Results 51 to 60 of about 21,138,684 (162)

Investigating the mechanisms and outcomes of Sprouty-2 S-acylation [PDF]

, 2021
S-acylation is a reversible post-translational modification (PTM) that regulates proteins in several ways, including by modulating trafficking, stability and protein interactions. This PTM is mediated by twenty-three zinc finger DHHC (zDHHC) enzymes that
Locatelli, Carolina
core   +2 more sources

S-acylation dependent post-translational cross-talk regulates large conductance calcium- and voltage- activated potassium (BK) channels

Frontiers in Physiology, 2014
Mechanisms that control surface expression and/or activity of large conductance calcium-activated potassium (BK) channels are important determinants of their (patho)physiological function.
Michael J Shipston
doaj   +1 more source

Comprehensive palmitoyl-proteomic analysis identifies distinct protein signatures for large and small cancer-derived extracellular vesicles

Journal of Extracellular Vesicles, 2020
Extracellular vesicles (EVs) are membrane-enclosed particles that play an important role in cancer progression and have emerged as a promising source of circulating biomarkers. Protein S-acylation, frequently called palmitoylation, has been proposed as a
Javier Mariscal, Tatyana Vagner, Minhyung Kim, Bo Zhou, Andrew Chin, Mandana Zandian, Michael R. Freeman, Sungyong You, Andries Zijlstra, Wei Yang, Dolores Di Vizio   +10 more
doaj   +1 more source

2-Bromopalmitate reduces protein deacylation by inhibition of acyl-protein thioesterase enzymatic activities. [PDF]

PLoS ONE, 2013
S-acylation, the covalent attachment of palmitate and other fatty acids on cysteine residues, is a reversible post-translational modification that exerts diverse effects on protein functions.
Maria P Pedro, Aldo A Vilcaes, Vanesa M Tomatis, Rafael G Oliveira, Guillermo A Gomez, Jose L Daniotti   +5 more
doaj   +1 more source

New links between S-acylation and cancer

, 2014
S-acylation (also known as palmitoylation) is a major post-translational protein modification in all eukaryotic cells, involving the attachment of fatty acids onto cysteine residues.
Chamberlain, Luke, Greaves, Jennifer
core   +4 more sources

Dynamic S-acylation of IDH2 regulates mitochondrial redox homeostasis

Cell Reports
Summary: Mitochondrial redox homeostasis is fundamental for cellular function, and its dysregulation is associated with various diseases, including cancer. Isocitrate dehydrogenase 2 (IDH2) is a key enzyme that maintains this balance by generating NADPH.
Chen Miao, Zhen Wang, Jian Lin, Ziye Zhu, Jinan Wang, Baoen Chen   +5 more
doaj   +1 more source

FoxO1-zDHHC4-CD36 S-Acylation Axis Drives Metabolic Dysfunction in Diabetes. [PDF]

Circ Res
BACKGROUND: The fatty acid (FA) transporter CD36 (FA translocase/cluster of differentiation 36) is the gatekeeper of cardiac FA metabolism. Preferential localization of CD36 to the sarcolemma is one of the initiating cellular responses in the development
Dennis KMJH, Gopal K, Montes Aparicio CN, Zhang JA, Castro-Guarda M, Nicol T, Devereux RM, Carter RD, Azizi SA, Lan T, Purnama U, Carr CA, Simsek G, Gill EK, Swietach P, Sorop O, Heinonen IHA, Schianchi F, Luiken JJFP, Aksentijevic D, Duncker DJ, Dickinson BC, De Val S, Ussher JR, Fuller W, Heather LC.   +25 more
europepmc   +2 more sources

Technologies and Challenges in Proteomic Analysis of Protein S-acylation [PDF]

Journal of Proteomics & Bioinformatics, 2014
Protein S-acylation (also called palmitoylation) is a pervasive post-translational modification that plays critical roles in regulating protein trafficking, localization, stability, activity, and complex formation. The past decade has witnessed tremendous advances in the study of protein S-acylation, largely owing to the development of novel S ...
Zhou, Bo, An, Mingrui, Freeman, Michael R, Yang, Wei   +3 more
openaire   +2 more sources

Metabolically controlled histone H4K5 acylation/acetylation ratio drives BRD4 genomic distribution

Cell Reports, 2021
Summary: In addition to acetylation, histones are modified by a series of competing longer-chain acylations. Most of these acylation marks are enriched and co-exist with acetylation on active gene regulatory elements.
Mengqing Gao, Jin Wang, Sophie Rousseaux, Minjia Tan, Lulu Pan, Lijun Peng, Sisi Wang, Wenqian Xu, Jiayi Ren, Yuanfang Liu, Martin Spinck, Sophie Barral, Tao Wang, Florent Chuffart, Ekaterina Bourova-Flin, Denis Puthier, Sandrine Curtet, Lisa Bargier, Zhongyi Cheng, Heinz Neumann, Jian Li, Yingming Zhao, Jian-Qing Mi, Saadi Khochbin   +23 more
doaj   +1 more source

Dynamic acylome reveals metabolite driven modifications in Syntrophomonas wolfei

Frontiers in Microbiology, 2022
Syntrophomonas wolfei is an anaerobic syntrophic microbe that degrades short-chain fatty acids to acetate, hydrogen, and/or formate. This thermodynamically unfavorable process proceeds through a series of reactive acyl-Coenzyme A species (RACS). In other
Janine Y. Fu, John M. Muroski, Mark A. Arbing, Jessica A. Salguero, Neil Q. Wofford, Michael J. McInerney, Robert P. Gunsalus, Robert P. Gunsalus, Robert P. Gunsalus, Joseph A. Loo, Joseph A. Loo, Joseph A. Loo, Joseph A. Loo, Rachel R. Ogorzalek Loo, Rachel R. Ogorzalek Loo, Rachel R. Ogorzalek Loo   +15 more
doaj   +1 more source