Zobrazeno 1 - 7
of 7
pro vyhledávání: '"W Grant, Ludlam"'
Autor:
Kevin M. Knight, Brian E. Krumm, Nicholas J. Kapolka, W. Grant Ludlam, Meng Cui, Sepehr Mani, Iya Prytkova, Elizabeth G. Obarow, Tyler J. Lefevre, Wenyuan Wei, Ning Ma, Xi-Ping Huang, Jonathan F. Fay, Nagarajan Vaidehi, Alan V. Smrcka, Paul A. Slesinger, Diomedes E. Logothetis, Kirill A. Martemyanov, Bryan L. Roth, Henrik G. Dohlman
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-18 (2024)
Abstract Many neurotransmitter receptors activate G proteins through exchange of GDP for GTP. The intermediate nucleotide-free state has eluded characterization, due largely to its inherent instability. Here we characterize a G protein variant associ
Externí odkaz:
https://doaj.org/article/a1bbb4b8f5a447f79e49586a70a5bd73
Autor:
Jorge Cuéllar, W. Grant Ludlam, Nicole C. Tensmeyer, Takuma Aoba, Madhura Dhavale, César Santiago, M. Teresa Bueno-Carrasco, Michael J. Mann, Rebecca L. Plimpton, Aman Makaju, Sarah Franklin, Barry M. Willardson, José M. Valpuesta
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-14 (2019)
β-propeller domains are an important class of folding substrates for the eukaryotic cytosolic chaperonin CTT. Here the authors find that CTT contributes to the folding and assembly of two β-propeller proteins from mTOR complexes, mLST8 and Raptor,
Externí odkaz:
https://doaj.org/article/23eeb432bf314670b0ab58f513d2d7e9
Autor:
Shuxin Wang, Mikaila I. Sass, Yujin Kwon, W. Grant Ludlam, Theresa M. Smith, Ethan J. Carter, Nathan E. Gladden, Margot Riggi, Janet H. Iwasa, Barry M. Willardson, Peter S. Shen
Publikováno v:
bioRxiv
SUMMARYThe cytosolic Chaperonin Containing Tailless polypeptide 1 (CCT) complex is an essential protein folding machine with a diverse clientele of substrates, including many proteins with β- propeller domains. Here, we determined structures of CCT
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c741741a50baa357305f450c8e1904b9
https://doi.org/10.1101/2023.05.04.539424
https://doi.org/10.1101/2023.05.04.539424
Autor:
Barry M. Willardson, M. Teresa Bueno-Carrasco, José M. Valpuesta, Sarah Franklin, Takuma Aoba, Jorge Cuéllar, W. Grant Ludlam, Aman Makaju, James D. Moody
Publikováno v:
Digital.CSIC. Repositorio Institucional del CSIC
instname
Digital.CSIC: Repositorio Institucional del CSIC
Consejo Superior de Investigaciones Científicas (CSIC)
J Biol Chem
instname
Digital.CSIC: Repositorio Institucional del CSIC
Consejo Superior de Investigaciones Científicas (CSIC)
J Biol Chem
© 2019 Ludlam et al.
Bardet-Biedl syndrome (BBS) is a genetic disorder characterized by malfunctions in primary cilia resulting from mutations that disrupt the function of the BBSome, an 8-subunit complex that plays an important role in protein
Bardet-Biedl syndrome (BBS) is a genetic disorder characterized by malfunctions in primary cilia resulting from mutations that disrupt the function of the BBSome, an 8-subunit complex that plays an important role in protein
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3f2a4c1c6315fe3b5cd6541a5c280547
http://hdl.handle.net/10261/240872
http://hdl.handle.net/10261/240872
Autor:
Namath S. Hussain, Mackenzie Piper, Marc R. Mayberg, William H. Ludlam, Cindy J. Fuller, W Grant Ludlam
Publikováno v:
Journal of Neurosurgery. 119:1453-1460
Object Transient delayed postoperative hyponatremia (DPH) after transsphenoidal surgery (TSS) is common and can have potentially devastating consequences. However, the true prevalence of transient symptomatic and asymptomatic DPH has not been studied
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2234a0dc0942e7bcdd6ac048d496bedd
https://doi.org/10.3171/2013.8.jns13411
https://doi.org/10.3171/2013.8.jns13411
Akademický článek
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Autor:
Jorge Cuéllar, Josefine Vallin, Andreas Svanström, Moisés Maestro-López, María Teresa Bueno-Carrasco, W. Grant Ludlam, Barry M. Willardson, José M. Valpuesta, Julie Grantham
Publikováno v:
J Mol Biol
The actin filament severing and capping protein gelsolin plays an important role in modulation of actin filament dynamics by influencing the number of actin filament ends. During apoptosis, gelsolin becomes constitutively active due to cleavage by ca
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::00748966d212889108ffab734758bee2