The roles of monomeric GTP-binding proteins in macroautophagy in Saccharomyces cerevisiae. [PDF]
Autophagy is a cellular degradation process that sequesters components into a double-membrane structure called the autophagosome, which then fuses with the lysosome or vacuole for hydrolysis and recycling of building blocks. Bulk phase autophagy, also known as macroautophagy, controlled by specific Atg proteins, can be triggered by a variety of ...
Yang S, Rosenwald AG.
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Autophagy in Saccharomyces cerevisiae requires the monomeric GTP-binding proteins, Arl1 and Ypt6. [PDF]
Macroautophagy/autophagy is a cellular degradation process that sequesters organelles or proteins into a double-membrane structure called the phagophore; this transient compartment matures into an autophagosome, which then fuses with the lysosome or vacuole to allow hydrolysis of the cargo.
Yang S, Rosenwald AG.
europepmc +4 more sources
Recent discoveries suggest links between abnormalities in cell morphogenesis in the brain and the functional deficiency of molecules controlling signal transduction in glial cells such as oligodendroglia.
Shoya Fukatsu +8 more
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A specific role for importin-5 and NASP in the import and nuclear hand-off of monomeric H3
Core histones package chromosomal DNA and regulate genomic transactions, with their nuclear import and deposition involving importin-β proteins and a dedicated repertoire of histone chaperones. Previously, a histone H3-H4 dimer has been isolated bound to
Alonso Javier Pardal +1 more
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Structure of UreG/UreF/UreH complex reveals how urease accessory proteins facilitate maturation of Helicobacter pylori urease. [PDF]
Urease is a metalloenzyme essential for the survival of Helicobacter pylori in acidic gastric environment. Maturation of urease involves carbamylation of Lys219 and insertion of two nickel ions at its active site. This process requires GTP hydrolysis and
Yu Hang Fong +5 more
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Ethylene Regulates Monomeric GTP-Binding Protein Gene Expression and Activity in Arabidopsis [PDF]
AbstractEthylene rapidly and transiently up-regulates the activity of several monomeric GTP-binding proteins (monomeric G proteins) in leaves of Arabidopsis as determined by two-dimensional gel electrophoresis and autoradiographic analyses. The activation is suppressed by the receptor-directed inhibitor 1-methylcyclopropene.
Igor E, Moshkov +4 more
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Potassium acts as a GTPase-activating element on each nucleotide-binding domain of the essential Bacillus subtilis EngA. [PDF]
EngA proteins form a unique family of bacterial GTPases with two GTP-binding domains in tandem, namely GD1 and GD2, followed by a KH (K-homology) domain.
Anne-Emmanuelle Foucher +4 more
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Biochemical characterization of highly purified leucine-rich repeat kinases 1 and 2 demonstrates formation of homodimers. [PDF]
Leucine-rich repeat kinase 1 and 2 (LRRK1 and LRRK2) are large multidomain proteins containing kinase, GTPase and multiple protein-protein interaction domains, but only mutations in LRRK2 are linked to familial Parkinson's disease (PD).
Laura Civiero +13 more
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The nucleotide exchange factor Ric-8A is a chaperone for the conformationally dynamic nucleotide-free state of Gαi1. [PDF]
Heterotrimeric G protein α subunits are activated upon exchange of GDP for GTP at the nucleotide binding site of Gα, catalyzed by guanine nucleotide exchange factors (GEFs). In addition to transmembrane G protein-coupled receptors (GPCRs), which act on G
Celestine J Thomas +7 more
doaj +1 more source
Study of the Interaction of the Myelin Monomeric GTP‐Binding Proteins with Other Brain Proteins [PDF]
Abstract: Although several monomeric GTP‐binding proteins have been found in myelin, the signaling pathways in which they operate are not known. To define these signaling pathways we searched for specific target proteins that interact with the myelin monomeric GTP‐binding proteins. A blot overlay approach was used.
A G, Rodriguez-Gabin +3 more
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