WorldCat Identities

Tsumoto, Kouhei

Overview
Works: 22 works in 30 publications in 2 languages and 41 library holdings
Roles: Other, Contributor
Publication Timeline
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Most widely held works by Kouhei Tsumoto
Shinkino kotai kaihatsu handobukku( Book )

2 editions published in 2012 in Japanese and held by 4 WorldCat member libraries worldwide

Makutanpakushitsu kogaku handobukku( Book )

2 editions published in 2020 in Japanese and held by 4 WorldCat member libraries worldwide

How proteins work by Mike Williamson( Book )

3 editions published in 2016 in Japanese and held by 4 WorldCat member libraries worldwide

This is a clear, up-to-date and authoritative account of the principles that govern the way proteins work. The book provides advanced undergraduate students in biochemistry and biophysics in vivo context for the standard protein sequence-structure-function model
Seimei kinzoku dainamikusu : seitainai ni okeru kinzoku no kyodō to seigyo( Book )

3 editions published in 2021 in Japanese and held by 3 WorldCat member libraries worldwide

111In-labeled anti-cadherin17 antibody D2101 has potential as a noninvasive imaging probe for diagnosing gastric cancer and lymph-node metastasis by Kentaro Fujiwara( )

1 edition published in 2019 in English and held by 2 WorldCat member libraries worldwide

Biochemistry of signal transduction and regulation by Gerhard Krauss( Book )

2 editions published in 2017 in Japanese and held by 2 WorldCat member libraries worldwide

"This all-new edition of a best-selling text has been thoroughly updated to keep pace with the rapid progress in signal transduction research. With didactic skill and clarity, the molecular basis of signal transduction, regulated gene expression, the cell cycle, tumorigenesis and apoptosis is made transparent for everyone with a basic knowledge in biochemistry or molecular biology. The unique textbook may be used as a companion for a course on regulation and signal transduction as well as an introductory reference to the field for students and researchers."--Jacket
Seitai bunshi kagaku : kiso kara ōyō made by Naoki Sugimoto( Book )

2 editions published in 2017 in Japanese and held by 2 WorldCat member libraries worldwide

<> by Masato Kiyoshi( )

1 edition published in 2018 in English and held by 2 WorldCat member libraries worldwide

A secondary RET mutation in the activation loop conferring resistance to vandetanib by Takashi Nakaoku( )

1 edition published in 2018 in English and held by 2 WorldCat member libraries worldwide

Tosa no shinkino kaihatsu oyo handobukku : Soyaku iryo kara shokuhin kaihatsu made( Book )

1 edition published in 2015 in Japanese and held by 2 WorldCat member libraries worldwide

Assessment of the Protein-Protein Interactions in a Highly Concentrated Antibody Solution by Using Raman Spectroscopy by Chikashi Ota( )

1 edition published in 2015 in English and held by 2 WorldCat member libraries worldwide

Structural basis for binding and transfer of heme in bacterial heme-acquisition systems( )

1 edition published in 2017 in English and held by 1 WorldCat member library worldwide

Abstract: Periplasmic heme-binding proteins (PBPs) in Gram-negative bacteria are components of the heme acquisition system. These proteins shuttle heme across the periplasmic space from outer membrane receptors to ATP-binding cassette (ABC) heme importers located in the inner-membrane. In the present study, we characterized the structures of PBPs found in the pathogen Burkholderia cenocepacia (BhuT) and in the thermophile Roseiflexus sp . RS-1 (RhuT) in the heme-free and heme-bound forms. The conserved motif, in which a well-conserved Tyr interacts with the nearby Arg coordinates on heme iron, was observed in both PBPs. The heme was recognized by its surroundings in a variety of manners including hydrophobic interactions and hydrogen bonds, which was confirmed by isothermal titration calorimetry. Furthermore, this study of 3 forms of BhuT allowed the first structural comparison and showed that the heme-binding cleft of BhuT adopts an "open" state in the heme-free and 2-heme-bound forms, and a "closed" state in the one-heme-bound form with unique conformational changes. Such a conformational change might adjust the interaction of the heme(s) with the residues in PBP and facilitate the transfer of the heme into the translocation channel of the importer
Enzymatically cleavable traceless biotin tags for protein PEGylation and purification1( )

1 edition published in 2018 in English and held by 1 WorldCat member library worldwide

