Results 61 to 70 of about 902,862 (301)

Respiratory syncytial virus (RSV) entry is inhibited by serine protease inhibitor AEBSF when present during an early stage of infection

Virology Journal, 2017
Background Host proteases have been shown to play important roles in many viral activities such as entry, uncoating, viral protein production and disease induction.
Winke Van der Gucht, Annelies Leemans, Marjorie De Schryver, Annick Heykers, Guy Caljon, Louis Maes, Paul Cos, Peter L. Delputte   +7 more
doaj   +1 more source

How conformational changes can affect catalysis, inhibition and drug resistance of enzymes with induced-fit binding mechanism such as the HIV-1 protease

, 2013
A central question is how the conformational changes of proteins affect their function and the inhibition of this function by drug molecules. Many enzymes change from an open to a closed conformation upon binding of substrate or inhibitor molecules ...
Hemmateenejad, Bahram, Weikl, Thomas R.
core   +1 more source

Hyperosmotic stress induces PARP1‐mediated HPF1‐dependent mono(ADP‐ribosyl)ation

FEBS Letters, EarlyView.
Sorbitol‐induced hyperosmotic stress rapidly induces reversible mono(ADP‐ribosyl)ation (MARylation) on PARP1 without the signs of genotoxic signaling. We show that PARP1 autoMARylation is HPF1 dependent and forms hydroxylamine‐resistant O‐glycosidic linkages.
Anna Georgina Kopasz, Mihály Mérey, Rebeka Vásárhelyi, Ramóna Pék, Victor Imburchia, László Henn, Adrián Kószó, Nicholas D. Lakin, Ivan Ahel, Sébastien Huet, Ágnes Czibula, Gyula Timinszky   +11 more
wiley   +1 more source

Three cryo-EM structures of CD109 reveal its mechanism of protease inhibition

Cell Reports
Summary: CD109 is a glycosylphosphatidylinositol-anchored protein. In addition to regulating transforming growth factor β (TGF-β) network signaling, CD109 is also a protease inhibitor. Protease cleavage of its bait region triggers a conformational change
Ana V. Almeida, Kathrine T. Jensen, Seandean L. Harwood, Martin H. Jørgensen, Nadia S. Nielsen, Ida B. Thøgersen, Jan J. Enghild, Gregers R. Andersen   +7 more
doaj   +1 more source

An isoform of 14‐3‐3 protein regulates transbilayer lipid movement at the plasma membrane

FEBS Letters, EarlyView.
Loss of 14‐3‐3ζ in CHO cells confers resistance to exogenous phosphatidylserine (PS) and impairs endocytosis‐independent inward flip‐flop of fluorescent PS at the plasma membrane. RNAi‐mediated knockdown reproduces this defect, while no additive effect is seen in ATP11C‐deficient cells.
Akiko Yamaji‐Hasegawa, Akira Hattori, Masafumi Tsujimoto, Toshihide Kobayashi   +3 more
wiley   +1 more source

Preliminary Characterization of Protease Inhibitor from Bacteria Associated with Sponge from Panggang Island, Seribu Islands

Hayati Journal of Biosciences, 2006
Pathogenic bacteria produced protease that involved in molecular mechanism of foodborne disease. Produced protease involved in molecular mechanisms of foodborne diseases. The purpose of this research was to screen, identify and characterize the potential
TATI NURHAYATI, MAGGY THENAWIDJAJA SUHARTONO, LILIS NURAIDA, SRI BUDIARTI POERWANTO   +3 more
doaj  

AAA+ protein unfoldases—the Moirai of the proteome

FEBS Letters, EarlyView.
AAA+ unfoldases are essential molecular motors that power protein degradation and disaggregation. This review integrates recent cryo‐electron microscopy (cryo‐EM) structures and single‐molecule biophysical data to reconcile competing models of substrate translocation.
Stavros Azinas, Marta Carroni
wiley   +1 more source

Diversity of cultivable protease-producing bacteria in sediments of Jiaozhou Bay, China

Frontiers in Microbiology, 2015
Although protease-producing bacteria are key players in the degradation of organic nitrogen and essential for the nitrogen recycling in marine sediments, diversity of both these bacteria and their extracellular proteases is still largely unknown.
Xi-Ying eZhang, Xiao-Xu eHan, Xiu-Lan eChen, Hong-Yue eDang, Bin-Bin eXie, Qi-Long eQin, Mei eShi, Bai-Cheng eZhou, Yu-Zhong eZhang   +8 more
doaj   +1 more source

Non-active site mutants of HIV-1 protease influence resistance and sensitisation towards protease inhibitors

Retrovirology, 2020
Background HIV-1 can develop resistance to antiretroviral drugs, mainly through mutations within the target regions of the drugs. In HIV-1 protease, a majority of resistance-associated mutations that develop in response to therapy with protease ...
Tomas Bastys, Vytautas Gapsys, Hauke Walter, Eva Heger, Nadezhda T. Doncheva, Rolf Kaiser, Bert L. de Groot, Olga V. Kalinina   +7 more
doaj   +1 more source

pH‐mediated activation of the lysosomal arginine sensor SLC38A9

FEBS Letters, EarlyView.
Cells monitor nutrient levels via the lysosomal transporter SLC38A9 to activate the mechanistic target of rapamycin complex 1 (mTORC1). This study reveals that SLC38A9 function is regulated by pH. We identified histidine 544 as a critical pH sensor that undergoes conformational changes to control amino acid efflux from lysosomes; therefore, it ...
Xuelang Mu, Ampon Sae Her, Tamir Gonen
wiley   +1 more source