1. Kei SAOTOME - Anime News Network
Animation Director (ep 1) Obey Me! (ONA) : Animation Director (Mutsu Planning; eps 1, 5) Overlord III (TV) : Animation Director (eps 2, 9, 12-13), ...
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2. Saotome Kei | K-Pop Fanon Fandom Wiki
Bevat niet: net | Resultaten tonen met:net
Saotome Kei (Jap: 早乙女 圭, Kor: 사오토메 케이) is a Japanese Singer, Model currently based on South Korea under NEBULA+ and A PLUS Media. She debuted as a Soloist on September 8, 2020 with the Digital Single "Do I Have To". She is a member of the South Korean Girl Group UNISONE formed from the Survival Show Planetary Girls 100 where Kei ranked 8th overall. SLEN Japan (now A PLUS Media) on January 1, 2020, Revealed their new batch of Japanese Trainees with interest in promoting on South Korea. Saotome Ke
3. Kei Minamikaze (Daikessen!) | Getter Robo Wiki - Fandom
Bevat niet: net | Resultaten tonen met:net
Kei Minamikaze is a member of the Saotome Research Institute working as an extra pilot in the Getter Robo Daikessen! video game. Kei is a young woman standing at an average height and build with short, light orange colored hair that's pointed upwards. She possesses a unique pair of eyes that lack pupils and have pale blue irises. Kei is shown to be loyal to her team mates. Kei is a good pilot, having worked her way up the ranks to pilot Getter Machines. By inputing her name as "げんき”/Genki at the
4. Structural insights into CXCR4 modulation and oligomerization
10 feb 2024 · Structural insights into CXCR4 modulation and oligomerization. Kei Saotome, Luke L. McGoldrick, Jo-Hao Ho, Trudy F. Ramlall, Sweta Shah, Michael J. Moore, Jee ...
Activation of the chemokine receptor CXCR4 by its chemokine ligand CXCL12 regulates diverse cellular processes. CXCR4 also serves as a key target for diseases such as cancer and HIV. Previously reported crystal structures of CXCR4 bound to antagonists revealed the architecture of an inactive, homodimeric receptor. However, many structural aspects of CXCR4 remain poorly understood, including its activation by CXCL12, as well as its assembly into higher-order oligomers. Here, we use cryoelectron microscopy (cryoEM) to investigate various modes of CXCR4 regulation in the presence and absence of Gi protein. CXCL12 activates CXCR4 by inserting its N-terminus deep into the CXCR4 orthosteric pocket. The binding of FDA-approved antagonist AMD3100 is stabilized by electrostatic interactions with acidic residues in the 7 transmembrane helix bundle. A potent antibody blocker, REGN7663, binds across the extracellular face of CXCR4 and inserts its CDR-H3 loop into the orthosteric pocket. Trimeric and tetrameric structures of CXCR4 reveal, to our knowledge, previously undescribed modes of GPCR oligomerization. Remarkably, CXCR4 adopts distinct subunit conformations in trimeric and tetrameric assemblies, highlighting how oligomerization could allosterically regulate chemokine receptor function. ### Competing Interest Statement Regeneron authors own options and/or stock of the company. W.C.O. is an officer of Regeneron.
5. Kei Saotomé: Pianiste
Bevat niet: net work
Invitée par les scènes internationales, la pianiste Kei Saotomé séduit le public dans le monde entier par son jeu mêlé d’éléments contrastés, entre dynamisme, et sensibilité à fleur de peau, entre joie de vie et infinie mélancolie, ou encore entre virtuosité et profondeur presque religieuse.
6. Korea Environment Institute (KEI) | Green Policy Platform
The Korea Environment Institute (KEI) is the national leading think tank on environmental policies and environmental impact assessment in the Republic of ...
The Korea Environment Institute (KEI) is the national leading think tank on environmental policies and environmental impact assessment in the Republic of Korea. Established in 1993 by the Korean government, KEI has been at the heart of developing environment agendas through policy research and recommendations. With the vision to be the ‘world-class environmental policy research institute leading sustainable development,’ KEI is committed to providing proactive environmental policy research that can contribute to preventing and solving environmental problems.
