A potent HIV protease inhibitor, darunavir, does not inhibit ZMPSTE24 or lead to an accumulation of farnesyl-prelamin A in cells.
about
Dynamics of lamin-A processing following precursor accumulation.The posttranslational processing of prelamin A and disease.Functional characterization of the atypical integral membrane lipid phosphatase PDP1/PPAPDC2 identifies a pathway for interconversion of isoprenols and isoprenoid phosphates in mammalian cells.AIM2 inflammasome is activated by pharmacological disruption of nuclear envelope integrityHIV protease inhibitors block streptolysin S productionAbsence of progeria-like disease phenotypes in knock-in mice expressing a non-farnesylated version of progerin.HIV protease inhibitors do not cause the accumulation of prelamin A in PBMCs from patients receiving first line therapy: the ANRS EP45 "aging" studyHIV-associated lipodystrophy: impact of antiretroviral therapy.Inhibitors of protein geranylgeranyltransferase-I lead to prelamin A accumulation in cells by inhibiting ZMPSTE24Biogenesis of the Saccharomyces cerevisiae pheromone a-factor, from yeast mating to human disease.Progerin elicits disease phenotypes of progeria in mice whether or not it is farnesylated.HIV-protease inhibitors block the enzymatic activity of purified Ste24p.Increasing the length of progerin's isoprenyl anchor does not worsen bone disease or survival in mice with Hutchinson-Gilford progeria syndrome.Mass spectrometry captures off-target drug binding and provides mechanistic insights into the human metalloprotease ZMPSTE24.ZMPSTE24, an integral membrane zinc metalloprotease with a connection to progeroid disorders.Neural induction and early patterning in vertebrates.The induction of a nucleoplasmic reticulum by prelamin A accumulation requires CTP:phosphocholine cytidylyltransferase-α.Formation of a nucleoplasmic reticulum requires de novo assembly of nascent phospholipids and shows preferential incorporation of nascent lamins.Protein farnesyltransferase-catalyzed isoprenoid transfer to peptide depends on lipid size and shape, not hydrophobicity.LMNA missense mutations causing familial partial lipodystrophy do not lead to an accumulation of prelamin A.Different prelamin A forms accumulate in human fibroblasts: a study in experimental models and progeria.a-Factor Analogues Containing Alkyne- and Azide-Functionalized Isoprenoids Are Efficiently Enzymatically Processed and Retain Wild-Type Bioactivity.Human CaaX protease ZMPSTE24 expressed in yeast: Structure and inhibition by HIV protease inhibitors.MicroRNAs in hereditary and sporadic premature aging syndromes and other laminopathies.
P2860
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P2860
A potent HIV protease inhibitor, darunavir, does not inhibit ZMPSTE24 or lead to an accumulation of farnesyl-prelamin A in cells.
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
2008年论文
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name
A potent HIV protease inhibito ...... farnesyl-prelamin A in cells.
@ast
A potent HIV protease inhibito ...... farnesyl-prelamin A in cells.
@en
type
label
A potent HIV protease inhibito ...... farnesyl-prelamin A in cells.
@ast
A potent HIV protease inhibito ...... farnesyl-prelamin A in cells.
@en
prefLabel
A potent HIV protease inhibito ...... farnesyl-prelamin A in cells.
@ast
A potent HIV protease inhibito ...... farnesyl-prelamin A in cells.
@en
P2093
P2860
P356
P1476
A potent HIV protease inhibito ...... farnesyl-prelamin A in cells.
@en
P2093
Catherine Coffinier
Chika Nobumori
Christine A Hrycyna
Douglas A Andres
Emily A Farber
H Peter Spielmann
Jeffrey H Miner
Loren G Fong
Sarah E Hudon
P2860
P304
P356
10.1074/JBC.M709629200
P407
P577
2008-01-28T00:00:00Z