Results 61 to 70 of about 34,702 (278)

PalmPred: an SVM based palmitoylation prediction method using sequence profile information.

PLoS ONE, 2014
Protein palmitoylation is the covalent attachment of the 16-carbon fatty acid palmitate to a cysteine residue. It is the most common acylation of protein and occurs only in eukaryotes.
Bandana Kumari, Ravindra Kumar, Manish Kumar   +2 more
doaj   +1 more source

Palmitoylation of Hedgehog Proteins [PDF]

, 2012
Hedgehog (Hh) proteins are secreted signaling proteins that contain amide-linked palmitate at the N-terminus and cholesterol at the C-terminus. Palmitoylation of Hh proteins is critical for effective long- and short-range signaling. The palmitoylation reaction occurs during transit of Hh through the secretory pathway, most likely in the lumen of the ER.
John A, Buglino, Marilyn D, Resh
openaire   +2 more sources

Fas palmitoylation by the palmitoyl acyltransferase DHHC7 regulates Fas stability [PDF]

Cell Death & Differentiation, 2014
The death receptor Fas undergoes a variety of post-translational modifications including S-palmitoylation. This protein acylation has been reported essential for an optimal cell death signaling by allowing both a proper Fas localization in cholesterol and sphingolipid-enriched membrane nanodomains, as well as Fas high-molecular weight complexes.
Rossin, A, Durivault, J, Chakhtoura-Feghali, T, Lounnas, N, Gagnoux-Palacios, L, Hueber, A-O   +5 more
openaire   +3 more sources

Ufmylation‐Deficient DDRGK1 Ameliorates Obesity by Inhibiting FASN‐Mediated Adipocyte Lipogenesis

Advanced Science, EarlyView.
DDRGK1 regulates de novo lipogenesis via stabilization of fatty acid synthase (FASN). DDRGK1‐mediated UFMylation of FASN prevents its ubiquitin–proteasomal degradation. Reduced DDRGK1 expression or mutation at the key UFMylation site enhances FASN degradation and suppresses fatty acid synthesis (FAS), resulting in smaller adipocytes and improved ...
Yin Li, Tangjun Zhou, Xiao Yang, Kewei Rong, Xiankun Cao, Lei Shi, Xin Wang, Hongjin Wan, Lei Cui, Kexin Liu, Tong Xing, Hang Zhang, Chen Zhao, Tingxian Guo, Peixiang Ma, Jie Zhao, An Qin   +16 more
wiley   +1 more source

Posttranslational Protein Palmitoylation [PDF]

Arteriosclerosis, Thrombosis, and Vascular Biology, 2007
Posttranslational modification of proteins is the foundation of intracellular signaling. Without the ability to reversibly modify proteins and lipids, cells would be unable to react to signals received from their environment. Posttranslational modification of proteins usually, but not always, occurs after a protein has arrived at the appropriate ...
Adam D. Munday, José A. López
openaire   +1 more source

Chaperone‐Mediated Autophagic Degradation of USP9X in Macrophages Exacerbates Postmyocardial Infarction Inflammation and Cardiac Dysfunction

Advanced Science, EarlyView.
This study demonstrates that inflammatory stimuli induce the acetylation‐triggered, chaperone‐mediated autophagic degradation of ubiquitin‐specific peptidase 9 X‐linked (USP9X) in macrophages. USP9X acts as a macrophage “inflammation switch” after myocardial infarction (MI). USP9X loss destabilizes tumor necrosis factor receptor‐associated factor (TRAF)
Biqing Wang, Xiangheng Cai, Mengqi Li, Xue Liu, Junhui Xue, Ye Liu, Ding Ai, Xinyang Hu   +7 more
wiley   +1 more source

The Drosophila protein palmitoylome: Characterizing palmitoyl-thioesterases and DHHC palmitoyl-transferases [PDF]

