FullText URL fulltext20220509-1.pdf Supporting_Information20220509-1.pdf
Author Ohtsuka, Satomi| Okumura, Taisei| Τabuchi, Yuna| Miyagawa, Tomoyuki| Kanayama, Naoki| Magari, Masaki| Hatano, Naoya| Sakagami, Hiroyuki| Suizu, Futoshi| Ishikawa, Teruhiko| Tokumitsu, Hiroshi|
Note This document is the Accepted Manuscript version of a Published Work that appeared in final form in Biochemistry, copyright © American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see https://doi.org/10.1021/acs.biochem.1c00796|
Published Date 2022-03-11
Publication Title Biochemistry
Volume volume61
Issue issue7
Publisher American Chemical Society (ACS)
Start Page 545
End Page 553
ISSN 0006-2960
NCID AA00564599
Content Type Journal Article
language English
OAI-PMH Set 岡山大学
Copyright Holders Copyright © 2022 American Chemical Society
File Version author
DOI 10.1021/acs.biochem.1c00796
Web of Science KeyUT 000783678600007
Related Url isVersionOf https://doi.org/10.1021/acs.biochem.1c00796
JaLCDOI 10.18926/46955
FullText URL mfe_38_1-2_091_096.pdf
Author Kanayama, Naoki| Yamakoshi, Kimi| Kiyomi, Masaaki| Magari, Masaki| Ohmori, Hitoshi|
Abstract Generally, IgM antibodies (Abs) produced in a primary immune response show lower affinity for an inducing antigen (Ag) compared with the corresponding IgG Abs that are major switched isotypes formed in the secondary response. An IgM molecule is a pentamer with 10 Ag-binding sites that will contribute to an increase of avidity for an Ag. To estimate the contribution of the pentameric structure to the avidity of an IgM Ab, we generated IgM and IgG1 monoclonal Abs (mAbs) with identical V regions that are specific for 4-hydroxy-3-nitrophenylacetyl (NP) by in vitro class switching of B cells followed by the cell fusion with a mouse myeloma cell line. Compared with an anti-NP IgG1 mAb, the corresponding IgM mAb showed much higher avidity for NP-conjugated bovine serum albumin, which was drastically reduced after being dissociated into monomers.
Publication Title Memoirs of the Faculty of Engineering, Okayama University
Published Date 2004-03
Volume volume38
Issue issue1-2
Start Page 91
End Page 96
ISSN 0475-0071
language English
File Version publisher
NAID 80017001822
FullText URL fulltext.pdf
Author Yamamoto, Maho| Kondo, Rina| Hozumi, Haruka| Doi, Seita| Denda, Miwako| Magari, Masaki| Kanayama, Naoki| Hatano, Naoya| Morishita, Ryo| Tokumitsu, Hiroshi|
Keywords S100 protein HMG20A protein-protein interaction Ca2+-signal transduction genome-wide screening
Published Date 2021-03-30
Publication Title Biomolecules
Volume volume11
Issue issue4
Publisher MDPI
Start Page 510
ISSN 2218-273X
Content Type Journal Article
language English
OAI-PMH Set 岡山大学
File Version publisher
PubMed ID 33808200
NAID 120007037385
DOI 10.3390/biom11040510
Web of Science KeyUT 000642769800001
Related Url isVersionOf https://doi.org/10.3390/biom11040510
FullText URL fulltext20220106-5.pdf
Author Fukumoto, Yusei| Harada, Yuhei| Ohtsuka, Satomi| Kanayama, Naoki| Magari, Masaki| Hatano, Naoya| Sakagami, Hiroyuki| Tokumitsu, Hiroshi|
Keywords CaMKK oligomerization Ca2+-signaling phosphorylation CaM kinase cascade
Note © 2021 Elsevier Inc. This manuscript version is made available under the CC-BY-NC-ND 4.0 License. http://creativecommons.org/licenses/by-nc-nd/4.0/. This is the accepted manuscript version. The formal published version is available at [https://doi.org/10.1016/j.bbrc.2021.11.105] .|
Published Date 2022-1
Publication Title Biochemical and Biophysical Research Communications
Volume volume587
Publisher Elsevier BV
Start Page 160
End Page 165
ISSN 0006-291X
Content Type Journal Article
language English
OAI-PMH Set 岡山大学
Copyright Holders © 2021 Elsevier Inc.
