Results 11 to 20 of about 1,283,777 (223)

20S and 26S proteasome-binding proteins of the rabbit brain: A proteomic dataset

open access: yesData in Brief, 2021
Fractions of 26S and 20S proteasomes isolated from the rabbit brain by the method of salt fractionation (salt-induced precipitation) contain intrinsic proteasome proteins responsible for assembly of the core particle and regulatory particle of proteasome
Olga Buneeva   +4 more
doaj   +1 more source

Identification of nucleotide-binding sites in protein structures: a novel approach based on nucleotide modularity. [PDF]

open access: yesPLoS ONE, 2012
Nucleotides are involved in several cellular processes, ranging from the transmission of genetic information, to energy transfer and storage. Both sequence and structure based methods have been developed to predict the location of nucleotide-binding ...
Luca Parca   +6 more
doaj   +1 more source

The energetics of phosphate binding to a protein complex [PDF]

open access: yesProtein Science, 2000
AbstractThe heat of binding the serine protease, porcine pancreatic elastase, by the inhibitor, turkey ovomucoid third domain, is dependent on the presence of inorganic phosphate. This dependence is saturable and can be accurately modeled as the phosphate binding to a single site on the protease‐inhibitor complex; thus, the elastase‐ovomucoid system ...
S P, Edgcomb, B M, Baker, K P, Murphy
openaire   +2 more sources

Phosphate-binding Tag, a New Tool to Visualize Phosphorylated Proteins [PDF]

open access: yesMolecular & Cellular Proteomics, 2006
We introduce two methods for the visualization of phosphorylated proteins using alkoxide-bridged dinuclear metal (i.e. Zn(2+) or Mn(2+)) complexes as novel phosphate-binding tag (Phos-tag) molecules. Both Zn(2+)- and Mn(2+)-Phos-tag molecules preferentially capture phosphomonoester dianions bound to Ser, Thr, and Tyr residues. One method is based on an
Kinoshita, Eiji   +3 more
openaire   +4 more sources

Mechanism of phosphate sensing and signaling revealed by rice SPX1-PHR2 complex structure

open access: yesNature Communications, 2021
SPX proteins sense phosphate levels in plant cells by binding to inositol polyphosphates (InsP) and suppressing the activity of PHR transcription factors. Here the authors show that when bound to InsP6, the rice SPX1 protein inhibits the activity of PHR2
Jia Zhou   +13 more
doaj   +1 more source

The phosphatidylinositol 3-phosphate-binding protein SNX4 controls ATG9A recycling and autophagy [PDF]

open access: yesJournal of Cell Science, 2020
ABSTRACT Late endosomes and lysosomes (endolysosomes) receive proteins and cargo from the secretory, endocytic and autophagic pathways. Although these pathways and the degradative processes of endolysosomes are well characterized, less is understood about protein traffic from these organelles.
Anthony Ravussin   +3 more
openaire   +5 more sources

Structural comparison of unconventional G protein YchF with heterotrimeric G protein and small G protein

open access: yesPlant Signaling & Behavior, 2022
Guanine nucleotide-binding (G) proteins, namely, phosphate-binding (P) loop GTPases, play a critical role in life processes among different species. Based on the structural characteristics, G proteins can be divided into heterotrimeric G proteins, small ...
Maozhen Luo   +7 more
doaj   +1 more source

Molecular mechanism of Gαi activation by non-GPCR proteins with a Gα-Binding and Activating motif [PDF]

open access: yes, 2017
Heterotrimeric G proteins are quintessential signalling switches activated by nucleotide exchange on Gα. Although activation is predominantly carried out by G-protein-coupled receptors (GPCRs), non-receptor guanine-nucleotide exchange factors (GEFs) have
Baillie, George S.   +14 more
core   +1 more source

Distinction between 2′- and 3′-Phosphate Isomers of a Fluorescent NADPH Analogue Led to Strong Inhibition of Cancer Cells Migration

open access: yesAntioxidants, 2021
Specific inhibition of NADPH oxidases (NOX) and NO-synthases (NOS), two enzymes associated with redox stress in tumor cells, has aroused great pharmacological interest.
Raoul Manuel   +18 more
doaj   +1 more source

Contribution of protein phosphorylation to binding-induced folding of the SLBP–histone mRNA complex probed by phosphorus-31 NMR

open access: yesFEBS Open Bio, 2014
Phosphorus-31 (31P) NMR can be used to characterize the structure and dynamics of phosphorylated proteins. Here, I use 31P NMR to report on the chemical nature of a phosphothreonine that lies in the RNA binding domain of SLBP (stem-loop binding protein).
Roopa Thapar
doaj   +1 more source

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