imaizumi Genki¹,Fujiwara Toru²,Romero Michael F.³⁴⁵^ORCID,Kato Akira¹³⁶^ORCID

Affiliation:

1. School of Life Science and Technology Tokyo Institute of Technology Yokohama Japan

2. Department of Applied Biological Chemistry Graduate School of Agricultural and Life Sciences The University of Tokyo Tokyo Japan

3. Department of Physiology and Biomedical Engineering Mayo Clinic College of Medicine & Science Rochester Minnesota USA

4. Nephrology and Hypertension Mayo Clinic College of Medicine & Science Rochester Minnesota USA

5. O’Brien Urology Research Center Mayo Clinic College of Medicine & Science Rochester Minnesota USA

6. Center for Biological Resources and Informatics Tokyo Institute of Technology Yokohama Japan

Funder

Mayo Foundation for Medical Education and Research

Foundation for the National Institutes of Health

Japan Society for the Promotion of Science

Publisher

Wiley

Subject

Physiology (medical),Physiology

Link

https://onlinelibrary.wiley.com/doi/pdf/10.14814/phy2.15164

Reference53 articles.

1. Aquaporin water channels – from atomic structure to clinical medicine

2. The Aquaporin Splice Variant NbXIP1;1α Is Permeable to Boric Acid and Is Phosphorylated in the N-terminal Domain

3. Human Aquaporins: Functional Diversity and Potential Roles in Infectious and Non-infectious Diseases

4. Point mutations in the aromatic/arginine region in aquaporin 1 allow passage of urea, glycerol, ammonia, and protons

5. BORON IN PLANT STRUCTURE AND FUNCTION

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