J. Anglister

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NMR structure of an anti-gp120 antibody complex with a V3 peptide reveals a surface important for co-receptor binding.

V. Tugarinov, A. Zvi, R. Levy, 2000, Structure.

Three-dimensional solution structure of the complex of alpha-bungarotoxin with a library-derived peptide.

E. Katchalski‐Katzir, J. Anglister, M. Balass, 1997, Proceedings of the National Academy of Sciences of the United States of America.

The mechanism for acetylcholine receptor inhibition by alpha-neurotoxins and species-specific resistance to alpha-bungarotoxin revealed by NMR.

M. Eisenstein, J. Anglister, A. Samson, 2002, Neuron.

Carbon-13 line narrowing by deuterium decoupling in deuterium/carbon-13/nitrogen-15 enriched proteins. Application to triple resonance 4D J connectivity of sequential amides

S. Grzesiek, A. Bax, J. Anglister, 1993 .

Solution structures of a highly insecticidal recombinant scorpion alpha-toxin and a mutant with increased activity.

V. Tugarinov, J. Anglister, M. Gurevitz, 1997, Biochemistry.

Sodium channel modifiers from scorpion venom: structure-activity relationship, mode of action and application.

V. Tugarinov, J. Anglister, M. Adams, 1998, Toxicon : official journal of the International Society on Toxinology.

A T1 rho-filtered two-dimensional transferred NOE spectrum for studying antibody interactions with peptide antigens.

J. Anglister, T. Scherf, 1993, Biophysical journal.

Expression, purification, and isotope labeling of a gp120 V3 peptide and production of a Fab from a HIV-1 neutralizing antibody for NMR studies.

R. Levy, Y. Hayek, J. Anglister, 2002, Protein expression and purification.

NMR mapping of RANTES surfaces interacting with CCR5 using linked extracellular domains

J. Anglister, N. Kessler, F. Naider, 2013, The FEBS journal.

A monomeric 3(10)-helix is formed in water by a 13-residue peptide representing the neutralizing determinant of HIV-1 on gp41.

Y. Hayek, J. Anglister, F. Naider, 2002, Biochemistry.

J. Anglister, A. Samson, Osnat Rosen, 2008, Proteins.

Multiple binding modes of an N‐terminal CCR5‐peptide in complex with HIV‐1 gp120

J. Anglister, F. Naider, Sabine R. Akabayov, 2021, The FEBS journal.

Defining specific residue‐to‐residue interactions between the gp120 bridging sheet and the N‐terminal segment of CCR5: applications of transferred NOE NMR

J. Anglister, N. Kessler, F. Naider, 2018, The FEBS journal.

NMR backbone dynamics of the human type I interferon binding subunit, a representative cytokine receptor.

J. Anglister, J. Chill, S. Quadt, 2004, Biochemistry.

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

R. Levy, J. Anglister, N. Kessler, 2006, Protein science : a publication of the Protein Society.

The solution structure of monomeric CCL5 in complex with a doubly sulfated N‐terminal segment of CCR5

M. Levitt, J. Anglister, F. Naider, 2018, The FEBS journal.

2D-NMR and ATR-FTIR study of the structure of a cell-selective diastereomer of melittin and its orientation in phospholipids.

J. Anglister, Y. Shai, M. Sharon, 1999, Biochemistry.

The membrane proximal external region of the HIV-1 envelope glycoprotein gp41 contributes to the stabilization of the six-helix bundle formed with a matching N' peptide.

J. Anglister, F. Naider, B. Arshava, 2008, Biochemistry.

An Efficient and Facile Synthesis of Tyrosine-Sulfate-Containing Peptides: Synthesis of the N-Terminal Peptide of CCR5 and Its Analog

J. Anglister, F. Naider, Patricia Cano, 2006 .

Line-shape analysis of NMR difference spectra of an anti-spin-label antibody.

J. Anglister, H. Mcconnell, T. Frey, 1988, Biochemistry.

NMR study of the complexes between a synthetic peptide derived from the B subunit of cholera toxin and three monoclonal antibodies against it.

J. Anglister, C. Jacob, G. Ast, 1988, Biochemistry.

Distances of tyrosine residues from a spin-label hapten in the combining site of a specific monoclonal antibody.

J. Anglister, H. Mcconnell, T. Frey, 1984, Biochemistry.

Diversity of Molecular Recognition: The Combining Sites of Monoclonal Anti Spin Label Antibodies

J. Anglister, H. Mcconnell, M. Whittaker, 1986 .

NMR analysis of interaction of LqhalphaIT scorpion toxin with a peptide corresponding to the D4/S3-S4 loop of insect para voltage-gated sodium channel.

J. Anglister, D. Gordon, M. Gurevitz, 2008, Biochemistry.

Resonance Rayleigh scattering of cyanine dyes in solution

I. Z. Steinberg, J. Anglister, 1983 .

Measurement of the depolarization ratio of Rayleigh scattering at absorption bands

I. Z. Steinberg, J. Anglister, 1981 .

Synthesis and NMR Analysis of CCR5 and CXCR4 Peptides Containing Tyrosine Sulfate

Inbal Ayzenshtat, J. Anglister, F. Naider, 2006 .

