Superior HIV-1 TAR Binders with Conformationally Constrained R52 Arginine Mimics in the Tat(48-57) Peptide.

scientific article published on 4 January 2018

Superior HIV-1 TAR Binders with Conformationally Constrained R52 Arginine Mimics in the Tat(48-57) Peptide. is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1002/CMDC.201700653
P8608Fatcat IDrelease_bt4vklcso5f7llkdhvmpehoepu
P698PubMed publication ID29314706

P50authorSantosh KumarQ44565398
Moneesha FernandesQ87897073
Souvik MaitiQ18217615
P2093author name stringDurba Sengupta
Govind S Bhosle
Shalmali Kharche
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Structure-guided peptidomimetic design leads to nanomolar beta-hairpin inhibitors of the Tat-TAR interaction of bovine immunodeficiency virusQ27643539
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Sequence-specific interaction of Tat protein and Tat peptides with the transactivation-responsive sequence element of human immunodeficiency virus type 1 in vitroQ33900660
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Calculating thermodynamic data for transitions of any molecularity from equilibrium melting curvesQ36472087
Discovery of selective, small-molecule inhibitors of RNA complexes—1. The tat protein/TAR RNA complexes required for HIV-1 transcriptionQ36870972
Specific binding of arginine to TAR RNAQ36918014
What does the structure-function relationship of the HIV-1 Tat protein teach us about developing an AIDS vaccine?Q37220038
Circular dichroism and molecular modeling yield a structure for the complex of human immunodeficiency virus type 1 trans-activation response RNA and the binding region of Tat, the trans-acting transcriptional activatorQ37251783
P433issue3
P304page(s)220-226
P577publication date2018-01-15
P1433published inChemMedChemQ2962252
P1476titleSuperior HIV-1 TAR Binders with Conformationally Constrained R52 Arginine Mimics in the Tat(48-57) Peptide
P478volume13

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