Author

Hiroyuki Nakai

Niigata UniversityORCID 0009-0007-4682-336XUnclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

Click to filter author papers

Signature Assays, Organisms & Methods

Click to filter · or open tag

Approach:experimental assay· 3 Organism:bacteria (other)· 2 Research Focus:cell type annotation· 1 Research Focus:clustering· 1 Organism:fungi (other)· 1 Research Focus:host-pathogen & immune response· 1 Assay:proteomics· 1

Frequent Co-Authors

Masahiro NakajimaiD· 3 shared Sei MotouchiiD· 3 shared Hayao TaguchiiD· 2 shared Hisaka Shimizu· 2 shared Kaito KobayashiiD· 2 shared Nobukiyo TanakaiD· 2 shared Yoshinao Kitano· 2 shared Ai Ishiguro· 1 shared

Activity by Year

2025-2025 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 35 mutual co-author links

Click any collaborator node to inspect or filter shared papers

Focal author (center)Selected co-authorORCID co-authorUnlinked name

Curved chords = mutual co-authorship

3 shared papersBiochemistry

Masahiro NakajimaORCID

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

BiochemistryProtein SciencePeer-reviewedMay 24, 2025

Extensive distribution of β-1,2-glucanases: finding of new glycoside hydrolase families of β-1,2-glucanases

Masahiro Nakajima, Nobukiyo Tanaka, Sei Motouchi…·Hayao Taguchi

The paper identifies three new glycoside hydrolase families of β-1,2-glucanases and reveals their functional and structural relationships within a superfamily.

4 citations

bacteria (other)fungi (other)

𝕏 PostBluesky

BiochemistrybioRxivPreprintApr 21, 2025

Discovery of a wide variety of α-1,6-cyclized β-1,2-glucan synthases: a new entrance for host-microbe interactions.

Sei Motouchi, Inhyuk Kim, Ai Ishiguro…·Masahiro Nakajima

The paper identifies and characterizes α-1,6-cyclized β-1,2-glucan synthases, revealing their role in plant-pathogen interactions and potential applications in agriculture.

DOI 10.1101/2025.04.21.649730

experimental assayhost-pathogen & immune response

𝕏 PostBluesky

BiochemistryCommunications BiologyPeer-reviewedJan 16, 2025

A beta-Galactosidase acting on unique galactosides: the structure and function of a beta-1,2-galactosidase from Bacteroides xylanisolvens, an intestinal bacterium

Yutaka Nakazawa, Masumi Kageyama, Tomohiko Matsuzawa…·Masahiro Nakajima

This study identifies a beta-galactosidase from Bacteroides xylanisolvens that hydrolyzes beta-1,2-galactooligosaccharides, revealing its unique substrate specificity through structural and biochemical analysis.

10 citations

bacteria (other)experimental assay

𝕏 PostBluesky