Results 91 to 100 of about 248,730 (279)

Serine protease-driven entry and S2 ' cleavage flexibility of feline coronavirus during feline enterocyte infections.

open access: yesPLoS Pathogens
Coronaviruses not only hijack host cells to serve as viral factories but also exploit host proteolytic systems to activate their spike (S) protein, the key glycoprotein mediating receptor binding and membrane fusion.
Bixia Chen   +5 more
doaj   +1 more source

Virtual Screening of Transmembrane Serine Protease Inhibitors

open access: yesBio-Protocol, 2017
The human family of type II transmembrane serine proteases includes 17 members. The defining features of these proteases are an N-terminal transmembrane domain and a C-terminal serine protease of the chymotrypsin (S1) fold, separated from each other by a
Antti Poso   +2 more
doaj   +1 more source

TMPRSS4, a type II transmembrane serine protease, as a potential therapeutic target in cancer

open access: yesExperimental and Molecular Medicine, 2023
Proteases are involved in almost all biological processes, implying their importance for both health and pathological conditions. Dysregulation of proteases is a key event in cancer.
Semi Kim
doaj   +1 more source

SPHINX31 acts as a SRPK1 inhibitor targeting the ATR/DNA‐PKcs/CHK1 replicative checkpoint to inhibit cell growth in non‐small cell lung cancer

open access: yesMolecular Oncology, EarlyView.
The kinase SRPK1 directly interacts with the protein TOPBP1 and regulates the pre‐mRNA splicing of WIZ thereby contributing to the activation of the ATR/CHK1 replicative checkpoint in response to replicative stress. This allows cancer cells' genomic stability and survival.
Amani Shreim   +17 more
wiley   +1 more source

Importin 7 mediates the nuclear import of HIV‐1 integrase via a specific interacting interface

open access: yesFEBS Open Bio, EarlyView.
HIV‐1 integrase enables viral DNA integration into the host genome. By binding to the core domain of the host protein Importin 7 via its C‐terminal domain, the integrase is transported across the nuclear membrane into the nucleus, where integration of the viral genome into host DNA takes place. This translocation is a critical step for subsequent viral
Juana Bana   +5 more
wiley   +1 more source

Elevated serum matrix metalloprotease (MMP-2) as a candidate biomarker for stable COPD

open access: yesBMC Pulmonary Medicine, 2020
Background The increasing trend of Chronic Obstructive Pulmonary Disease (COPD) in becoming the third leading cause of deaths by 2020 is of great concern, globally as well as in India.
Durga Mahor   +10 more
doaj   +1 more source

Midgut proteases from larval spodoptera littoralis (lepidoptera: noctutoae) [PDF]

open access: yes, 1992
The presence and properties of proteases present in larval midgut extracts from Spodoptera littoralis was investigated. Trypsin and chymotrypsin activities were found mainly in the midgut lumen while leucine aminopeptidase and dipeptidyl aminopeptidase ...
Lee, Michael James, Lee, M.J
core  

Structural studies and functional engineering of NanX: an anhydro‐sialic acid transporter from Escherichia coli

open access: yesFEBS Open Bio, EarlyView.
Biophysical characterisation shows that NanX, a membrane transport protein from the major facilitator superfamily (MFS), forms both monomers and dimers after purification. AlphaFold modelling and substrate docking provide information on residues likely involved in substrate recognition for NanX and another MFS member, NanT.
Michael C. Newton‐Vesty   +13 more
wiley   +1 more source

Purification and functional characterisation of rhinocerase, a novel serine protease from the venom of Bitis gabonica rhinoceros.

open access: yesPLoS ONE, 2010
BackgroundSerine proteases are a major component of viper venoms and are thought to disrupt several distinct elements of the blood coagulation system of envenomed victims.
Sakthivel Vaiyapuri   +4 more
doaj   +1 more source

HtrA serine proteases as potential therapeutic targets in cancer

open access: yes, 2009
The human HtrA family of serine proteases consists of four members: HtrA1, HtrA2, HtrA3 and HtrA4. Although prokaryotic HtrA proteins are well characterized in their dual roles as chaperones and proteases that degrade misfolded proteins in the periplasm,
CHIEN J   +3 more
core   +1 more source

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