Zobrazeno 1 - 10
of 69
pro vyhledávání: '"Tomoaki Niimi"'
Autor:
Yoichi Nakanishi, Syuntaro Iida, Hanayo Ueoka-Nakanishi, Tomoaki Niimi, Rie Tomioka, Masayoshi Maeshima
Publikováno v:
PLoS ONE, Vol 8, Iss 3, p e58175 (2013)
Molybdenum (Mo) is an essential trace element for almost all living organisms including animals. Mo is used as a catalytic center of molybdo-enzymes for oxidation/reduction reactions of carbon, nitrogen, and sulfur metabolism. Whilst living cells are
Externí odkaz:
https://doaj.org/article/a137e5d9be294ec2af2d94524ff22d2f
Publikováno v:
Journal of Molecular Biology. 434:167777
Since neural epidermal growth factor-like-like (NELL) 2 was identified as a novel ligand for the roundabout (Robo) 3 receptor, research on NELL-Robo signaling has become increasingly important. We have previously reported that Robo2 can bind to NELL1
Autor:
Tomoaki, Niimi
Publikováno v:
Advances in experimental medicine and biology. 21
Slit guidance ligands (Slits) and their roundabout (Robo) family of receptors are well-known axon guidance molecules that were originally identified in Drosophila mutants with commissural axon pathfinding defects. However, Slit-Robo signaling has bee
Autor:
Tomoaki Niimi
Publikováno v:
Advances in Experimental Medicine and Biology ISBN: 9783030678135
Slit guidance ligands (Slits) and their roundabout (Robo) family of receptors are well-known axon guidance molecules that were originally identified in Drosophila mutants with commissural axon pathfinding defects. However, Slit-Robo signaling has bee
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f6fb18e52f9ce1b17666697d91b82a1b
https://doi.org/10.1007/5584_2020_586
https://doi.org/10.1007/5584_2020_586
Publikováno v:
International Journal of Molecular Sciences
The CACNA1C gene encodes for the CaV1.2 protein, which is the pore subunit of cardiac l-type voltage-gated calcium (Ca2+) channels (l-channels). Through alternative splicing, CACNA1C encodes for various CaV1.2 isoforms with different electrophysiolog
Autor:
Yoshitaka Fujihara, Tomoaki Niimi, Tomomi Minemura, Shun'ichi Kuroda, Koichi Takimoto, Sébastien Wälchli, Jumpei Ito, Andrés D. Maturana
Publikováno v:
International Journal of Molecular Sciences
Volume 22
Issue 7
International Journal of Molecular Sciences, Vol 22, Iss 3561, p 3561 (2021)
Volume 22
Issue 7
International Journal of Molecular Sciences, Vol 22, Iss 3561, p 3561 (2021)
Aldosterone excess is a cardiovascular risk factor. Aldosterone can directly stimulate an electrical remodeling of cardiomyocytes leading to cardiac arrhythmia and hypertrophy. L-type and T-type voltage-gated calcium (Ca2+) channels expression are in
Autor:
Nobuo Yoshimoto, Riko Koyama, Shun'ichi Kuroda, Jumpei Ito, Andrés D. Maturana, Tomoaki Niimi, Miyuki Nakatani, Masumi Iijima
Publikováno v:
Biochemical and Biophysical Research Communications. 474:413-420
Enigma Homolog 1 (ENH1) is a scaffold protein for signaling proteins and transcription factors. Previously, we reported that ENH1 overexpression promotes the differentiation of C2C12 myoblasts. However, the molecular mechanism underlying the role of
Autor:
Kaneyoshi Takahashi, Nobuo Yoshimoto, Masumi Iijima, Arisa Imai, Shun'ichi Kuroda, Tomoaki Niimi, Andrés D. Maturana
Publikováno v:
FEBS Letters. 589:4026-4032
Neural epidermal growth factor-like (NEL)-like 1 (NELL1) is a secretory osteogenic protein comprising an N-terminal thrombospondin-1-like (TSPN) domain, four von Willebrand factor type C domains, and six epidermal growth factor-like repeats. NELL1 sh
Autor:
Nobuo Yoshimoto, Shun'ichi Kuroda, Yoko Nakamura, Andrés D. Maturana, Masumi Iijima, Tomoaki Niimi, Kaneyoshi Takahashi, Ai Hasebe, Kang Ting
Publikováno v:
Journal of Biological Chemistry. 289:9781-9794
NELL1 is a large oligomeric secretory glycoprotein that functions as an osteoinductive factor. NELL1 contains several conserved domains, has structural similarities to thrombospondin 1, and supports osteoblastic cell adhesion through integrins. To de
Publikováno v:
International Journal of Molecular Sciences, Vol 20, Iss 22, p 5591 (2019)
International Journal of Molecular Sciences
Volume 20
Issue 22
International Journal of Molecular Sciences
Volume 20
Issue 22
The CACNA1C gene encodes for the CaV1.2 protein, which is the pore subunit of cardiac l-type voltage-gated calcium (Ca2+) channels (l-channels). Through alternative splicing, CACNA1C encodes for various CaV1.2 isoforms with different electrophysiolog