Ho Jung Shin
Kyorin University
9 Papers
39 Citations
Ho Jung Shin is an academic researcher from Kyorin University. The author has contributed to research in topics: Organic anion transporter 1 & Transporter. The author has an hindex of 8, co-authored 8 publications.
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Papers
Molecular identification of a novel carnitine transporter specific to human testis. Insights into the mechanism of carnitine recognition.
Atsushi Enomoto,Michael F. Wempe,Hiroki Tsuchida,Ho Jung Shin,Seok Ho Cha,Naohiko Anzai,Akiteru Goto,Atsuhiko Sakamoto,Toshimitsu Niwa,Yoshikatsu Kanai,M. W. Anders,Hitoshi Endou +11 more
TL;DR: The identification of CT2 represents an interesting evolutionary link between OCT/OCTNs and OATs, as well as provides an important insight into the maturation of human spermatozoa.
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Interactions of Human Organic Anion Transporters with Diuretics
Habib Hasannejad,Michio Takeda,Kentarou Taki,Ho Jung Shin,Ellappan Babu,Promsuk Jutabha,Suparat Khamdang,Mahmoud Aleboyeh,Maristela L. Onozato,Akihiro Tojo,Atsushi Enomoto,Naohiko Anzai,Shinichi Narikawa,Xiu-Lin Huang,Toshimitsu Niwa,Hitoshi Endou +15 more
TL;DR: HOAT1 may play an important role in the basolateral uptake of thiazides, and hOAT3 in the uptake of loop diuretics, and it was suggested that bumetanide taken up by hO AT3 and/or hOat1 is excreted into the urine by h OAT4.
Novel liver-specific organic anion transporter OAT7 that operates the exchange of sulfate conjugates for short chain fatty acid butyrate†
Ho Jung Shin,Naohiko Anzai,Atsushi Enomoto,Xin He,Do Kyung Kim,Hitoshi Endou,Yoshikatsu Kanai +6 more
TL;DR: OAT7 is the first liver‐specific transporter among members of the organic anion transporters of SLC22 family and provides evidence for the transport of anionic substances such as sulfate‐conjugates in exchange for butyrate in hepatocytes.
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Novel single nucleotide polymorphisms of organic cation transporter 1 (SLC22A1) affecting transport functions.
Takeshi Sakata,Naohiko Anzai,Ho Jung Shin,Rie Noshiro,Taku Hirata,Hirokazu Yokoyama,Yoshikatsu Kanai,Hitoshi Endou +7 more
TL;DR: It is suggested that the newly found OCT1 variants will contribute to inter-individual variations leading to the differences in cationic drug disposition and perhaps certain disease processes.
110
Modulation of Renal Apical Organic Anion Transporter 4 Function by Two PDZ Domain–Containing Proteins
Hiroki Miyazaki,Naohiko Anzai,Sophapun Ekaratanawong,Takeshi Sakata,Ho Jung Shin,Promsuk Jutabha,Taku Hirata,Xin He,Hiroshi Nonoguchi,Kimio Tomita,Yoshikatsu Kanai,Hitoshi Endou +11 more
TL;DR: The functional activity of OAT4 is modulated through the PDZ interaction with the network of PDZK1 and NHERF1 and suggests that Oat4 is involved in the regulated apical organic anion handling in the renal proximal tubules, provided by the PDz scaffold.
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