Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Ventzislava A. Hristova"'
Autor:
Ventzislava A. Hristova, Alastair Watson, Raghothama Chaerkady, Matthew S. Glover, Jodie Ackland, Bastian Angerman, Graham Belfield, Maria G. Belvisi, Hannah Burke, Doriana Cellura, Howard W. Clark, Damla Etal, Anna Freeman, Ashley I. Heinson, Sonja Hess, Michael Hühn, Emily Hall, Alex Mackay, Jens Madsen, Christopher McCrae, Daniel Muthas, Steven Novick, Kristoffer Ostridge, Lisa Öberg, Adam Platt, Anthony D. Postle, C. Mirella Spalluto, Outi Vaarala, Junmin Wang, Karl J. Staples, Tom M.A. Wilkinson, on behalf of the MICA II Study group
Publikováno v:
ERJ Open Research, Vol 9, Iss 3 (2022)
Rationale Pulmonary surfactant is vital for lung homeostasis as it reduces surface tension to prevent alveolar collapse and provides essential immune-regulatory and antipathogenic functions. Previous studies demonstrated dysregulation of some individ
Externí odkaz:
https://doaj.org/article/d0133b7993c74d2bbea08bf595e4130e
Autor:
Helge M. Magnussen, Syed F. Ahmed, Gary. J. Sibbet, Ventzislava A. Hristova, Koji Nomura, Andreas K. Hock, Lewis J. Archibald, Andrew G. Jamieson, David Fushman, Karen H. Vousden, Allan M. Weissman, Danny T. Huang
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-15 (2020)
p53 is an important tumor suppressor protein which is regulated by the E3 ubiquitin ligase MDM2. Here the authors reveal that DNA damage-induced Ser429 phosphorylation of MDM2 serve to boost the activity of MDM2 homodimer by stabilizing the active E2
Externí odkaz:
https://doaj.org/article/80e8bf383dda460bb88d16b6b1cd6555
Publikováno v:
Expert Review of Proteomics. 16:93-103
INTRODUCTION: Cancer is often diagnosed at late stages when the chance of cure is relatively low and although research initiatives in oncology discover many potential cancer biomarkers, few transition to clinical applications. This review addresses t
Publikováno v:
Clinical Proteomics
Background Ubiquitination is a post-translational modification where ubiquitin is covalently attached to lysine residues on substrate proteins to signal their degradation by the 26S proteasome or initiate other non-degradation functions such as cellu
Autor:
Syed Faisal Ahmed, Andrew G. Jamieson, Andreas K. Hock, Helge M. Magnussen, Karen H. Vousden, Ventzislava A. Hristova, Lewis J. Archibald, Danny T. Huang, Gary J. Sibbet, Koji Nomura, David Fushman, Allan M. Weissman
Publikováno v:
Nature Communications
Nature Communications, Vol 11, Iss 1, Pp 1-15 (2020)
Nature Communications, Vol 11, Iss 1, Pp 1-15 (2020)
Phosphorylation of MDM2 by ATM upon DNA damage is an important mechanism for deregulating MDM2, thereby leading to p53 activation. ATM phosphorylates multiple residues near the RING domain of MDM2, but the underlying molecular basis for deregulation
Publikováno v:
Clinical Proteomics
Background Ubiquitination is a post-translational modification where ubiquitin is covalently attached to lysine residues on substrate proteins to signal their degradation by the 26S proteasome or initiate other non-degradation functions such as cellu
Health care is increasingly challenged by issues of clinically managing obese patients; this is of increased interest because the proportion of obese people in the general population is higher than ever and continues to increase. Obesity impacts the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c18f8f52a8add188ab70e6ba727f410d
https://doi.org/10.1016/b978-0-12-802025-8.00010-6
https://doi.org/10.1016/b978-0-12-802025-8.00010-6
Publikováno v:
Journal of Cell Science. 125:531-537
The post-translational attachment of ubiquitin, a highly conserved 76-amino-acid polypeptide, directs myriad eukaryotic proteins to a variety of fates and functions. Ubiquitylation is best-known for targeting proteins for degradation by the 26S prote
Publikováno v:
Proceedings of the National Academy of Sciences. 104:3095-3100
Mutations in Parkin are one of the predominant hereditary factors found in patients suffering from autosomal recessive juvenile Parkinsonism. Parkin is a member of the E3 ubiquitin ligase family that is defined by a tripartite RING1-in-between-ring (
Insights into Ubiquitination from the Unique Clamp-like Binding of the RING E3 AO7 to the E2 UbcH5B*
Autor:
Meredith B. Metzger, Daniel K. Stringer, Jess Li, Allan M. Weissman, Jennifer Mariano, Yu-He Liang, Yien Che Tsai, Ventzislava A. Hristova, Shengjian Li, Xinhua Ji, Paul A. Randazzo
RING proteins constitute the largest class of E3 ubiquitin ligases. Unlike most RINGs, AO7 (RNF25) binds the E2 ubiquitin-conjugating enzyme, UbcH5B (UBE2D2), with strikingly high affinity. We have defined, by co-crystallization, the distinctive mean
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::af940272e730a82913133b796ed68b0c
https://europepmc.org/articles/PMC4683248/
https://europepmc.org/articles/PMC4683248/