| FullText URL | fulltext.pdf |
|---|---|
| Author | Yoshida, Akari| Ohtsuka, Satomi| Matsumoto, Fumiya| Miyagawa, Tomoyuki| Okino, Rei| Ikeda, Yumeya| Tada, Natsume| Gotoh, Akira| Magari, Masaki| Hatano, Naoya| Morishita, Ryo| Satoh, Ayano| Sunatsuki, Yukinari| Nilsson, Ulf J.| Ishikawa, Teruhiko| Tokumitsu, Hiroshi| |
| Note | The version of record of this article, first published in Scientific Reports, is available online at Publisher’s website: http://dx.doi.org/10.1038/s41598-024-57051-9| |
| Published Date | 2024-03-20 |
| Publication Title | Scientific Reports |
| Volume | volume14 |
| Issue | issue1 |
| Publisher | Nature Portfolio |
| Start Page | 6723 |
| ISSN | 2045-2322 |
| Content Type | Journal Article |
| language | English |
| OAI-PMH Set | 岡山大学 |
| Copyright Holders | © The Author(s) 2024 |
| File Version | publisher |
| PubMed ID | 38509168 |
| DOI | 10.1038/s41598-024-57051-9 |
| Web of Science KeyUT | 001192455600061 |
| Related Url | isVersionOf https://doi.org/10.1038/s41598-024-57051-9 |
| 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 |
| 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 |
| 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 | 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 |
| JaLCDOI | 10.18926/47025 |
|---|---|
| FullText URL | mfe_36_2_051_060.pdf |
| Author | Hikida, Masaki| Magari, Masaki| Nakayama, Yasunori| Kanayama, Naoki| Ohmori, Hitoshi| |
| Abstract | A population of peripheral B cells have been shown to express recombination activating gene products, RAG-1 and RAG-2, which are considered to be involved in revising the B cell antigen receptor (BCR) in the periphery. BCR engagement has been reported to turn off RAG expression in peripheral B cells, whereas the same treatment has an opposite effect in immature B cells in the bone marrow. In contrast to receptor editing that is involved in the removal of autoreactivity in immature B cells, it has been shown that secondary V(D)J rearrangement in peripheral B cells, termed receptor revision, contributes to affinity maturation of antibodies. Here, we show that RAG-2 expression in murine splenic B cells was abrogated by the coligation of BCR with complement receptors (CD21/CD35) much more efficiently than by the engagement of BCR alone. On the other hand, the same coligation augmented proliferation of anti-CD40-stimulated B cells. Consistent with these observations, RAG-2 expression was lower in the draining lymph nodes of the quasi-monoclonal mice when they were immunized with a high-affinity antigen than with a low-affinity one. These findings suggest a crucial role for CD21/CD35 in directing the conservation or the revision of BCRs in peripheral B cells. |
| Publication Title | Memoirs of the Faculty of Engineering, Okayama University |
| Published Date | 2002-03 |
| Volume | volume36 |
| Issue | issue2 |
| Start Page | 51 |
| End Page | 60 |
| ISSN | 0475-0071 |
| language | English |
| File Version | publisher |
| NAID | 80015582223 |
| 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 |
| Author | 曲 正樹| |
|---|---|
| Published Date | 2002-09-30 |
| Publication Title | |
| Content Type | Thesis or Dissertation |
