HIV-protease inhibitors block the enzymatic activity of purified Ste24p.
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Human ZMPSTE24 disease mutations: residual proteolytic activity correlates with disease severityStructure of the integral membrane protein CAAX protease Ste24p.Dynamics of lamin-A processing following precursor accumulation.Leptin revisited: its mechanism of action and potential for treating diabetes.The posttranslational processing of prelamin A and disease.Requirements for efficient proteolytic cleavage of prelamin A by ZMPSTE24.HIV protease inhibitors do not cause the accumulation of prelamin A in PBMCs from patients receiving first line therapy: the ANRS EP45 "aging" studyLipodystrophy syndromesLMNA mutations induce a non-inflammatory fibrosis and a brown fat-like dystrophy of enlarged cervical adipose tissue.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.The HIV-1 protease inhibitor nelfinavir activates PP2 and inhibits MAPK signaling in macrophages: a pathway to reduce inflammation.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.Exploring the pathophysiology behind the more common genetic and acquired lipodystrophies.The induction of a nucleoplasmic reticulum by prelamin A accumulation requires CTP:phosphocholine cytidylyltransferase-α.Cross-sectional comparison of the prevalence of age-associated comorbidities and their risk factors between HIV-infected and uninfected individuals: the AGEhIV cohort study.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.Lamin A/C deficiency is an independent risk factor for cervical cancer.
P2860
Q24611268-B17651CE-8DDC-4F9B-A8D0-469AE17104C6Q27677111-8E79DB54-C529-4C24-9D14-3EEB2675DEE7Q33595869-DAB85F4B-CA53-4704-931C-D59BD03868F7Q33602487-E25538A3-FEA0-405D-977E-CACA1F23BAFBQ33758494-9C00D528-26AC-4C7A-9004-D5868AEE5D95Q34166555-720B6033-D081-4037-B635-2849F1DC5744Q34534986-1675305D-C804-4933-9DD9-704C1183C544Q34597209-F7E4D066-4B8F-4F5D-A40E-A58E042BFC10Q35474290-797C3111-7C23-4A3F-B500-295296FB2F0CQ35958478-58B78E84-6884-4F76-A824-0E50E5CDA355Q36194945-A6E36EDB-797B-4C4F-8949-5CDF2C2F2422Q36232217-6FF3D0A6-0F62-4C43-BB47-70D562BB37CAQ37441222-5918180A-AF6A-48BC-96D2-4BE873D9ECFBQ37488230-E56C4580-086C-4E24-88EA-6E5C46C5C0BAQ38155007-634E1DC6-1FBC-4BBE-8D79-19F533D0AF85Q40394191-DE0C506C-F9EA-418A-A492-049D68CB2A79Q41757466-64C96E71-6809-47BB-B591-53277BE59D8CQ47348414-FFC68F37-F611-4C95-8111-0A2BC43E2D60Q50326629-2D9D335C-E7FE-4C3F-AFC5-23D2AF8BFAF5Q53784074-BF8DBDD5-5EBA-441F-A2EC-4B4B12FAECCF
P2860
HIV-protease inhibitors block the enzymatic activity of purified Ste24p.
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
@zh
2008年论文
@zh-cn
name
HIV-protease inhibitors block the enzymatic activity of purified Ste24p.
@en
type
label
HIV-protease inhibitors block the enzymatic activity of purified Ste24p.
@en
prefLabel
HIV-protease inhibitors block the enzymatic activity of purified Ste24p.
@en
P2093
P2860
P1476
HIV-protease inhibitors block the enzymatic activity of purified Ste24p
@en
P2093
Catherine Coffinier
Christine A Hrycyna
Loren G Fong
Sarah E Hudon
Susan Michaelis
P2860
P304
P356
10.1016/J.BBRC.2008.07.033
P407
P577
2008-07-17T00:00:00Z