Výsledky vyhledávání - "Hidemi Hirano"

Crystal structure of the Xpo1p nuclear export complex bound to the SxFG/PxFG repeats of the nucleoporin Nup42p

Autor: Yoshiyuki Matsuura, Natsuki Shirai, Masako Koyama, Hidemi Hirano

Publikováno v: Genes to cells : devoted to molecularcellular mechanisms. 22(10)

Xpo1p (yeast CRM1) is the major nuclear export receptor that carries a plethora of proteins and ribonucleoproteins from the nucleus to cytoplasm. The passage of the Xpo1p nuclear export complex through nuclear pore complexes (NPCs) is facilitated by

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c3f95581628e827f37115243f2215bce
https://pubmed.ncbi.nlm.nih.gov/28791779

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Structural basis for the regulation of nuclear import of Epstein-Barr virus nuclear antigen 1 (EBNA1) by phosphorylation of the nuclear localization signal

Autor: Yoshiyuki Matsuura, Hidemi Hirano, Ryohei Nakada

Publikováno v: Biochemical and biophysical research communications. 484(1)

Epstein-Barr virus (EBV) nuclear antigen 1 (EBNA1) is expressed in every EBV-positive tumor and is essential for the maintenance, replication, and transcription of the EBV genome in the nucleus of host cells. EBNA1 is a serine phosphoprotein, and it

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::55059acc1185da4cea5d14241653f956
https://pubmed.ncbi.nlm.nih.gov/28104399

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Structures of the Karyopherins Kap121p and Kap60p Bound to the Nuclear Pore-Targeting Domain of the SUMO Protease Ulp1p

Autor: Junya Kobayashi, Yoshiyuki Matsuura, Hidemi Hirano

Publikováno v: Journal of molecular biology. 429(2)

The budding yeast small ubiquitin-like modifier (SUMO) protease Ulp1p catalyzes both the processing of newly synthesized SUMO to its mature form and the deconjugation of SUMO from target proteins, thereby regulating a wide range of cellular processes

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0e679aeda0ff3c25737fbe7440e53737
https://pubmed.ncbi.nlm.nih.gov/27939291

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Structure of importin-α bound to a non-classical nuclear localization signal of the influenza A virus nucleoprotein

Autor: Ryohei Nakada, Yoshiyuki Matsuura, Hidemi Hirano

Publikováno v: Scientific Reports

A non-classical nuclear localization signal (ncNLS) of influenza A virus nucleoprotein (NP) is critical for nuclear import of viral genomic RNAs that transcribe and replicate in the nucleus of infected cells. Here we report a 2.3 Å resolution crysta

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4c447670b6a0a314759d7f761d236287

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Crystal structure of the karyopherin Kap121p bound to the extreme C-terminus of the protein phosphatase Cdc14p

Autor: Junya Kobayashi, Hidemi Hirano, Yoshiyuki Matsuura

Publikováno v: Biochemical and biophysical research communications. 463(3)

In Saccharomyces cerevisiae, the protein phosphatase Cdc14p is an antagonist of mitotic cyclin-dependent kinases and is a key regulator of late mitotic events such as chromosome segregation, spindle disassembly and cytokinesis. The activity of Cdc14p

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::24828d20635ffdf33cf98140fa8856b3
https://pubmed.ncbi.nlm.nih.gov/26022122

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Sensing actin dynamics: structural basis for G-actin-sensitive nuclear import of MAL

Autor: Hidemi Hirano, Yoshiyuki Matsuura

Publikováno v: Biochemical and biophysical research communications. 414(2)

The coordination of cytoskeletal actin dynamics with gene expression reprogramming is emerging as a crucial mechanism to control diverse cellular processes, including cell migration, differentiation and neuronal circuit assembly. The actin-binding tr

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0f9b20f272c0b9f0728d7dd53e92ce6c
https://pubmed.ncbi.nlm.nih.gov/21964294

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Mechanism of Lck recruitment to the T-cell receptor cluster as studied by single-molecule-fluorescence video imaging

Autor: Akiko Kato, Atsushi Kosugi, Ken Ritchie, Ryota Iino, Akihiro Kusumi, Hiroshi Ike, Takahiro K. Fujiwara, Hidemi Hirano

Publikováno v: Chemphyschem : a European journal of chemical physics and physical chemistry. 4(6)

The T-cell receptor (TCR) signaling has fascinated many researchers, because, in addition to its immunological importance, it appears to provide interesting paradigms for the study of the basic design/concepts on how cellular signaling transduction i

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8e2affb2dbd1912c3b8457017448807d
https://pubmed.ncbi.nlm.nih.gov/12836486

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S1e1-5 Raft and non-raft molecules undergo very similar diffusion in the time scales between 25 microseconds and 2.5 seconds(S1-e1: 'Unraveling the membrane microdomains using new biophysical tools',Symposia,Abstract,Meeting Program of EABS & BSJ 2006)

Autor: Hidemi Hirano, Kenichi G. N. Suzuki, Michael Edidin, Takahiro K. Fujiwara, Ken Ritchie, Akihiro Kusumi

Publikováno v: Seibutsu Butsuri. 46:S109

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::aff8518718439bd3d9ca0d028ea78b5e
https://doi.org/10.2142/biophys.46.s109_2

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2N1430 Mechanism for Lck recruitment to TCR clusters as studied by single fluorophore video microscopy

Autor: Atsushi Kosugi, Ken Ritchie, Ryota Iino, Takahiro K. Fujiwara, Hiroshi Ike, Hidemi Hirano, N. Tanimura, Akihiro Kusumi

Publikováno v: Seibutsu Butsuri. 42:S141

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::337feb96f33041c87d361d995c84df6b
https://doi.org/10.2142/biophys.42.s141_4

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