Results 51 to 60 of about 695,446 (323)

A Cre‐dependent lentiviral vector for neuron subtype‐specific expression of large proteins

open access: yesFEBS Letters, EarlyView.
We designed a versatile and modular lentivector comprising a Cre‐dependent switch and self‐cleaving 2A peptide and tested it for co‐expression of GFP and a 2.8 kb gene of interest (GOI) in mouse cortical parvalbumin (PV+) interneurons and midbrain dopamine (TH+) neurons.
Weixuan Xue   +6 more
wiley   +1 more source

C-Terminal Extended Hexapeptides as Potent Inhibitors of the NS2B-NS3 Protease of the ZIKA Virus

open access: yesFrontiers in Medicine, 2022
The Zika virus (ZIKV) protease is an attractive drug target for the design of novel inhibitors to control the ZIKV infection. As the protease substrate-binding site contains acidic residues, inhibitors with basic residues can be beneficial for the ...
Suyash Pant, Nihar R. Jena
doaj   +1 more source

By dawn or dusk—how circadian timing rewrites bacterial infection outcomes

open access: yesFEBS Letters, EarlyView.
The circadian clock shapes immune function, yet its influence on infection outcomes is only beginning to be understood. This review highlights how circadian timing alters host responses to the bacterial pathogens Salmonella enterica, Listeria monocytogenes, and Streptococcus pneumoniae revealing that the effectiveness of immune defense depends not only
Devons Mo   +2 more
wiley   +1 more source

Novel cruzain inhibitors for the treatment of Chagas' disease. [PDF]

open access: yes, 2012
The protozoan parasite Trypanosoma cruzi, the etiological agent of Chagas' disease, affects millions of individuals and continues to be an important global health concern.
Arkin, Michelle R   +6 more
core   +1 more source

The Caenorhabditis elegans DPF‐3 and human DPP4 have tripeptidyl peptidase activity

open access: yesFEBS Letters, EarlyView.
The dipeptidyl peptidase IV (DPPIV) family comprises serine proteases classically defined by their ability to remove dipeptides from the N‐termini of substrates, a feature that gave the family its name. Here, we report the discovery of a previously unrecognized tripeptidyl peptidase activity in DPPIV family members from two different species.
Aditya Trivedi, Rajani Kanth Gudipati
wiley   +1 more source

Accessory mutations balance the marginal stability of the HIV-1 protease in drug resistance

open access: yes, 2020
The HIV-1 protease is a major target of inhibitor drugs in AIDS therapies. The therapies are impaired by mutations of the HIV-1 protease that can lead to resistance to protease inhibitors.
Hemmateenejad, B., Weikl, T.
core   +1 more source

Identification of drug resistance mutations in HIV from constraints on natural evolution [PDF]

open access: yes, 2015
Human immunodeficiency virus (HIV) evolves with extraordinary rapidity. However, its evolution is constrained by interactions between mutations in its fitness landscape.
Barton, John P.   +3 more
core   +2 more sources

Crosstalk between the ribosome quality control‐associated E3 ubiquitin ligases LTN1 and RNF10

open access: yesFEBS Letters, EarlyView.
Loss of the E3 ligase LTN1, the ubiquitin‐like modifier UFM1, or the deubiquitinating enzyme UFSP2 disrupts endoplasmic reticulum–ribosome quality control (ER‐RQC), a pathway that removes stalled ribosomes and faulty proteins. This disruption may trigger a compensatory response to ER‐RQC defects, including increased expression of the E3 ligase RNF10 ...
Yuxi Huang   +8 more
wiley   +1 more source

Commentary on the role of treatment-related HIV compensatory mutations on increasing virulence: new discoveries twenty years since the clinical testing of protease inhibitors to block HIV-1 replication

open access: yesBMC Medicine, 2012
Approximately 20 years has passed since the first human trial with HIV-1 protease inhibitors. Protease inhibitors set the stage for combination therapy in the mid-1990s but are now rarely used in first-line combination therapy and reserved for salvage ...
Arts Eric J
doaj   +1 more source

Peptide‐based ligand antagonists block a Vibrio cholerae adhesin

open access: yesFEBS Letters, EarlyView.
The structure of a peptide‐binding domain of the Vibrio cholerae adhesin FrhA was solved by X‐ray crystallography, revealing how the inhibitory peptide AGYTD binds tightly at its Ca2+‐coordinated pocket. Structure‐guided design incorporating D‐amino acids enhanced binding affinity, providing a foundation for developing anti‐adhesion therapeutics ...
Mingyu Wang   +9 more
wiley   +1 more source

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