Abstract : Immobilized lipase was successfully employed for the rapid removal of a biotin tag from a protein-PEG conjugate under mild conditions. Abstract : Here we report an example of a protein-PEG conjugate with a biotin tag cleavable by lipase-catalyzed hydrolysis. Very mild cleavage conditions, heterogeneous, easily separable catalysts, and traceless design make this method attractive for the preparation and purification of PEGylated proteins
Tōsa no shinkinō kaihatsu ōyō handobukku : sōyaku iryō kara shokuhin kaihatsu made( Book )

1 edition published in 2015 in Japanese and held by 1 WorldCat member library worldwide

Development of drug discovery screening system by molecular interaction kinetics-mass spectrometry( )

1 edition published in 2018 in English and held by 1 WorldCat member library worldwide

Tokushū jisedai kōtai iyaku no shōgeki( Book )

1 edition published in 2018 in Japanese and held by 1 WorldCat member library worldwide

Cover Image( )

1 edition published in 2018 in English and held by 1 WorldCat member library worldwide

Abstract : The cover image, by Naoko Obi et al., is based on the Research Article Development of Drug Discovery Screening System by Molecular Interaction Kinetics Mass Spectrometry, DOI:10.1002/rcm. 8083
A combination of 19F NMR and surface plasmon resonance for site-specific hit selection and validation of fragment molecules that bind to the ATP-binding site of a kinase( )

1 edition published in 2018 in English and held by 1 WorldCat member library worldwide

Graphical abstract: Abstract: 19 F NMR has recently emerged as an efficient, sensitive tool for analyzing protein binding to small molecules, and surface plasmon resonance (SPR) is also a popular tool for this purpose. Herein a combination of 19 F NMR and SPR was used to find novel binders to the ATP-binding pocket of MAP kinase extracellular regulated kinase 2 (ERK2) by fragment screening with an original fluorinated-fragment library. The 19 F NMR screening yielded a high primary hit rate of binders to the ERK2 ATP-binding pocket compared with the rate for the SPR screening. Hit compounds were evaluated and categorized according to their ability to bind to different binding sites in the ATP-binding pocket. The binding manner was characterized by using isothermal titration calorimetry and docking simulation. Combining 19 F NMR with other biophysical methods allows the identification of multiple types of hit compounds, thereby increasing opportunities for drug design using preferred fragments
Functional Contacts between MPER and the Anti-HIV-1 Broadly Neutralizing Antibody 4E10 Extend into the Core of the Membrane( )

1 edition published in 2017 in English and held by 1 WorldCat member library worldwide

Abstract: The exceptional breadth of broadly neutralizing antibodies (bNAbs) against the membrane-proximal external region (MPER) of the transmembrane protein gp41 makes this class of antibodies an ideal model to design HIV vaccines. From a practical point of view, however, the preparation of vaccines eliciting bNAbs is still a major roadblock that limits their clinical application. Fresh mechanistic insights are necessary to develop more effective strategies. In particular, the function of the unusually long complementarity-determining region three of the heavy chain (CDRH3) of 4E10, an anti-MPER bNAb, is an open question that fascinates researchers in the field. Residues comprising the apex region are dispensable for engagement of the epitope in solution; still, their single mutation profoundly impairs the neutralization capabilities of the antibody. Since this region is very hydrophobic, it has been proposed that the apex is essential for anchoring the antibody to the viral membrane where MPER resides. Herein, we have critically examined this idea using structural, biophysical, biochemical, and cell-based approaches. Our results demonstrate that the apex region is not just a "greasy" spot merely increasing the affinity of the antibody for the membrane. We demonstrate the three-dimensional engagement of the apex region of the CDRH3 with the conglomerate of gp41 epitope and membrane lipids as a means of effective binding and neutralization of the virus. This mechanism of recognition suggests a standard route of antibody ontogeny. Therefore, we need to focus our efforts on recreating a more realistic MPER/lipid immunogen in order to generate more effective anti-HIV-1 vaccines. Graphical Abstract: Highlights: The hydrophobic apex of CDRH3 of 4E10 is critical for blocking HIV-1, but why? Hydrophobicity facilitates membrane binding but cannot explain neutralization potency. The two tryptophan residues of the apex penetrate into the core of the lipid bilayer. One of these tryptophan residues contacts the epitope in the interior of the membrane. The mechanism revealed in this study may impact the design of anti-HIV-1 vaccines
 
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Audience level: 0.88 (from 0.55 for How protei ... to 0.99 for Biochemist ...)

Alternative Names
Tsumoto, Kohei

Tsumoto, Kouhei

ツモト, コウヘイ

Languages
Japanese (17)

English (11)