Ryosuke Ishimura
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Explore the profile of Ryosuke Ishimura including associated specialties, affiliations and a list of published articles.
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12
Citations
852
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Recent Articles
1.
Ishimura R, Ito S, Mao G, Komatsu-Hirota S, Inada T, Noda N, et al.
Sci Adv
. 2023 Aug;
9(33):eadh3635.
PMID: 37595036
Ubiquitin-fold modifier 1 (UFM1) is a ubiquitin-like protein covalently conjugated with intracellular proteins through ufmylation, similar to ubiquitylation. Ufmylation is involved in processes such as endoplasmic reticulum (ER)-associated protein degradation,...
2.
Ishimura R, El-Gowily A, Noshiro D, Komatsu-Hirota S, Ono Y, Shindo M, et al.
Nat Commun
. 2022 Dec;
13(1):7857.
PMID: 36543799
Protein modification by ubiquitin-like proteins (UBLs) amplifies limited genome information and regulates diverse cellular processes, including translation, autophagy and antiviral pathways. Ubiquitin-fold modifier 1 (UFM1) is a UBL covalently conjugated...
3.
Sakai S, Hasegawa A, Ishimura R, Tamura N, Kageyama S, Komatsu-Hirota S, et al.
Mol Cell Biol
. 2021 Nov;
42(1):e0002421.
PMID: 34748402
A germ line copy number duplication of chromosome 14q32, which contains and , was identified in families with myeloproliferative neoplasm (MPN). Here, we show that mice lacking both and ,...
4.
Briere L, Walker M, High F, Cooper C, Rogers C, Callahan C, et al.
Cold Spring Harb Mol Case Stud
. 2021 Apr;
7(3).
PMID: 33811063
Early infantile epileptic encephalopathy-44 (EIEE44, MIM: 617132) is a previously described condition resulting from biallelic variants in , a gene involved in a ubiquitin-like post-translational modification system called UFMylation. Here...
5.
Cabrera-Serrano M, Coote D, Azmanov D, Goullee H, Andersen E, McLean C, et al.
J Med Genet
. 2020 Mar;
57(12):835-842.
PMID: 32179706
Background: UBA5 is the activating enzyme of UFM1 in the ufmylation post-translational modification system. Different neurological phenotypes have been associated with pathogenic variants including epilepsy, intellectual disability, movement disorders and...
6.
Nahorski M, Maddirevula S, Ishimura R, Alsahli S, Brady A, Begemann A, et al.
Brain
. 2018 Jun;
141(7):1934-1945.
PMID: 29868776
The post-translational modification of proteins through the addition of UFM1, also known as ufmylation, plays a critical developmental role as revealed by studies in animal models. The recent finding that...
7.
Tamura R, Yoshihara K, Saito T, Ishimura R, Martinez-Ledesma J, Xin H, et al.
Oncogenesis
. 2018 Jan;
7(1):4.
PMID: 29358619
We previously found that therapeutic targetable fusions are detected across various cancers. To identify therapeutic targetable fusion in uterine cervical cancer, for which no effective gene targeted therapy has yet...
8.
Ishimura R, Obata M, Kageyama S, Daniel J, Tanaka K, Komatsu M
FEBS Lett
. 2016 Dec;
591(1):196-204.
PMID: 27926783
The ubiquitin-fold modifier 1 (UFM1)-system, a ubiquitin-like protein conjugation system, is involved in the development of breast cancer and several hereditary neurological syndromes. However, the molecular mechanisms of UFM1-related pathogenesis...
9.
Muona M, Ishimura R, Laari A, Ichimura Y, Linnankivi T, Keski-Filppula R, et al.
Am J Hum Genet
. 2016 Aug;
99(3):683-694.
PMID: 27545674
The ubiquitin fold modifier 1 (UFM1) cascade is a recently identified evolutionarily conserved ubiquitin-like modification system whose function and link to human disease have remained largely uncharacterized. By using exome...
10.
Kageyama S, Sou Y, Uemura T, Kametaka S, Saito T, Ishimura R, et al.
J Biol Chem
. 2014 Jul;
289(36):24944-55.
PMID: 25049227
The ubiquitin-proteasome system and autophagy are crucially important for proteostasis in cells. These pathways are interdependent, and dysfunction in either pathway causes accumulation of ubiquitin-positive aggregates, a hallmark of human...