Contribution of tryptophan residues to the combining site of a monoclonal anti dinitrophenyl spin-label antibody.

M. Levitt, J. Anglister, D. Leahy, 1987, Biochemistry.

NMR technique for assessing contributions of heavy and light chains to an antibody combining site

J. Anglister, H. Mcconnell, T. Frey, 1985, Nature.

Magnetic resonance of a monoclonal anti-spin-label antibody

J. Anglister, H. Mcconnell, T. Frey, 1984 .

Stabilization of the biologically active conformation of the principal neutralizing determinant of HIV-1(IIIB) containing a cis-proline surrogate: 1H NMR and molecular modeling study.

J. Anglister, P. Dumy, Julian Garcia, 2006, Biochemistry.

Use of deuterium labelling in NMR studies of antibody combining site structure

J. Anglister, 1990, Quarterly Reviews of Biophysics.

Depolarized rayleigh light scattering in absorption bands measured in lycopene solution

I. Z. Steinberg, J. Anglister, 1979 .

Resonance rayleigh light scattering of some porphyrins in solution: Intensities and depolarization ratios

I. Z. Steinberg, J. Anglister, 1983 .

Correlation of Backbone Amide and Aliphatic Side-Chain Resonances in 13C/15N-Enriched Proteins by Isotropic Mixing of 13C Magnetization

S. Grzesiek, A. Bax, J. Anglister, 1993 .

1H, 13C, 15N nuclear magnetic resonance backbone assignments and secondary structure of human calcineurin B.

S. Grzesiek, A. Bax, C. Klee, 1994, Biochemistry.

Probing antibody diversity by 2D NMR: comparison of amino acid sequences, predicted structures, and observed antibody-antigen interactions in complexes of two antipeptide antibodies.

M. Levitt, R. Levy, J. Anglister, 1989, Biochemistry.

NMR mapping and secondary structure determination of the major acetylcholine receptor alpha-subunit determinant interacting with alpha-bungarotoxin.

J. Anglister, A. Samson, T. Scherf, 2001, Biochemistry.

Alternative conformations of HIV-1 V3 loops mimic beta hairpins in chemokines, suggesting a mechanism for coreceptor selectivity.

Michal Sharon, Matthias Görlach, Rina Levy, 2003, Structure.

Immunofocusing using conformationally constrained V3 peptide immunogens improves HIV-1 neutralization.

J. Anglister, F. Naider, E. Sinha, 2017, Vaccine.

Synergism between a CD4-mimic peptide and antibodies elicited by a constrained V3 peptide.

J. Anglister, F. Naider, F. Ding, 2013, AIDS research and human retroviruses.

An optimally constrained V3 peptide is a better immunogen than its linear homolog or HIV-1 gp120.

J. Anglister, F. Naider, S. Tantry, 2010, Virology.

The human type I interferon receptor: NMR structure reveals the molecular basis of ligand binding.

R. Levy, J. Anglister, G. Schreiber, 2003, Structure.

The human interferon receptor: NMR-based modeling, mapping of the IFN-alpha 2 binding site, and observed ligand-induced tightening.

S. Albeck, R. Levy, J. Anglister, 2002, Biochemistry.

Nuclear magnetic resonance for studying peptide-antibody complexes by transferred nuclear Overhauser effect difference spectroscopy.

J. Anglister, F. Naider, 1991, Methods in enzymology.

Interactions of antibody aromatic residues with a peptide of cholera toxin observed by two-dimensional transferred nuclear Overhauser effect difference spectroscopy.

R. Levy, J. Anglister, T. Scherf, 1989, Biochemistry.

Solution Structure of an Antibody-Bound HIV-1IIIB V3 Peptide: A Cis Proline Turn Linking Two β-hairpin Strands

V. Tugarinov, J. Anglister, 2000, Journal of biomolecular structure & dynamics.

A cis proline turn linking two β-hairpin strands in the solution structure of an antibody-bound HIV-1IIIB V3 peptide

Rina Levy, Anat Zvi, V. Tugarinov, 1999, Nature Structural Biology.

Two-dimensional measurement of proton T1rho relaxation in unlabeled proteins: mobility changes in alpha-bungarotoxin upon binding of an acetylcholine receptor peptide.

J. Anglister, A. Samson, J. Chill, 2005, Biochemistry.

Induced peptide conformations in different antibody complexes: molecular modeling of the three-dimensional structure of peptide-antibody complexes using NMR-derived distance restraints.

M. Levitt, J. Anglister, F. Naider, 1992, Biochemistry.

NMR mapping of the IFNAR1-EC binding site on IFNalpha2 reveals allosteric changes in the IFNAR2-EC binding site.

