Author

P. Wiriyasermkul

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biochemistry· 4

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Organism:human· 3 Research Focus:protein structure prediction· 2 Assay:structural biology· 2 Organism:bacteria (other)· 1 Research Focus:cell type annotation· 1 Assay:cryo-EM· 1 Research Focus:host-pathogen & immune response· 1

Frequent Co-Authors

S. Nagamori· 3 shared S. Moriyama· 2 shared Y. Lee· 2 shared A. Matsuda· 1 shared C. Jin· 1 shared D. J. Mills· 1 shared E. G. Iturbe· 1 shared H. Endou· 1 shared

Activity by Year

2019-2021 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 17 mutual co-author links

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3 shared papersBiochemistry

S. Nagamori

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4 papers

Recent·Most cited

Insight into the mechanism of H+-coupled nucleobase transport

J. Weng, X. Zhou, P. Wiriyasermkul, Z. Ren, X. Yan, K. Chen, E. G. Iturbe, M. Zhou, M. Quick

The paper reports the structure and function of PurTCp, a NAT family transporter from Colwellia psychrerythraea, showing it transports purines via H+-dependent mechanism and identifies a critical aspartate residue.

bioRxiv · Dec 20, 2021 · PreprintBiochemistry

Ca2+-mediated higher-order assembly of b0,+AT-rBAT is a key step for system b0,+ biogenesis and cystinuria

Y. Lee, P. Wiriyasermkul, S. Moriyama, D. J. Mills, W. Kühlbrandt, S. Nagamori

This study identifies Ca2+-mediated higher-order assembly of b0,+AT-rBAT as critical for system b0,+ trafficking and reveals its role in type I cystinuria.

bioRxiv · May 6, 2021 · PreprintBiochemistry

A multi-hierarchical approach reveals D-serine as a hidden substrate of sodium-coupled monocarboxylate transporters

P. Wiriyasermkul, S. Moriyama, M. Suzuki, P. Kongpracha, N. Nakamae, S. Takeshita, Y. Tanaka, A. Matsuda, M. Miyasaka, K. Hamase, T. Kimura, M. Mita, J. Sasabe, S. Nagamori

The paper identifies two renal D-serine transport systems, revealing ASCT2 as a noncanonical substrate of SMCTs and highlighting their physiological and pathological roles.

bioRxiv · Aug 10, 2020Biochemistry

Cryo-EM structure of the human L-type amino acid transporter 1 in complex with glycoprotein CD98hc

Y. Lee, P. Wiriyasermkul, C. Jin, L. Quan, R. Ohgaki, S. Okuda, T. Kusakizako, T. Nishizawa, K. Oda, R. Ishitani, T. Yokoyama, T. Nakane, M. Shirouzu, H. Endou, S. Nagamori, , O. Nureki

This paper reports the cryo-EM structure of the human LAT1-CD98hc heterodimer, revealing its architecture and interactions, and maps disease mutations to explain congenital disorders.

bioRxiv · Mar 14, 2019Biochemistry