Results 61 to 70 of about 1,452,849 (304)

Structures of mycobacterial 3‐methylcrotonyl‐CoA carboxylase reveal carrier‐domain translocation between catalytic sites

FEBS Letters, EarlyView.
Mycobacterial 3‐methylcrotonyl‐CoA carboxylase uses a mobile biotin‐carrying domain to shuttle a carboxyl group between two catalytic sites, enabling carboxylation of 3‐methylcrotonyl‐CoA during leucine breakdown. Cryo‐electron microscopy captures the carrier at both sites and reveals an inward loop movement that may prevent futile rebinding to the ...
Ajit Yadav, Bogdan I. Florea, Sebastian Geibel   +2 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

Assay for Protealysin-like Protease Inhibitor Activity

Bio-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, Maria Karaseva, Ilya Demidyuk   +2 more
doaj   +1 more source

The Shewanella oneidensis Fic enzyme SoFic targets the switch‐I region of EF‐Tu for AMPylation

FEBS Letters, EarlyView.
Fic enzymes mediate diverse post‐translational modifications across all domains of life, including AMPylation. Prokaryotic EF‐Tu can be AMPylated and deAMPylated by the conserved Fic enzyme SoFic. Structural and biochemical approaches were used to characterize the effect of AMPylation on EF‐Tu, SoFic's enzymatic activities, and the enzyme‐target ...
Svenja Runge, Vivian Pogenberg, Alexander Baumgart, Bente Siebels, Hartmut Schlüter, Michael Hecht‐Bucher, Aymelt Itzen   +6 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  

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

L‐aspartate oxidase provides new insights into fumarate reduction in anaerobic darkness in Synechocystis sp. PCC6803

FEBS Letters, EarlyView.
Synechocystis strains deficient in succinate dehydrogenase (SDH) secrete more succinate than the WT under dark anaerobic conditions, supporting that SDH then primarily acts as SDH, not as a fumarate reductase. L‐aspartate oxidase (Laspo) from Synechocystis is functional under anaerobic conditions, reducing fumarate to succinate.
Kateryna Kukil, Jeffrey A. Hawkes, Cecilia Blikstad, Pia Lindberg   +3 more
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

A context‐dependent modulatory role for eIF6 in acquired resistance to vemurafenib in melanoma

FEBS Letters, EarlyView.
Acquired resistance to vemurafenib upregulates the translation factor eIF6 in melanoma cells. Silencing eIF6 in resistant cells reduces proliferation and partially restores drug sensitivity, whereas its overexpression increases sensitivity across melanoma lines regardless of BRAF status, via modulation of mTOR, S6K, and MAPK signaling.
George Kyriakopoulos, Antonia Petropoulou, Alexandra Anastogianni, Angelina Bania, Vassilis Stamatakis, Argyris Alexiou, Chi‐Ping Day, Glenn Merlino, Katerina Grafanaki, Constantinos Stathopoulos   +9 more
wiley   +1 more source

Inhibitors of rhomboid proteases [PDF]

Biochimie, 2016
Rhomboid proteases form one of the most widespread families of intramembrane proteases. They utilize a catalytic serine-histidine dyad located several Å below the surface of the membrane for substrate hydrolysis. Multiple studies have implicated rhomboid proteases in biologically and medically relevant processes. Several assays have been developed that
Wolf, Eliane V., Verhelst, Steven
openaire   +3 more sources