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AAA proteases: cellular machines for degrading membrane proteins
AAA proteases are a conserved class of ATP-dependent proteases that mediate the degradation of membrane proteins in bacteria, mitochon
Diverse functions with a common regulator: Ubiquitin takes command of an AAA ATPase
Cdc48/p97, a member of the AAA (ATPase associated with various cellular activities) ATPase family, participates in various cellular pa
Recognition of misfolded proteins by Lon, a AAA(+) protease.
Proteins unfold constantly in cells, especially under stress conditions. Degradation of denatured polypeptides by Lon and related ATP-
Mitochondrial AAA proteases — Towards a molecular understanding of membrane-bound proteolytic
AbstractMitochondrial AAA proteases play an important role in the maintenance of mitochondrial proteostasis. They regulate and promote
Regulation of OPA1 processing and mitochondrial fusion by m-AAA protease isoenzymes and OMA1.
Mitochondrial fusion depends on the dynamin-like guanosine triphosphatase OPA1, whose activity is controlled by proteolytic cleavage.
Chaperone-like activity of the AAA domain of the yeast Yme1 AAA protease.
The AAA domain, a conserved Walker-type ATPase module, is a feature of members of the AAA family of proteins, which are involved in ma
Structure and function of the bacterial AAA protease FtsH.
Proteolysis of regulatory proteins or key enzymes of biosynthetic pathways is a universal mechanism to rapidly adjust the cellular pro
The i-AAA protease YME1L and OMA1 cleave OPA1 to balance mitochondrial fusion and fission.
Mitochondrial fusion and structure depend on the dynamin-like GTPase OPA1, whose activity is regulated by proteolytic processing. Cons
Evolutionary history and higher order classification of AAA+ ATPases.
The AAA+ ATPases are enzymes containing a P-loop NTPase domain, and function as molecular chaperones, ATPase subunits of proteases, he
TRIP13 is a protein-remodeling AAA+ ATPase that catalyzes MAD2 conformation switching.
The AAA+ family ATPase TRIP13 is a key regulator of meiotic recombination and the spindle assembly checkpoint, acting on signaling pro
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