7. Structural insights into CXCR4 modulation and oligomerization
23 sep 2024 · Structural insights into CXCR4 modulation and oligomerization. Kei Saotome ... work. Primary Handling Editor: Katarzyna Ciazynska, in ...
Activation of the chemokine receptor CXCR4 by its chemokine ligand CXCL12 regulates diverse cellular processes. Previously reported crystal structures of CXCR4 revealed the architecture of an inactive, homodimeric receptor. However, many structural aspects of CXCR4 remain poorly understood. Here, we use cryo-electron microscopy to investigate various modes of human CXCR4 regulation. CXCL12 activates CXCR4 by inserting its N terminus deep into the CXCR4 orthosteric pocket. The binding of US Food and Drug Administration-approved antagonist AMD3100 is stabilized by electrostatic interactions with acidic residues in the seven-transmembrane-helix bundle. A potent antibody blocker, REGN7663, binds across the extracellular face of CXCR4 and inserts its complementarity-determining region H3 loop into the orthosteric pocket. Trimeric and tetrameric structures of CXCR4 reveal modes of G-protein-coupled receptor oligomerization. We show that CXCR4 adopts distinct subunit conformations in trimeric and tetrameric assemblies, highlighting how oligomerization could allosterically regulate chemokine receptor function. Here, cryo-electron microscopy structures reveal how the chemokine receptor CXCR4 oligomerizes and how it is regulated by its physiological ligand CXCL12, the small-molecule drug AMD3100 and the monoclonal antibody REGN7663.
8. Structural analysis of cancer-relevant TCR-CD3 and peptide-MHC ...
26 apr 2023 · ... work. Peer reviewer reports are available. Data availability ... Kei Saotome, Email: kei.saotome@regeneron.com. Matthew C. Franklin ...
The recognition of antigenic peptide-MHC (pMHC) molecules by T-cell receptors (TCR) initiates the T-cell mediated immune response. Structural characterization is key for understanding the specificity of TCR-pMHC interactions and informing the ...
9. Swarthmore was well represented at the 2011 Biophysical Society ...
... Kei Saotome '11 and Patrick Hartnett '11. Also present but not in the ... Work at Swarthmore. Social Links. Site Feedback and Accessibility. If you have ...
Swarthmore Chemistry Major Kei Saotome '11 presented a poster describing his senior thesis research on the conformation of the influenza A M2 protein at the Biophysical Society meeting on March 8, 2011 at the Baltimore Convention Center. Swarthmore College's Howard Hughes Medical Institute grant and a Howard Lab NIH grant provided funding for the trip.
10. Structural characterization of two full length γδ TCR/CD3 complexes
19 jul 2024 · Franklin, Tong Zhang, Kei Saotome. doi: https://doi.org/10.1101/2024.07.19.604350. This article is a preprint and has not been certified by ...
The T-cell receptor (TCR)/CD3 complex plays an essential role in the immune response and is a key player in cancer immunotherapies. There are two classes of TCR/CD3 complexes, defined by their TCR chain usage (αβ or γδ). Recently reported structures have revealed the organization of the αβ TCR/CD3 complex, but similar studies regarding the γδ TCR/CD3 complex have lagged behind. Here, we report cryoelectron microscopy (cryoEM) structural analysis of two full-length γδ TCRs, G115 (Vγ9Vδ2) and 9C2 (Vγ5Vδ1), in complex with CD3 subunits. Our results show that the overall subunit organization of the γδ TCR-CD3 complexes is similar to αβ TCRs. However, both γδ TCRs display highly mobile extracellular domains (ECDs), unlike αβ TCRs, which have TCR ECDs that are rigidly coupled to its transmembrane (TM) domains. We corroborate this finding in cells by demonstrating that a γδ T-cell specific antibody can bind a site that would be inaccessible in the more rigid αβ TCR/CD3 complex. Furthermore, we observed that a Vγ5Vδ1 complex forms a TCR γ5-chain mediated dimeric species whereby two TCR/CD3 complexes are assembled. Collectively, these data shed light on γδ TCR/CD3 complex formation and may aid the design of γδ TCR-based therapies. ### Competing Interest Statement All authors are employees of Regeneron Pharmaceuticals and own options and/or stock. J.C.L. and W.C.O. are officers of Regeneron.
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