Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Wendy K. Greentree"'
Autor:
Tao Yu, Dan Hou, Jiaqi Zhao, Xuan Lu, Wendy K. Greentree, Qian Zhao, Min Yang, Don-Gerard Conde, Maurine E. Linder, Hening Lin
Publikováno v:
Cell Reports, Vol 43, Iss 4, Pp 114070- (2024)
Summary: Nucleotide oligomerization domain (NOD)-like receptor protein 3 (NLRP3) inflammasome hyperactivation contributes to many human chronic inflammatory diseases, and understanding how NLRP3 inflammasome is regulated can provide strategies to tre
Externí odkaz:
https://doaj.org/article/364166cdf5514bd08b0ded6877667215
Publikováno v:
Frontiers in Physiology, Vol 14 (2023)
Protein S-acylation is a reversible lipid post-translational modification that allows dynamic regulation of processes such as protein stability, membrane association, and localization. Palmitoyltransferase ZDHHC9 (DHHC9) is one of the 23 human DHHC a
Externí odkaz:
https://doaj.org/article/cc98a24d49c9413d8abd6c376be24779
Publikováno v:
Journal of Biological Chemistry. 276:43300-43304
Many signaling proteins are targeted to low density, sphingomyelin- and cholesterol-enriched membranes, also called lipid rafts. These domains organize receptor-mediated signaling events at the plasma membrane. Fatty acylation is one mechanism for ta
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f062cbafe3395a00cc3f7ffab8c407b9
https://doi.org/10.1074/jbc.m104275200
https://doi.org/10.1074/jbc.m104275200
Publikováno v:
Journal of Biological Chemistry. 271:7154-7159
Heterotrimeric G proteins are covalently modified by lipids. Myristoylation of G-protein alpha subunits and prenylation of gamma subunits are stable modifications. In contrast, palmitoylation of alpha subunits is dynamic and thus has the potential fo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::21ee996a8770976664b9c873f54fa091
https://doi.org/10.1074/jbc.271.12.7154
https://doi.org/10.1074/jbc.271.12.7154
Autor:
Maurine E. Linder, Wendy K. Greentree
The purification of recombinant G protein a subunits expressed in Escherichia coli (E. coli) is a convenient and inexpensive method to obtain homogeneous preparations of protein for biochemical and biophysical analyses. Wild-type and mutant forms of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d7af422e029c037b1820b959cc53d5c5
https://doi.org/10.1385/1-59259-430-1:3
https://doi.org/10.1385/1-59259-430-1:3
Autor:
Wendy K, Greentree, Maurine E, Linder
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 237
The purification of recombinant G protein a subunits expressed in Escherichia coli (E. coli) is a convenient and inexpensive method to obtain homogeneous preparations of protein for biochemical and biophysical analyses. Wild-type and mutant forms of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::81e288667d05fee9eb5b4dc2ad51f4e4
https://pubmed.ncbi.nlm.nih.gov/14501035
https://pubmed.ncbi.nlm.nih.gov/14501035
Autor:
John R. Silvius, Jens K. Knudsen, Wendy K. Greentree, Julianne T. Dunphy, Maurine E. Linder, Rania Leventis, Hans Schroeder
Publikováno v:
Biochimica et biophysica acta. 1485(2-3)
Both enzymatic and autocatalytic mechanisms have been proposed to account for protein thioacylation (commonly known as palmitoylation). Acyl-CoA binding proteins (ACBP) strongly suppress non-enzymatic thioacylation of cysteinyl-containing peptides by
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ffdd26d028aec66b79eed553e99198b7
https://pubmed.ncbi.nlm.nih.gov/10832099
https://pubmed.ncbi.nlm.nih.gov/10832099
Publikováno v:
The Journal of biological chemistry. 274(30)
SNAP-25, syntaxin, and synaptobrevin are SNARE proteins that mediate fusion of synaptic vesicles with the plasma membrane. Membrane attachment of syntaxin and synaptobrevin is achieved through a C-terminal hydrophobic tail, whereas SNAP-25 associatio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f09e9cbaad72a88664372a7dacf4d7cd
https://pubmed.ncbi.nlm.nih.gov/10409690
https://pubmed.ncbi.nlm.nih.gov/10409690