Results 61 to 70 of about 711,796 (313)
Autoacylation of G Protein α Subunits [PDF]
Journal of Biological Chemistry, 1996 The palmitoylation or S-acylation of at least some G protein alpha subunits is a dynamic process that is regulated in vivo by the activation of associated receptors. Highly purified, myristoylated Gialpha1 and other G protein alpha subunits react spontaneously with palmitoyl-CoA in vitro to form thioesterified proteins.
J A, Duncan, A G, Gilman
openaire +2 more sources
FEBS Letters, EarlyView.The Ile181Asn variant of human UDP‐xylose synthase (hUXS1), associated with a short‐stature genetic syndrome, has previously been reported as inactive. Our findings demonstrate that Ile181Asn‐hUXS1 retains catalytic activity similar to the wild‐type but exhibits reduced stability, a looser oligomeric state, and an increased tendency to precipitate ...
Tuo Li +2 more
wiley +1 more source
Purification and characterization of a calmodulin-dependent protein kinase that is highly concentrated in brain [PDF]
, 1983 A calcium and calmodulin-dependent protein kinase has been purified from rat brain. It was monitored during the purification by its ability to phosphorylate the synaptic vesicle-associated protein, synapsin I.
Bennett, Mark K. +2 more
core
An update on transcriptional and post-translational regulation of brain voltage-gated sodium channels [PDF]
, 2015 Voltage-gated sodium channels are essential proteins in brain physiology, as they generate the sodium currents that initiate neuronal action potentials.
Beltran-Alvarez, Pedro +1 more
core +1 more source
Structural biology of ferritin nanocages
FEBS Letters, EarlyView.Ferritin is a conserved iron‐storage protein that sequesters iron as a ferric mineral core within a nanocage, protecting cells from oxidative damage and maintaining iron homeostasis. This review discusses ferritin biology, structure, and function, and highlights recent cryo‐EM studies revealing mechanisms of ferritinophagy, cellular iron uptake, and ...
Eloise Mastrangelo, Flavio Di Pisa
wiley +1 more source
Frontiers in Genetics, 2020 Chaperonin containing tailless complex polypeptide 1 (CCT) or tailless complex polypeptide 1 ring complex (TRiC) is an essential eukaryotic molecular chaperone. It is a multi-subunit oligomer of two rings of eight individual protein subunits.
Julie Grantham
doaj +1 more source
Understanding protein-complex assembly through grand canonical maximum entropy modeling
Physical Review Research, 2021 Inside a cell, heterotypic proteins assemble in inhomogeneous, crowded systems where the abundance of these proteins vary with cell types. While some protein complexes form putative structures that can be visualized with imaging, there are far more ...
Andrei G. Gasic +2 more
doaj +1 more source
Architecture of coatomer: Molecular characterization of delta-COP and protein interactions within the complex [PDF]
, 1996 Copyright © 2011 by The Rockefeller University Press.Coatomer is a cytosolic protein complex that forms the coat of COP I-coated transport vesicles.
Auerbach, S +9 more
core +1 more source
FEBS Letters, EarlyView.In this study, we found that human cervical‐derived adipocytes maintain intracellular iron level by regulating the expression of iron transport‐related proteins during adrenergic stimulation. Melanotransferrin is predicted to interact with transferrin receptor 1 based on in silico analysis.
Rahaf Alrifai +9 more
wiley +1 more source
BMC Cell Biology, 2009 Background The Arabidopsis ortholog of the 30 kD subunit of the mammalian Cleavage and Polyadenylation Specificity Factor (AtCPSF30) is an RNA-binding endonuclease that is associated with other Arabidopsis CPSF subunits (orthologs of the 160, 100, and 73
Dinkins Randy D +2 more
doaj +1 more source