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Correlated mutations at gp120 positions 322 and 440: Implications for gp120 structure.
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- Proteins, 2008, v. 71, n. 3, p. 1066, doi. 10.1002/prot.21982
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- Article
The methyl 13C-edited/13C-filtered transferred NOE for studying protein interactions with short linear motifs.
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- Journal of Biomolecular NMR, 2020, v. 74, n. 12, p. 681, doi. 10.1007/s10858-020-00340-y
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- Article
The chemokines CCL5 and CXCL12 exhibit high‐affinity binding to N‐terminal peptides of the non‐cognate receptors CXCR4 and CCR5, respectively.
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- FEBS Journal, 2024, v. 291, n. 3, p. 458, doi. 10.1111/febs.17013
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- Article
Multiple binding modes of an N‐terminal CCR5‐peptide in complex with HIV‐1 gp120.
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- 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
LIGHT SCATTERING BY CHROMOPHORES AT THEIR ABSORPTION BANDS.
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- Annals of the New York Academy of Sciences, 1981, v. 366, n. 1, p. 125, doi. 10.1111/j.1749-6632.1981.tb20750.x
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- Article
Two-Dimensional nmr studies of the interactions between a peptide of cholera toxin and monoclonal antibodies.
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- Biopolymers, 1995, v. 37, n. 6, p. 383, doi. 10.1002/bip.360370605
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- Article
The solution structure of monomeric CCL5 in complex with a doubly sulfated N‐terminal segment of CCR5.
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- FEBS Journal, 2018, v. 285, n. 11, p. 1988, doi. 10.1111/febs.14460
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- Article
Detection of intermolecular transferred-NOE interactions in small and medium size protein complexes: RANTES complexed with a CCR5 N-terminal peptide.
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- FEBS Journal, 2017, v. 284, n. 4, p. 586, doi. 10.1111/febs.14000
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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
NMR mapping of RANTES surfaces interacting with CCR5 using linked extracellular domains.
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- FEBS Journal, 2013, v. 280, n. 9, p. 2068, doi. 10.1111/febs.12230
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- Article
Use of deuterium labelling in NMR studies of antibody combining site structure.
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- Quarterly Reviews of Biophysics, 1990, v. 23, n. 2, p. 175, doi. 10.1017/S0033583500005539
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- Article
A cis proline turn linking two β-hairpin strands in the solution structure of an antibody-bound HIV-1<sub>IIIB</sub> V3 peptide.
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- Nature Structural Biology, 1999, v. 6, n. 4, p. 331
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- Article
Solid?state NMR evidence for an antibody?dependent conformation of the V3 loop of HIV?1 gp120.
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- Nature Structural Biology, 1999, v. 6, n. 2, p. 141
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- Article
Probing hydrogen bonds in the antibody-bound HIV-1 gp120 V3 loop by solid state NMR REDOR measurements.
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- Journal of Biomolecular NMR, 2000, v. 16, n. 4, p. 313, doi. 10.1023/A:1008343623240
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- Article
Determination of the human type I interferon receptor binding site on human interferon-α2 by cross saturation and an NMR-based model of the complex.
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- Protein Science: A Publication of the Protein Society, 2006, v. 15, n. 11, p. 2656, doi. 10.1110/ps.062283006
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- Article