Fly, 2008
Palmitoylation is the post-translational addition of a palmitate moiety to a cysteine residue through a covalent thioester bond. The addition and removal of this modification is controlled by both palmitoyl acyl-transferases and thioesterases. Using bioinformatic analysis, we identified 22 DHHC family palmitoyl acyl-transferase homologs in the ...
Barbra A, Bannan, Jamie, Van Etten, John A, Kohler, Yui, Tsoi, Nicole M, Hansen, Stacey, Sigmon, Elizabeth, Fowler, Haley, Buff, Tiffany S, Williams, Jeffrey G, Ault, Robert L, Glaser, Christopher A, Korey   +11 more
openaire   +2 more sources

SMAD4 Palmitoylation Drives a Metabolic‐Transcriptional Circuit to Promote Tumorigenesis and Confers Radiosensitivity in Pancreatic Cancer

Advanced Science, EarlyView.
This study identifies palmitoylation as a novel regulatory modification of SMAD4, mediated by ZDHHC22/APT2. It activates fatty acid synthesis, creating a self‐reinforcing SMAD4–FASN–palmitate feedback loop that drives pancreatic cancer growth and enhances radiotherapy sensitivity.
Yang Wang, Shan Zhang, Junping Bai, Xiaobing Li, Yi Han, Min Ji, Chongyi Jiang, Xiaobei Ge, Tianyu Yu, Yongying Hou, Jun Zhang, Wangting Li, Yiran Song, Jiaying Cai, Yingqun Zhou, Liwei An, Feng Wang   +16 more
wiley   +1 more source

Fibronectin rescues estrogen receptor α from lysosomal degradation in breast cancer cells [PDF]

, 2018
Estrogen receptor α (ERα) is expressed in tissues as diverse as brains and mammary glands. In breast cancer, ERα is a key regulator of tumor progression.
Acconcia, Acconcia, Acerbi, Adlanmerini, Alfredo Cáceres, Ambrose, Andrés M. Toscani, Arjonen, Arnal, Axelrod, Axelrod, Bacia, Bae, Barabas, Bates, Bermudez-Hernandez, Bonifacino, Bradford, Cancer Genome Atlas Network, Caswell, Cerami, Chaumet, Chung, Ciriello, Ciriello, Correia, Cosker, Cosker, Couse, Cox, Dante R. Chialvo, De Franceschi, Debnath, Degasperi, Delcroix, Dozynkiewicz, Dunn, Eirew, Federico Coluccio Leskow, Fernando D. Stefani, Gao, Gao, Ghajar, Gillespie, Gould, Graham, Grant, Han, Han, Hartley, He, Heery, Helleman, Hernández, Hines, Honerkamp-Smith, Ianina L. Violi, Jeselsohn, Johnson, Jonathon N. Lakins, Kate Thi, Kisler, La Rosa, Letoha, Levin, Li, Long, Lu, Lu, Luciano A. Masullo, Luzio, Mak, Marina Simian, Marino, Matthew G. Rubashkin, Mayor, Mayor, Małecki, McDonough, Mina J. Bissell, Moreno-Layseca, Nam, Nardone, Nicovich, Ovesný, Pedram, Pereira, Pietras, Pontiggia, Razandi, Reid, Rocío G. Sampayo, Rust, Savkur, Schindelin, Schlegel, Skliris, Solowska, Su, Sung, Takahashi, Tiwari, Totta, Totta, Upla, Valerie M. Weaver, van de Linde, Vanlandingham, Wang, Waxmonsky, William C. Hines, Yao   +111 more
core   +2 more sources

Biochemical Characterization of a Palmitoyl Acyltransferase Activity That Palmitoylates Myristoylated Proteins [PDF]

Journal of Biological Chemistry, 1995
Dynamic regulation of signal transduction by reversible palmitoylation-depalmitoylation cycles has been recently described. However, further understanding of fatty acylation reactions has been hampered by our lack of knowledge about the specific transferases and thioesterases involved.
L, Berthiaume, M D, Resh
openaire   +2 more sources