Naotaka Sekiyama - Concepedia

Author

Naotaka Sekiyama

Kyoto University ORCID

Also Known As

, N. Sekiyama, Naotaka SEKIYAMA, Naotaka Sekiyama, Sekiyama, Naotaka

Publications

524

Citations

H-Index

Concepts

All Affiliations

Kyoto University Japan Science and Technology Agency RIKEN Center for Sustainable Resource Science National Institute of Biomedical Innovation, Health and Nutrition The University of Osaka

About

Naotaka Sekiyama is an author at Kyoto University specializing in structural biology, molecular biology, and medicine.

Top Concepts

#	Concept	H-Index	Publications	Citations
1	Medicine	4	4	171
2	Natural Sciences	4	4	171
3	Molecular Biology	4	4	171
4	Cell Biology	2	2	110
5	Biochemistry	1	1	45

Naotaka Sekiyama

Publications

508

Citations

H-Index

Page 1

	Year	Citations
Recognition of modification status on a histone H3 tail by linked histone reader modules of the epigenetic regulator UHRF1 Kyohei Arita, Shin Isogai, Takashi Oda, Proceedings of the National Academy of Sciences	2012	215
Molecular mechanism of the dual activity of 4EGI-1: Dissociating eIF4G from eIF4E but stabilizing the binding of unphosphorylated 4E-BP1 Naotaka Sekiyama, Haribabu Arthanari, Evangelos Papadopoulos, Proceedings of the National Academy of Sciences	2015	112
Structure of the Small Ubiquitin-like Modifier (SUMO)-interacting Motif of MBD1-containing Chromatin-associated Factor 1 Bound to SUMO-3 Naotaka Sekiyama, Takahisa Ikegami, Tsutomu Yamane, Journal of Biological Chemistry Protein AssemblyMolecular BiologyEpigeneticsProtein FoldingProtein Function	2008	79
ALS mutations in the TIA-1 prion-like domain trigger highly condensed pathogenic structures Naotaka Sekiyama, Kiyofumi Takaba, Saori Maki-Yonekura, Proceedings of the National Academy of Sciences Pathogenic StructuresProtein AssemblyMolecular BiologyAls MutationsDisease Gene Identification	2022	45
Structural basis for regulation of poly‐SUMO chain by a SUMO‐like domain of Nip45 Naotaka Sekiyama, Kyohei Arita, Yoshihiro Ikeda, Proteins Structure Function and Bioinformatics Sumo‐like DomainProtein AssemblyMolecular RegulationMolecular BiologyNip45 Sld2 Shares	2009	31
NMR analysis of Lys63-linked polyubiquitin recognition by the tandem ubiquitin-interacting motifs of Rap80 Naotaka Sekiyama, Jun‐Goo Jee, Shin Isogai, Journal of Biomolecular NMR Systems BiologyStructural BioinformaticsProtein FoldingLys63-linked Polyubiquitin RecognitionMedicine	2012	16
Conformational Space Sampled by Domain Reorientation of Linear Diubiquitin Reflected in Its Binding Mode for Target Proteins Xue‐Ni Hou, Naotaka Sekiyama, Yasuko Ohtani, ChemPhysChem	2021	10

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