Zobrazeno 1 - 10
of 26
pro vyhledávání: '"Suzanne J, Randle"'
Autor:
David B. Chou, Brooke A. Furlong, Ryan R. Posey, Christos Kyprianou, Lucy R. O’Sullivan, Rhiannon David, Suzanne J. Randle, Urszula M. Polanska, Jon Travers, Jelena Urosevic, John N. Hutchinson, Jianwei Che, Anna M. Howley, Robert P. Hasserjian, Rachelle Prantil-Baun, Donald E. Ingber
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-10 (2022)
Patients treated with Aurora kinase inhibitors experience dose-limiting neutropenia while other cytopenias are rare. Here, Chou et al. show that this cell-type specific side effect is partly explained by loss of drug efflux pump expression during neu
Externí odkaz:
https://doaj.org/article/30b138eaa22049aea33459bc0a7f87f2
Autor:
Claudia C. Rathje, Suzanne J. Randle, Sara Al Rawi, Benjamin M. Skinner, David E. Nelson, Antara Majumdar, Emma E. P. Johnson, Joanne Bacon, Myrto Vlazaki, Nabeel A. Affara, Peter J. Ellis, Heike Laman
Publikováno v:
Frontiers in Physiology, Vol 10 (2019)
Fbxo7 is the substrate-recognition subunit of an SCF-type ubiquitin E3 ligase complex. It has physiologically important functions in regulating mitophagy, proteasome activity and the cell cycle in multiple cell types, like neurons, lymphocytes and er
Externí odkaz:
https://doaj.org/article/bf91cd19ddc4493c928825893fa10f43
Publikováno v:
Biochemical and Biophysical Research Communications
Fbxo7 is a key player in the differentiation and function of numerous blood cell types, and in neurons, oligodendrocytes and spermatocytes. In an effort to gain insight into the physiological and pathological settings where Fbxo7 is likely to play a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::008b85e63d51ba5831950b532c6288fe
https://pubmed.ncbi.nlm.nih.gov/33774278
https://pubmed.ncbi.nlm.nih.gov/33774278
Autor:
Patrícia Maria Siqueira dos Passos, Natália Borges Simaroli, Felipe R. Teixeira, Tycho E. T. Mevissen, Joice S. Oliveira, Marcelo D. Gomes, Heike Laman, Valentine Spagnol, Camila R.S.T.B. de Correia, Suzanne J. Randle, David Komander, Caio Almeida Batista de Oliveira, Ana C. Medeiros
Publikováno v:
Repositório Institucional da USP (Biblioteca Digital da Produção Intelectual)
Universidade de São Paulo (USP)
instacron:USP
Biochimica et Biophysica Acta. General Subjects
Universidade de São Paulo (USP)
instacron:USP
Biochimica et Biophysica Acta. General Subjects
Background Ubiquitously eXpressed Transcript isoform 2 (UXT—V2) is a prefoldin-like protein involved in NF-κB signaling, apoptosis, and the androgen and estrogen response. UXT-V2 is a cofactor in the NF-κB transcriptional enhanceosome, and its kn
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::75f95f5b0ac07eecea9d520eac11761e
https://www.repository.cam.ac.uk/handle/1810/310834
https://www.repository.cam.ac.uk/handle/1810/310834
Publikováno v:
Open Biology, Vol 3, Iss 10 (2013)
F-box proteins (FBPs) are substrate-recruiting subunits of Skp1-cullin1-FBP (SCF)-type E3 ubiquitin ligases. To date, 69 FBPs have been identified in humans, but ubiquitinated substrates have only been identified for a few, with the majority of FBPs
Externí odkaz:
https://doaj.org/article/bcf47db3c0b24e94a66f70867008e51a
Autor:
Mikhail Lomonosov, El Kahina Meziane, Hongtao Ye, David E Nelson, Suzanne J Randle, Heike Laman
Publikováno v:
PLoS ONE, Vol 6, Iss 6, p e21165 (2011)
Fbxo7 is an unusual F box protein that augments D-type cyclin complex formation with Cdk6, but not Cdk4 or Cdk2, and its over-expression has been demonstrated to transform immortalised fibroblasts in a Cdk6-dependent manner. Here we present new evide
Externí odkaz:
https://doaj.org/article/153ac863f59348c4b49bbdc5327612de
Autor:
Suzanne J. Randle, Heike Laman
Fbxo7 is a key player in the differentiation and function of numerous blood cell types, and in neurons, oligodendrocytes and spermatocytes. In an effort to gain insight into the physiological and pathological settings where Fbxo7 is likely to play a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::af1a76e871823382c9697ddc8840a827
Autor:
Suzanne J. Randle, Joanne Bacon, Nabeel A. Affara, Heike Laman, Emma Elizabeth Philippa Johnson, Claudia Cattoni Rathje, David E. Nelson, Antara Majumdar, Benjamin M. Skinner, Myrto Vlazaki, Sara Al Rawi, Peter J. I. Ellis
Publikováno v:
Frontiers in Physiology
Frontiers in Physiology, Vol 10 (2019)
Frontiers in Physiology, Vol 10 (2019)
Fbxo7 is the substrate-recognition subunit of an SCF-type ubiquitin E3 ligase complex. It has physiologically important functions in regulating mitophagy, proteasome activity and the cell cycle in multiple cell types, like neurons, lymphocytes and er
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::026f44abddd98197c8077719c6884439
http://europepmc.org/articles/PMC6795710
http://europepmc.org/articles/PMC6795710
Publikováno v:
Cellular and Molecular Life Sciences
G1 phase cell cycle proteins, such as cyclin-dependent kinase 6 (Cdk6) and its activating partners, the D-type cyclins, are important regulators of T-cell development and function. An F-box protein, called F-box only protein 7 (Fbxo7), acts as a cell
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::28bc6d8848fd25085672bd191a86e974
https://doi.org/10.1007/s00018-016-2427-3
https://doi.org/10.1007/s00018-016-2427-3
Autor:
Peter, St George-Hyslop, Julie Qiaojin, Lin, Akinori, Miyashita, Emma C, Phillips, Seema, Qamar, Suzanne J, Randle, GuoZhen, Wang
Publikováno v:
Brain Research
Graphical abstract
Highlights • Some intrinsically disordered proteins undergo reversible phase separation/gelation. • Reversible phase separation/gelation underpins function of membraneless organelles. • fALS-FUS mutations increase propen
Highlights • Some intrinsically disordered proteins undergo reversible phase separation/gelation. • Reversible phase separation/gelation underpins function of membraneless organelles. • fALS-FUS mutations increase propen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::d7c33cdb5ca19f9cf1f4a371dcd4e851
https://pubmed.ncbi.nlm.nih.gov/29723523
https://pubmed.ncbi.nlm.nih.gov/29723523