Results 41 to 50 of about 34,702 (278)

Post-translational palmitoylation of metabolic proteins

open access: yesFrontiers in Physiology, 2023
Numerous cellular proteins are post-translationally modified by addition of a lipid group to their structure, which dynamically influences the proteome by increasing hydrophobicity of proteins often impacting protein conformation, localization, stability,
Kaitlyn M. J. H. Dennis, Lisa C. Heather
doaj   +1 more source

Protein palmitoylation: an emerging regulator of inflammatory signaling and diseases

open access: yesFrontiers in Immunology
Protein palmitoylation is a reversible lipid modification in which palmitoyl esters are covalently attached to cysteine residues of proteins. It controls various cellular physiological processes and alters protein stability, conformation, localization ...
Rong Chen   +6 more
doaj   +1 more source

Palmitoylation-dependent protein sorting [PDF]

open access: yesThe Journal of Cell Biology, 2007
S-palmitoylation is a posttranslational modification that regulates membrane–protein interactions. However, palmitate is more than just a hydrophobic membrane anchor, as many different types of protein are palmitoylated, including transmembrane proteins. Indeed, there is now compelling evidence that palmitoylation plays a key role in regulating various
Greaves, J., Chamberlain, L.H.
openaire   +3 more sources

Understanding the process of envelope glycoprotein incorporation into virions in simian and feline immunodeficiency viruses [PDF]

open access: yes, 2014
The lentiviral envelope glycoproteins (Env) mediate virus entry by interacting with specific receptors present at the cell surface, thereby determining viral tropism and pathogenesis.
Affranchino, Jose Luis   +1 more
core   +4 more sources

Protein palmitoylation and cancer [PDF]

open access: yesEMBO reports, 2018
Protein S-palmitoylation is a reversible post-translational modification that alters the localization, stability, and function of hundreds of proteins in the cell. S-palmitoylation is essential for the function of both oncogenes (e.g., NRAS and EGFR) and tumor suppressors (e.g., SCRIB, melanocortin 1 receptor).
Pin‐Joe Ko, Scott J Dixon
openaire   +2 more sources

Primary fibroblasts from CSPα mutation carriers recapitulate hallmarks of the adult onset neuronal ceroid lipofuscinosis [PDF]

open access: yes, 2017
Mutations in the co- chaperone protein, CSPα, cause an autosomal dominant, adult-neuronal ceroid lipofuscinosis (AD-ANCL). The current understanding of CSPα function exclusively at the synapse fails to explain the autophagy-lysosome pathway (ALP ...
Benitez, Bruno A, Sands, Mark S
core   +2 more sources

S-palmitoylation of MAP kinase is essential for fungal virulence

open access: yesmBio
S-palmitoylation is an important reversible protein post-translational modification in organisms. However, its role in fungi is uncertain. Here, we found the treatment of the rice false fungus Ustilaginoidea virens with S-palmitoylation inhibitor 2 BP ...
Yuhang Duan   +18 more
doaj   +1 more source

PRDX6: A protein bridging S-palmitoylation and diabetic neuropathy

open access: yesFrontiers in Endocrinology, 2022
Diabetic neuropathy is regarded as one of the most debilitating outcomes of diabetes. It can affect both the peripheral and central nervous systems, leading to pain, decreased motility, cognitive decline, and dementia.
Yan Cao   +3 more
doaj   +1 more source

Phosphatidylinositol 4‐kinase as a target of pathogens—friend or foe?

open access: yesFEBS Letters, EarlyView.
This graphical summary illustrates the roles of phosphatidylinositol 4‐kinases (PI4Ks). PI4Ks regulate key cellular processes and can be hijacked by pathogens, such as viruses, bacteria and parasites, to support their intracellular replication. Their dual role as essential host enzymes and pathogen cofactors makes them promising drug targets.
Ana C. Mendes   +3 more
wiley   +1 more source

Hippo pathway at the crossroads of stemness and therapeutic resistance in breast cancer

open access: yesMolecular Oncology, EarlyView.
Dysregulation of the Hippo pathway drives nuclear accumulation of YAP/TAZ, activating stemness‐related transcriptional programs that sustain breast cancer stemness and fuel therapeutic resistance across subtypes, underscoring Hippo signaling as a targetable vulnerability. Figure created and edited with BioRender.com.
Giulia Schiavoni   +11 more
wiley   +1 more source

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