Results 41 to 50 of about 638,874 (218)

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

open access: yesFEBS 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   +11 more
wiley   +1 more source

PEMURNIAN DAN KARAKTERISASI INHIBITOR PROTEASE DARI Chromohalobacter sp. 6A3, BAKTERI YANG BERASOSIASI DENGAN SPONS Xetospongia testudinaria [Purification and Characterization of Protease Inhibitor from Chromohalobacter sp. 6A3, Bacteria-associated with Sponge Xetospongia testudinaria]

open access: yesJurnal Teknologi dan Industri Pangan, 2010
Various sponges has been reported to produce protease inhibitor which could inhibit protease activity of pathogenic bacteria. The previous research showed that bacteria-associated with sponge could produce bioactive compound similar to their host ...
Tati Nurhayati1)*   +3 more
doaj  

Reverse Zymmogram Analysis for the Detection of Protease Inhibitor Activity

open access: yesBio-Protocol, 2013
This protocol describes a gel-based procedure to detect protease inhibitor activity. In this method gelatin is used as a substrate for proteolysis and is copolymerized within the polyacrylamide matrix. Protein extracts are fractioned by SDS-PAGE and then
Lilia Bernal   +3 more
doaj   +1 more source

Assay for Protealysin-like Protease Inhibitor Activity

open access: yesBio-Protocol, 2022
Here, we present the first quantitative method for the activity analysis of protealysin-like protease (PLP) inhibitors. This approach is based on a previously developed method for protealysin activity determination by hydrolysis of internally quenched ...
Igor Berdyshev   +2 more
doaj   +1 more source

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

open access: yesFEBS 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   +3 more
wiley   +1 more source

Potent, multi-target serine protease inhibition achieved by a simplified β-sheet motif.

open access: yesPLoS ONE, 2019
Engagement of an extended β-sheet is a common substrate/inhibitor interaction at the active site of serine proteases and is an important feature of Laskowski mechanism inhibitors that present a substrate-like loop to a target protease.
Xingchen Chen   +10 more
doaj   +1 more source

Matriptase Complexes and Prostasin Complexes with HAI-1 and HAI-2 in Human Milk: Significant Proteolysis in Lactation.

open access: yesPLoS ONE, 2016
Significant proteolysis may occur during milk synthesis and secretion, as evidenced by the presence of protease-protease inhibitor complex containing the activated form of the type 2 transmembrane serine protease matriptase and the transmembrane Kunitz ...
Chih-Hsin Lai   +7 more
doaj   +1 more source

pH‐mediated activation of the lysosomal arginine sensor SLC38A9

open access: yesFEBS 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

Septin 9 PB domains coordinate centrosome positioning and microtubule acetylation to control epithelial polarity

open access: yesFEBS Letters, EarlyView.
Septin 9 polybasic domains couple phosphoinositide‐rich membrane binding to centrosome positioning, Golgi organization, and microtubule acetylation to control epithelial polarity. Their loss disrupts this axis, causing centrosome mispositioning, Golgi fragmentation, reduced microtubule acetylation, and polarity inversion via upregulation of the ...
Ting ting Cai   +4 more
wiley   +1 more source

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

open access: yesCell 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   +7 more
doaj   +1 more source

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