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Biology and Biochemistry

D-Index
55
Citations
12947
World Ranking
14905
National Ranking
1053

Overview

Yasushi Saeki is affiliated with the Tokyo Metropolitan Institute of Medical Science in Japan. Their research primarily focuses on Biochemistry, Genetics and Molecular Biology, with a significant number of publications also contributing to the field of Medicine. Within these areas, Saeki has a strong emphasis on Molecular Biology and Cell Biology, with additional work related to Infectious Diseases, Immunology, and Neurology.

The scientist's work prominently covers topics such as Ubiquitin and proteasome pathways, Endoplasmic Reticulum Stress and Disease, RNA modifications and cancer, Protein Degradation and Inhibitors, interferon and immune responses, SARS-CoV-2 and COVID-19 Research, and Autophagy in Disease and Therapy.

Saeki has contributed numerous publications in notable journals. Their frequent publication venues include:

  • bioRxiv (Cold Spring Harbor Laboratory)
  • Nature Communications
  • Communications Biology
  • Molecular Cell
  • Journal of Medicinal Chemistry

Among their recent papers are:

  • "Stress- and ubiquitylation-dependent phase separation of the proteasome" (2020, Nature)
  • "RQT complex dissociates ribosomes collided on endogenous RQC substrate SDD1" (2020, Nature Structural & Molecular Biology)
  • "Two distinct modes of DNMT1 recruitment ensure stable maintenance DNA methylation" (2020, Nature Communications)
  • "TRIP12 promotes small-molecule-induced degradation through K29/K48-branched ubiquitin chains" (2021, Molecular Cell)
  • "The HOIL-1L ligase modulates immune signalling and cell death via monoubiquitination of LUBAC" (2020, Nature Cell Biology)

Saeki has collaborated extensively with other researchers. Frequent co-authors include:

  • Akinori Endo
  • Fumiaki Ohtake
  • Keiji Tanaka
  • Takuya Tomita
  • Toshifumi Inada

Best Publications

  • Ubiquitin is phosphorylated by PINK1 to activate parkin

    Fumika Koyano;Kei Okatsu;Kei Okatsu;Hidetaka Kosako;Yasushi Tamura

  • Involvement of linear polyubiquitylation of NEMO in NF-kappaB activation.

    Fuminori Tokunaga;Shin-ichi Sakata;Shin-ichi Sakata;Yasushi Saeki;Yoshinori Satomi

  • SHARPIN is a component of the NF-κB-activating linear ubiquitin chain assembly complex

    Fuminori Tokunaga;Tomoko Nakagawa;Masaki Nakahara;Yasushi Saeki

  • Mutations in the deubiquitinase gene USP8 cause Cushing's disease

    Martin Reincke;Silviu Sbiera;Akira Hayakawa;Marily Theodoropoulou

  • Lysine 63-linked polyubiquitin chain may serve as a targeting signal for the 26S proteasome

    Yasushi Saeki;Tai Kudo;Takayuki Sone;Yoshiko Kikuchi

  • The K48-K63 Branched Ubiquitin Chain Regulates NF-κB Signaling.

    Fumiaki Ohtake;Fumiaki Ohtake;Yasushi Saeki;Satoshi Ishido;Jun Kanno

  • Collided ribosomes form a unique structural interface to induce Hel2-driven quality control pathways.

    Ken Ikeuchi;Petr Tesina;Yoshitaka Matsuo;Takato Sugiyama

  • Ubiquitination of stalled ribosome triggers ribosome-associated quality control

    Yoshitaka Matsuo;Ken Ikeuchi;Yasushi Saeki;Shintaro Iwasaki

  • K63 ubiquitylation triggers proteasomal degradation by seeding branched ubiquitin chains.

    Fumiaki Ohtake;Hikaru Tsuchiya;Yasushi Saeki;Keiji Tanaka

  • Phosphorylated ubiquitin chain is the genuine Parkin receptor

    Kei Okatsu;Fumika Koyano;Mayumi Kimura;Hidetaka Kosako

  • Stress- and ubiquitylation-dependent phase separation of the proteasome

    Sayaka Yasuda;Hikaru Tsuchiya;Ai Kaiho;Qiang Guo

  • Multiple proteasome-interacting proteins assist the assembly of the yeast 19S regulatory particle.

    Yasushi Saeki;Akio Toh-e;Tai Kudo;Hitomi Kawamura

  • Ubiquitin-like proteins and Rpn10 play cooperative roles in ubiquitin-dependent proteolysis.

    Yasushi Saeki;Aki Saitoh;Akio Toh-e;Hideyoshi Yokosawa

  • Identification of ubiquitin-like protein-binding subunits of the 26S proteasome.

    Yasushi Saeki;Takayuki Sone;Akio Toh-e;Hideyoshi Yokosawa

  • Ubiquitin recognition by the proteasome.

    Yasushi Saeki

  • Polyubiquitin conjugation to NEMO by triparite motif protein 23 (TRIM23) is critical in antiviral defense

    Kei-ichiro Arimoto;Kenji Funami;Yasushi Saeki;Keiji Tanaka

  • Sem1p Is a Novel Subunit of the 26 S Proteasome from Saccharomyces cerevisiae

    Takayuki Sone;Yasushi Saeki;Yasushi Saeki;Akio Toh-e;Hideyoshi Yokosawa

  • Ubiquitin acetylation inhibits polyubiquitin chain elongation

    Fumiaki Ohtake;Yasushi Saeki;Kensaku Sakamoto;Kazumasa Ohtake

  • Preparation of ubiquitinated substrates by the PY motif-insertion method for monitoring 26S proteasome activity.

    Yasushi Saeki;Erika Isono;Akio Toh‐e

  • Structure of the Dnmt1 Reader Module Complexed with a Unique Two-Mono-Ubiquitin Mark on Histone H3 Reveals the Basis for DNA Methylation Maintenance

    Satoshi Ishiyama;Atsuya Nishiyama;Yasushi Saeki;Kei Moritsugu

Frequent Co-Authors

Keiji Tanaka
Keiji Tanaka Tokyo Metropolitan Institute of Medical Science
Koichi Kato
Koichi Kato National Institutes of Natural Sciences
Kazuhiro Iwai
Kazuhiro Iwai Kyoto University
Toshifumi Inada
Toshifumi Inada Tohoku University
Shigeo Murata
Shigeo Murata University of Tokyo
Fuminori Tokunaga
Fuminori Tokunaga Osaka Metropolitan University
Hiroyasu Nakano
Hiroyasu Nakano Toho University
Nicholas T. Ingolia
Nicholas T. Ingolia University of California, Berkeley
Wolfgang Baumeister
Wolfgang Baumeister Max Planck Society
Hidetaka Kosako
Hidetaka Kosako University of Tokushima

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