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Multiple binding modes of an N‐terminal CCR5‐peptide in complex with HIV‐1 gp120.
- Published in:
- FEBS Journal, 2022, v. 289, n. 11, p. 3132, doi. 10.1111/febs.16328
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- Article
Allovalency observed by transferred NOE: interactions of sulfated tyrosine residues in the N‐terminal segment of CCR5 with the CCL5 chemokine.
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- FEBS Journal, 2021, v. 288, n. 5, p. 1648, doi. 10.1111/febs.15503
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- Article
Defining specific residue‐to‐residue interactions between the gp120 bridging sheet and the N‐terminal segment of CCR5: applications of transferred NOE NMR.
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- FEBS Journal, 2018, v. 285, n. 22, p. 4296, doi. 10.1111/febs.14673
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- Article
Detection of intermolecular transferred NOEs in large protein complexes using asymmetric deuteration: HIV-1 gp120 in complex with a CCR5 peptide.
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- FEBS Journal, 2016, v. 283, n. 22, p. 4084, doi. 10.1111/febs.13916
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- Article
The C4 region as a target for HIV entry inhibitors - NMR mapping of the interacting segments of T20 and gp120.
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- FEBS Journal, 2015, v. 282, n. 24, p. 4643, doi. 10.1111/febs.13541
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- Article
An extended CCR5 ECL2 peptide forms a helix that binds HIV-1 gp120 through non-specific hydrophobic interactions.
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- FEBS Journal, 2015, v. 282, n. 10, p. 1906, doi. 10.1111/febs.13243
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- Article
NMR observation of HIV-1 gp120 conformational flexibility resulting from V3 truncation.
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- FEBS Journal, 2014, v. 281, n. 13, p. 3019, doi. 10.1111/febs.12839
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- Article