Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Marie-Anne Pringle"'
Autor:
Juan Manuel Iglesias, Claire J Cairney, Roderick K Ferrier, Laura McDonald, Kelly Soady, Howard Kendrick, Marie-Anne Pringle, Reginald O Morgan, Finian Martin, Matthew J Smalley, Karen Blyth, Torsten Stein
Publikováno v:
PLoS ONE, Vol 10, Iss 3, p e0119718 (2015)
We have previously shown that Annexin A8 (ANXA8) is strongly associated with the basal-like subgroup of breast cancers, including BRCA1-associated breast cancers, and poor prognosis; while in the mouse mammary gland AnxA8 mRNA is expressed in low-pro
Externí odkaz:
https://doaj.org/article/bf01c0a98e5948528c6de9937ed9455a
Publikováno v:
Journal of Cell Science. 136
Proteins entering the secretory pathway need to attain native disulfide pairings to fold correctly. For proteins with complex disulfides, this process requires the reduction and isomerisation of non-native disulfides. Two key members of the protein d
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::80b328dfaa295c11874e1779bdf6fe16
https://doi.org/10.1242/jcs.260656
https://doi.org/10.1242/jcs.260656
Autor:
Ojore Benedict Valentine Oka, Arvin Shedrach Pierre, Marie Anne Pringle, Wanida Tungkum, Zhenbo Cao, Bethany Fleming, Neil John Bulleid
The unfolded protein response (UPR) maintains cellular proteostasis during stress by activating sensors located to the endoplasmic reticulum (ER) membrane. A major sensor for this response, ATF6α, is activated by release from ER retention and traffi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::53d7c6c7d46874b4b887a7ca41c4b7b8
https://eprints.gla.ac.uk/265205/1/265205.pdf
https://eprints.gla.ac.uk/265205/1/265205.pdf
Autor:
Jisu Im, Bethany Fleming, Marcel van Lith, Neil J. Bulleid, Marie Anne Pringle, Giorgia Gaeta, Reid Gilmore
N-linked glycosylation of proteins entering the secretory pathway is an essential post-translational modification required for protein stability and function. Previously, it has been shown that there is a temporal relationship between protein folding
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d95af0d1ae9dc2dfb76376352d2e427f
https://doi.org/10.1101/2021.08.31.458373
https://doi.org/10.1101/2021.08.31.458373
Autor:
Giorgia Gaeta, Jisu Im, Marcel van Lith, Reid Gilmore, Neil J. Bulleid, Marie Anne Pringle, Bethany Fleming
Publikováno v:
Journal of Cell Science
article-version (VoR) Version of Record
article-version (VoR) Version of Record
N-linked glycosylation of proteins entering the secretory pathway is an essential modification required for protein stability and function. Previously, it has been shown that there is a temporal relationship between protein folding and glycosylation,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1b24f777f8582c4049214a8f8997d157
https://pubmed.ncbi.nlm.nih.gov/34734627
https://pubmed.ncbi.nlm.nih.gov/34734627
Autor:
Sara Zanivan, Philip Robinson, Zhenbo Cao, Sergio Lilla, Xiaofei Cao, Tomasz Szmaja, Neil J. Bulleid, Ojore B. V. Oka, Marie Anne Pringle, Marcel van Lith
Publikováno v:
Journal of Cell Science
article-version (VoR) Version of Record
article-version (VoR) Version of Record
Folding of proteins entering the mammalian secretory pathway requires the insertion of the correct disulfides. Disulfide formation involves both an oxidative pathway for their insertion and a reductive pathway to remove incorrectly formed disulfides.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f984ccd87acdb9ba5d3e09f442e36ef1
Autor:
Marcel van Lith, Kenji Inaba, Zhenbo Cao, Marie Anne Pringle, Lorna J Mitchell, Neil J. Bulleid
Publikováno v:
Biochemical Journal. 473:851-858
The membrane topology of vitamin K epoxide reductase (VKOR) is controversial with data supporting both a three transmembrane and a four transmembrane model. The positioning of the transmembrane domains and the loops between these domains is critical
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::377ffa483ac657ad21e1e92abd46cfd0
https://doi.org/10.1042/bj20151223
https://doi.org/10.1042/bj20151223
Autor:
Greg J, Poet, Ojore Bv, Oka, Marcel, van Lith, Zhenbo, Cao, Philip J, Robinson, Marie Anne, Pringle, Elias Sj, Arnér, Neil J, Bulleid
Publikováno v:
The EMBO Journal
Folding of proteins entering the secretory pathway in mammalian cells frequently requires the insertion of disulfide bonds. Disulfide insertion can result in covalent linkages found in the native structure as well as those that are not, so‐called n
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::bf2fc023df07b11a4462f9c8d7a71bcc
https://pubmed.ncbi.nlm.nih.gov/28093500
https://pubmed.ncbi.nlm.nih.gov/28093500
Autor:
Camille Huser, Laura McDonald, François Vaillant, Ewan R. Cameron, Karen Blyth, Marie Anne Pringle, Torsten Stein, James C. Neil, Alma Jenkins
Publikováno v:
Blood Cells, Molecules, and Diseases. 45:117-123
The Runx transcription factors are essential for mammalian development, most notably in the haematopoietic and osteogenic lineages. Runx1 and its binding partner, CBFbeta, are frequently targeted in acute leukaemia but evidence is accumulating that a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::749d2fa5d1cb1dbfdb25c2549eb71aaa
https://doi.org/10.1016/j.bcmd.2010.05.007
https://doi.org/10.1016/j.bcmd.2010.05.007
Autor:
Camille Huser, Barry A. Gusterson, Howard Kendrick, Victoria J. Heath, Torsten Stein, Diane Crighton, Kevin M. Ryan, Alexandra K. Bell, Marie Anne Pringle, Matthew J. Smalley
Publikováno v:
Cell Death & Differentiation. 17:304-315
Transforming growth factor beta (TGFbeta)-stimulated clone-22 domain family member 1 (TSC-22D1) has previously been associated with enhanced apoptosis in several cell systems. In an attempt to identify novel factors that are involved in the control o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a5d62723706521b25e38b997ada6fac7
https://doi.org/10.1038/cdd.2009.126
https://doi.org/10.1038/cdd.2009.126