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

