Results 81 to 90 of about 15,262 (93)
Some of the next articles are maybe not open access.
Protein S-palmitoylation and cancer
Biochimica et Biophysica Acta (BBA) - Reviews on Cancer, 2015Protein S-palmitoylation is a reversible posttranslational modification of proteins with fatty acids, an enzymatic process driven by a recently discovered family of protein acyltransferases (PATs) that are defined by a conserved catalytic domain characterized by a DHHC sequence motif.
Maurine E. Linder +2 more
openaire +2 more sources
Science Signaling, 2020
Interrupting the palmitoylation-depalmitoylation cycle of the transcriptional regulator STAT3 relieves IBD symptoms in mice.
openaire +2 more sources
Interrupting the palmitoylation-depalmitoylation cycle of the transcriptional regulator STAT3 relieves IBD symptoms in mice.
openaire +2 more sources
Assays of protein palmitoylation
Methods, 2006Protein palmitoylation plays an important role in the structure and function of a wide array of proteins. Unlike other lipid modifications, protein palmitoylation is highly dynamic and cycles of palmitoylation and depalmitoylation can regulate protein function and localization.
Renaldo C. Drisdel +3 more
openaire +3 more sources
Palmitoylation of serotonin receptors
Biochemical Society Transactions, 2013The covalent attachment of palmitic acid to one or more cysteine residues (S-palmitoylation) is a widespread modification of signalling proteins. With the finding that palmitoylation is a dynamic process, it is now widely accepted that repeated cycles of palmitoylation/depalmitoylation could be involved in the regulation of multiple signalling ...
Evgeni Ponimaskin, Nataliya Gorinski
openaire +3 more sources
Journal of Molecular and Cellular Cardiology, 2021
High-throughput experiments suggest that almost 20% of human proteins may be S-palmitoylatable, a post-translational modification (PTM) whereby fatty acyl chains, most commonly palmitoyl chain, are linked to cysteine thiol groups that impact on protein trafficking, distribution and function.
Min Jiang +8 more
openaire +3 more sources
High-throughput experiments suggest that almost 20% of human proteins may be S-palmitoylatable, a post-translational modification (PTM) whereby fatty acyl chains, most commonly palmitoyl chain, are linked to cysteine thiol groups that impact on protein trafficking, distribution and function.
Min Jiang +8 more
openaire +3 more sources
Palmitoylation of proteins in cancer
Biochemical Society Transactions, 2017Post-translational modification of proteins by attachment of palmitate serves as a mechanism to regulate protein localization and function in both normal and malignant cells. Given the essential role that palmitoylation plays in cancer cell signaling, approaches that target palmitoylated proteins and palmitoyl acyltransferases (PATs) have the potential
openaire +3 more sources
The on–off story of protein palmitoylation
Trends in Cell Biology, 2003Palmitoylation is one of the most frequent post-translational modifications found on proteins. It contributes to membrane association, protein sorting and many other processes. Through its reversibility, palmitoylation also provides mechanisms to regulate the functional activities of integral and peripheral membrane proteins.
Bijlmakers, M J, Marsh, M
openaire +3 more sources
Science Signaling
Palmitoylation of intact or cleaved gasdermin D causes plasma membrane pore formation.
openaire +2 more sources
Palmitoylation of intact or cleaved gasdermin D causes plasma membrane pore formation.
openaire +2 more sources