File Version author
PubMed ID 34875535
DOI 10.1016/j.bbrc.2021.11.105
Web of Science KeyUT 000729413200005
Related Url isVersionOf https://doi.org/10.1016/j.bbrc.2021.11.105
FullText URL BBRC_525_1_251_257.pdf
Author Takabatake, Shota| Fukumoto, Yusei| Ohtsuka, Satomi| Kanayama, Naoki| Magari, Masaki| Sakagami, Hiroyuki| Hatano, Naoya| Tokumitsu, Hiroshi|
Keywords CaMKKβ Phosphorylation Dephosphorylation PP1 PP2A Okadaic acid
Note This fulltext is available in Feb. 2021.|
Published Date 2020-04-23
Publication Title Biochemical and Biophysical Research Communications
Volume volume525
Issue issue1
Publisher Academic Press
Start Page 251
End Page 257
ISSN 0006-291X
NCID AA00564395
Content Type Journal Article
language English
OAI-PMH Set 岡山大学
File Version author
PubMed ID 32085894
DOI 10.1016/j.bbrc.2020.02.056
Web of Science KeyUT 000526797700039
Related Url isVersionOf https://doi.org/10.1016/j.bbrc.2020.02.056
FullText URL BBA_1863_4_672.pdf
Author Takabatake, Shota| Ohtsuka, Satomi| Sugawara, Takeyuki| Hatano, Naoya| Kanayama, Naoki| Magari, Masaki| Sakagami, Hiroyuki| Tokumitsu, Hiroshi|
Keywords CaMKK Calmodulin Intracellular Ca(2+) PKA Phosphorylation Signal transduction
Published Date 2019-01-17
Publication Title Biochimica et Biophysica Acta (BBA) - General Subjects
Volume volume1863
Issue issue4
Publisher Elsevier Science
Start Page 672
End Page 680
ISSN 0304-4165
NCID AA00564679
Content Type Journal Article
language English
OAI-PMH Set 岡山大学
File Version author
PubMed ID 30660766
DOI 10.1016/j.bbagen.2018.12.012
Web of Science KeyUT 000460853200003
Related Url isVersionOf https://doi.org/10.1016/j.bbagen.2018.12.012
FullText URL BBRC_485_2_261.pdf
Author Kawaguchi, Yuka| Nariki, Hiroaki| Kawamoto, Naoko| Kanehiro, Yuichi| Miyazaki, Satoshi| Suzuki, Mari| Magari, Masaki| Tokumitsu, Hiroshi| Kanayama, Naoki|
Keywords AID DT40 Gene conversion Ig SRSF1 Somatic hypermutation
Published Date 2017-04
Publication Title Biochemical and Biophysical Research Communications
Volume volume485
Issue issue2
Publisher Elsevier
Start Page 261
End Page 266
ISSN 0006-291X
NCID AA00564395
Content Type Journal Article
language English
OAI-PMH Set 岡山大学
Copyright Holders https://creativecommons.org/licenses/by-nc-nd/4.0/deed.ja
File Version author
PubMed ID 28235482
DOI 10.1016/j.bbrc.2017.02.097
Web of Science KeyUT 000396798300007
Related Url isVersionOf https://doi.org/10.1016/j.bbrc.2017.02.097
FullText URL fulltext20220602-1.pdf
Author Kaneshige, Riku| Ohtsuka, Satomi| Harada, Yuhei| Kawamata, Issei| Magari, Masaki| Kanayama, Naoki| Hatano, Naoya| Sakagami, Hiroyuki| Tokumitsu, Hiroshi|
Keywords AMP-activated protein kinase Arg/Pro-rich insert domain (RP-domain) calcium/calmodulin-dependent protein kinase calcium/calmodulin-dependent protein kinase kinase substrate recognition
Note This is the peer reviewed version of the following article: [Kaneshige, R., Ohtsuka, S., Harada, Y., Kawamata, I., Magari, M., Kanayama, N., Hatano, N., Sakagami, H. and Tokumitsu, H. (2022), Substrate recognition by Arg/Pro-rich insert domain in calcium/calmodulin-dependent protein kinase kinase for target protein kinases. FEBS J, 289: 5971-5984. https://doi.org/10.1111/febs.16467], which has been published in final form at [https://doi.org/10.1111/febs.16467]. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Use of Self-Archived Versions. This article may not be enhanced, enriched or otherwise transformed into a derivative work, without express permission from Wiley or by statutory rights under applicable legislation. Copyright notices must not be removed, obscured or modified. The article must be linked to Wiley’s version of record on Wiley Online Library and any embedding, framing or otherwise making available the article or pages there of by third parties from platforms, services and websites other than Wiley Online Library must be prohibited.| This fulltext will be available in May 2023.|
Published Date 2022-05-17
Publication Title The FEBS Journal
Volume volume289
Issue issue19
Publisher Wiley
Start Page 5971
End Page 5984
ISSN 1742-464X
NCID AA11998513
Content Type Journal Article
language English
OAI-PMH Set 岡山大学
Copyright Holders © 2022 Federation of European Biochemical Societies.
File Version author
PubMed ID 35490408
DOI 10.1111/febs.16467
Web of Science KeyUT 000796673600001
Related Url isVersionOf https://doi.org/10.1111/febs.16467