Author

H. Noji

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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Biophysics· 3 Biochemistry· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Organism:E. coli· 2 Research Focus:protein folding & dynamics· 2 Organism:chicken / avian· 1 Research Focus:host-pathogen & immune response· 1 Organism:non-human primate· 1 Assay:proteomics· 1 Assay:structural biology· 1

Frequent Co-Authors

H. Ueno· 3 shared S. Honda· 2 shared Y. Minagawa· 2 shared A. G. Stewart· 1 shared K. Miyazaki· 1 shared K. V. Tabata· 1 shared M. Kato· 1 shared M. Sakuma· 1 shared

Activity by Year

2020-2021 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 19 mutual co-author links

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3 shared papersBiophysics

H. Ueno

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

Genetic perturbation enhances functional heterogeneity in alkaline phosphatase

M. Sakuma, S. Honda, H. Ueno, K. Miyazaki, N. Tokuriki, H. Noji

This study quantifies functional heterogeneity in wild-type and mutant alkaline phosphatase, finding that genetic perturbations increase heterogeneity and correlate with promiscuous activities.

bioRxiv · Nov 25, 2021 · PreprintBiochemistry

The six steps of the F1-ATPase rotary catalytic cycle

M. Sobti, H. Ueno, H. Noji, A. G. Stewart

This study determines the structure of the binding dwell state of F1-ATPase and provides a structural basis for the entire rotary catalysis cycle.

bioRxiv · Dec 15, 2020Biophysics

Multi-dimensional digital bioassay platform based on an air-sealed femtoliter reactor array device

S. Honda, Y. Minagawa, H. Noji, K. V. Tabata

This paper introduces a multi-dimensional digital bioassay platform for analyzing single molecules, demonstrating its ability to perform multi-conditional and multi-parametric assays with high stability and resolution.

bioRxiv · Oct 25, 2020Biophysics

Elucidation and control of low and high active populations of alkaline phosphatase molecules for quantitative digital bioassay

H. Ueno, M. Kato, Y. Minagawa, Y. Hirose, H. Noji

This study quantitatively analyzes single-molecule ALP activity, revealing two distinct populations with different catalytic properties and demonstrating methods to generate homogeneous ALP populations.

bioRxiv · Oct 18, 2020Biophysics