Results 51 to 60 of about 415,034 (343)

The role of Serine Proteases and Serine Protease Inhibitors in the migration of Gonadotropin-Releasing Hormone neurons [PDF]

open access: yesBMC Developmental Biology, 2002
Background: Mechanisms regulating neuronal migration during development remain largely undefined. Extracellular matrix cues, target site released factors, and components of the migratory neurons themselves are likely all coordinated in time and space directing neurons to their appropriate locations.
Drapkin, Paola   +2 more
openaire   +4 more sources

Protean proteases: At the cutting edge of lung diseases [PDF]

open access: yes, 2017
Proteases were traditionally viewed as mere protein-degrading enzymes with a very restricted spectrum of substrates. A major expansion in protease research has uncovered a variety of novel substrates, and it is now evident that proteases are critical ...
Borensztajn, Keren S.   +11 more
core   +3 more sources

Functions and evolution of FAM111 serine proteases

open access: yesFrontiers in Molecular Biosciences, 2022
Proteolysis plays fundamental and regulatory roles in diverse cellular processes. The serine protease FAM111A (FAM111 trypsin-like peptidase A) emerged recently as a protease involved in two seemingly distinct processes: DNA replication and antiviral defense. FAM111A localizes to nascent DNA and plays a role at the DNA replication fork.
Allison L. Welter   +2 more
openaire   +3 more sources

Defective Tmprss3-Associated Hair Cell Degeneration in Inner Ear Organoids [PDF]

open access: yes, 2019
Mutations in the gene encoding the type II transmembrane protease 3 (TMPRSS3) cause human hearing loss, although the underlying mechanisms that result in TMPRSS3-related hearing loss are still unclear.
Alex, Alpha L.   +8 more
core   +1 more source

Thermostable neutral metalloprotease from Geobacillus sp. EA1 does not share thermolysin's preference for substrates with leucine at the P1′ position

open access: yesFEBS Letters, EarlyView.
Knowing how proteases recognise preferred substrates facilitates matching proteases to applications. The S1′ pocket of protease EA1 directs cleavage to the N‐terminal side of hydrophobic residues, particularly leucine. The S1′ pocket of thermolysin differs from EA's at only one position (leucine in place of phenylalanine), which decreases cleavage ...
Grant R. Broomfield   +3 more
wiley   +1 more source

Evolutionary analysis of novel serine proteases in the venom gland transcriptome of Bitis gabonica rhinoceros.

open access: yesPLoS ONE, 2011
BackgroundSerine proteases are major components of viper venom and target various stages of the blood coagulation system in victims and prey. A better understanding of the diversity of serine proteases and other enzymes present in snake venom will help ...
Sakthivel Vaiyapuri   +4 more
doaj   +1 more source

Effect of supplemental serine-protease from Bacillus licheniformis on growth performance and physiological change of broiler chickens

open access: yesJournal of Applied Animal Research, 2020
An experimental study was conducted to examine the effects of adding serine-protease from Bacillus licheniformis on performance and physiological parameters of broiler chickens under Egyptian condition.
Ahmed A. Saleh   +5 more
doaj   +1 more source

HtrA2/Omi terminates cytomegalovirus infection and is controlled by the viral mitochondrial inhibitor of apoptosis (vMIA). [PDF]

open access: yesPLoS Pathogens, 2008
Viruses encode suppressors of cell death to block intrinsic and extrinsic host-initiated death pathways that reduce viral yield as well as control the termination of infection.
A Louise McCormick   +2 more
doaj   +1 more source

Protease inhibitors targeting coronavirus and filovirus entry. [PDF]

open access: yes, 2015
In order to gain entry into cells, diverse viruses, including Ebola virus, SARS-coronavirus and the emerging MERS-coronavirus, depend on activation of their envelope glycoproteins by host cell proteases.
Agudelo, Juliet   +10 more
core   +1 more source

Mechanistic basis for inhibition of the extended‐spectrum β‐lactamase GES‐1 by enmetazobactam and tazobactam

open access: yesFEBS Letters, EarlyView.
Antimicrobial resistance (AMR) is of huge importance, resulting in over 1 million deaths each year. Here, we describe how a new drug, enmetazobactam, designed to help fight resistant bacterial diseases, inhibits a key enzyme (GES‐1) responsible for AMR. Our data show it is a more potent inhibitor than the related tazobactam, with high‐level computation
Michael Beer   +10 more
wiley   +1 more source

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