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ROP2 from Toxoplasma gondii: a virulence factor with a protein-kinase fold and no enzymatic activity.
Fragment-based discovery of a new family of non-peptidic small-molecule cyclophilin inhibitors with potent antiviral activities
- A. Ahmed-Belkacem, L. Colliandre, J. Guichou
- Chemistry, BiologyNature communications
- 22 September 2016
A fragment-based drug discovery approach using nucleic magnetic resonance, X-ray crystallography and structure-based compound optimization is used to generate a new family of non-peptidic, small-molecule cyclophilin inhibitors with potent in vitro PPIase inhibitory activity and antiviral activity against hepatitis C virus, human immunodeficiency virus and coronaviruses.
Intrinsic disorder in Viral Proteins Genome-Linked: experimental and predictive analyses
This paper reports the bacterial expression, purification and biochemical characterization of two phytoviral VPgs, namely the VPgs of Rice yellow mottle virus and Lettuce mosaic virus, and proposes that intrinsic disorder is a common feature of VPgs.
Structural insight into the Mycobacterium tuberculosis Rv0020c protein and its interaction with the PknB kinase.
Homodimerization of RBPMS2 through a new RRM-interaction motif is necessary to control smooth muscle plasticity
This study demonstrates that RBPMS2 possesses an RRM domain harboring both RNA-binding and protein-binding properties and that the newly identified RRM-homodimerization motif is crucial for the function of RBP MS2 at the cell and tissue levels.
Microcin E492 antibacterial activity: evidence for a TonB‐dependent inner membrane permeabilization on Escherichia coli
It is proposed that MccE492 is recognized by iron‐siderophore receptors, including FepA, which promote its import across the outer membrane via a TonB‐ and energy‐dependent pathway, and then inserts into the inner membrane, whereupon the potential becomes destabilized by pore formation.
Direct interaction between the Rice yellow mottle virus (RYMV) VPg and the central domain of the rice eIF(iso)4G1 factor correlates with rice susceptibility and RYMV virulence.
- E. Hébrard, N. Poulicard, F. Vignols
- BiologyMolecular plant-microbe interactions : MPMI
- 5 October 2010
A direct interaction between RYMV VPg and the central domain of rice eIF(iso)4G1 is demonstrated both in vitro, using recombinant proteins, and in vivo, using a yeast two-hybrid assay, explaining the prevalence of virulence mutations fixed during experimental evolution studies and are consistent with the respective viral RNA accumulation levels of avirulent and virulent isolates.
Antibacterial peptide pleurocidin forms ion channels in planar lipid bilayers.
The RYMV-encoded viral suppressor of RNA silencing P1 is a zinc-binding protein with redox-dependent flexibility.