Chemical rescue of I-site cleavage in living cells and in vitro discriminates between the cytomegalovirus protease, assemblin, and its precursor, pUL80a.
about
Structural insights into catalytic and substrate binding mechanisms of the strategic EndA nuclease from Streptococcus pneumoniaeMechanism of tRNA-dependent editing in translational quality controlEnzymatic activities of human cytomegalovirus maturational protease assemblin and its precursor (pPR, pUL80a) are comparable: [corrected] maximal activity of pPR requires self-interaction through its scaffolding domain.Cytomegalovirus capsid protease: biological substrates are cleaved more efficiently by full-length enzyme (pUL80a) than by the catalytic domain (assemblin)
P2860
Chemical rescue of I-site cleavage in living cells and in vitro discriminates between the cytomegalovirus protease, assemblin, and its precursor, pUL80a.
description
2005 nî lūn-bûn
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2005年の論文
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2005年論文
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2005年論文
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2005年論文
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2005年論文
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2005年論文
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2005年论文
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2005年论文
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2005年论文
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name
Chemical rescue of I-site clea ...... in, and its precursor, pUL80a.
@en
type
label
Chemical rescue of I-site clea ...... in, and its precursor, pUL80a.
@en
prefLabel
Chemical rescue of I-site clea ...... in, and its precursor, pUL80a.
@en
P2093
P2860
P356
P1476
Chemical rescue of I-site clea ...... in, and its precursor, pUL80a.
@en
P2093
Amy N Loveland
Edward J Brignole
Keli N Kolegraff
LaShon M Ussin
Stephen A McCartney
Wade Gibson
P2860
P304
33206-33212
P356
10.1074/JBC.M506876200
P407
P577
2005-07-21T00:00:00Z