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Publications by Sara S. Yücel

Nucleoporin NUP153 Phenylalanine-Glycine Motifs Engage a Common Binding Pocket Within the HIV-1 Capsid Protein to Mediate Lentiviral Infectivity

PLoS Pathogens

English

Related publications

HIV-1 Capsid Undergoes Coupled Binding and Isomerization by the Nuclear Pore Protein NUP358

English

BI-2 Destabilizes HIV-1 Cores During Infection and Prevents Binding of CPSF6 to the HIV-1 Capsid

English

Distinct Sequence Motifs Within the 68-kDa Subunit of Cleavage Factor I M Mediate RNA Binding, Protein-Protein Interactions, and Subcellular Localization

Journal of Biological Chemistry

English

HIV-1 Protease Dimerization Dynamics Reveals a Transient Druggable Binding Pocket at the Interface

Scientific Reports

Multidisciplinary

2015

English

Structure of the HIV-1 Full-Length Capsid Protein in a Conformationally Trapped Unassembled State Induced by Small-Molecule Binding

Journal of Molecular Biology

English

Conserved GU-Rich Elements Mediate mRNA Decay by Binding to CUG-Binding Protein 1

English

Cyclic Peptides Can Engage a Single Binding Pocket Through Multiple, Entirely Divergent Modes

2019

English

Solid-State NMR Studies of HIV-1 Capsid Protein Assemblies

Journal of the American Chemical Society

English

Mutations in the Zinc-Binding Motif of the Reovirus Capsid Protein Delta 3 Eliminate Its Ability to Associate With Capsid Protein Mu 1.

English

Amanote Research

Discover open access scientific publications

Search, annotate, share and cite publications

Publications by Sara S. Yücel

Nucleoporin NUP153 Phenylalanine-Glycine Motifs Engage a Common Binding Pocket Within the HIV-1 Capsid Protein to Mediate Lentiviral Infectivity

Related publications

HIV-1 Capsid Undergoes Coupled Binding and Isomerization by the Nuclear Pore Protein NUP358

BI-2 Destabilizes HIV-1 Cores During Infection and Prevents Binding of CPSF6 to the HIV-1 Capsid

Distinct Sequence Motifs Within the 68-kDa Subunit of Cleavage Factor I M Mediate RNA Binding, Protein-Protein Interactions, and Subcellular Localization

HIV-1 Protease Dimerization Dynamics Reveals a Transient Druggable Binding Pocket at the Interface

Structure of the HIV-1 Full-Length Capsid Protein in a Conformationally Trapped Unassembled State Induced by Small-Molecule Binding

Conserved GU-Rich Elements Mediate mRNA Decay by Binding to CUG-Binding Protein 1

Cyclic Peptides Can Engage a Single Binding Pocket Through Multiple, Entirely Divergent Modes

Solid-State NMR Studies of HIV-1 Capsid Protein Assemblies

Mutations in the Zinc-Binding Motif of the Reovirus Capsid Protein Delta 3 Eliminate Its Ability to Associate With Capsid Protein Mu 1.