J. Anglister, Peter Lamken, J. Piehler, 2010, Biochemistry.

Letter to the Editor: Backbone and Cβ assignments of the anti-gp120 antibody Fv fragment complexed with an antigenic peptide

V. Tugarinov, R. Levy, J. Anglister, 1999, Journal of biomolecular NMR.

Isotope-edited multidimensional NMR of calcineurin B in the presence of the non-deuterated detergent CHAPS

S. Grzesiek, A. Bax, C. Klee, 1993, Journal of biomolecular NMR.

The Mechanism for Acetylcholine Receptor Inhibition by α-Neurotoxins and Species-Specific Resistance to α-Bungarotoxin Revealed by NMR

M. Eisenstein, J. Anglister, A. Samson, 2002, Neuron.

Yeast Expression and NMR Analysis of the Extracellular Domain of Muscle Nicotinic Acetylcholine Receptor α Subunit*

J. Anglister, A. Samson, J. Chill, 2002, The Journal of Biological Chemistry.

Scorpion neurotoxins: structure/function relationships and application in agriculture†

Oren Froy, Boaz Shaanan, J. Anglister, 2000 .

HIV-1 peptide vaccine candidates: selecting constrained V3 peptides with highest affinity to antibody 447-52D.

B. Mester, J. Anglister, F. Naider, 2009, Biochemistry.

NMR Mapping and Secondary Structure Determination of the Major Acetylcholine Receptor R-Subunit Determinant Interacting with R-Bungarotoxin

J. Anglister, A. Samson, T. Scherf, 2001 .

Detection of intermolecular NOE interactions in large protein complexes.

Gautam Srivastava, J. Anglister, F. Naider, 2016, Progress in nuclear magnetic resonance spectroscopy.

Molecular switch for alternative conformations of the HIV-1 V3 region: Implications for phenotype conversion

Michal Sharon, J. Anglister, M. Sharon, 2006, Proceedings of the National Academy of Sciences.

NMR observation of HIV‐1 gp120 conformational flexibility resulting from V3 truncation

J. Anglister, N. Kessler, F. Naider, 2014, The FEBS journal.

Solution conformation of a peptide corresponding to the principal neutralizing determinant of HIV-1IIIB: a two-dimensional NMR study.

A. Zvi, J. Anglister, R. Hiller, 1992, Biochemistry.

The conformation and orientation of a 27-residue CCR5 peptide in a ternary complex with HIV-1 gp120 and a CD4-mimic peptide.

Inbal Ayzenshtat, R. Levy, J. Anglister, 2011, Journal of molecular biology.

Mimicking the structure of the V3 epitope bound to HIV-1 neutralizing antibodies.

B. Mester, J. Anglister, F. Naider, 2009, Biochemistry.

A model of a gp120 V3 peptide in complex with an HIV-neutralizing antibody based on NMR and mutant cycle-derived constraints.

A. Horovitz, V. Tugarinov, A. Zvi, 2000, European journal of biochemistry.

The 2F5 epitope is helical in the HIV-1 entry inhibitor T-20.

Y. Hayek, J. Anglister, F. Naider, 2005, Biochemistry.

Detection of intermolecular transferred NOEs in large protein complexes using asymmetric deuteration: HIV‐1 gp120 in complex with a CCR5 peptide

J. Anglister, N. Kessler, F. Naider, 2016, The FEBS journal.

Observation of intermolecular interactions in large protein complexes by 2D-double difference nuclear Overhauser enhancement spectroscopy: application to the 44 kDa interferon-receptor complex.

J. Anglister, I. Nudelman, T. Scherf, 2011, Journal of the American Chemical Society.

Intermolecular interactions in a 44 kDa interferon-receptor complex detected by asymmetric reverse-protonation and two-dimensional NOESY.

R. Levy, J. Anglister, I. Nudelman, 2010, Biochemistry.

The C4 region as a target for HIV entry inhibitors – NMR mapping of the interacting segments of T20 and gp120

J. Anglister, F. Naider, T. Scherf, 2015, The FEBS journal.

Peptides in the treatment of AIDS.

J. Anglister, F. Naider, Jacob Anglister, 2009, Current opinion in structural biology.

A monomeric 3(10)-helix is formed in water by a 13-residue peptide representing the neutralizing determinant of HIV-1 on gp41.

Y. Hayek, J. Anglister, F. Naider, 2002, Biochemistry.

Epitope mapping of antibody-antigen complexes by nuclear magnetic resonance spectroscopy.

J. Anglister, Osnat Rosen, 2009, Methods in molecular biology.

Induced fit in HIV-neutralizing antibody complexes: evidence for alternative conformations of the gp120 V3 loop and the molecular basis for broad neutralization.

S. Zolla-Pazner, B. Mester, J. Anglister, 2005, Biochemistry.

Solid–state NMR evidence for an antibody–dependent conformation of the V3 loop of HIV–1 gp120

A. Zvi, J. Anglister, R. Tycko, 1999, Nature Structural Biology.

An extended CCR5 ECL2 peptide forms a helix that binds HIV‐1 gp120 through non‐specific hydrophobic interactions

J. Anglister, N. Kessler, F. Naider, 2015, The FEBS journal.

Expression, purification, and isotope labeling of the Fv of the human HIV-1 neutralizing antibody 447-52D for NMR studies.

M. Gorny, A. Zvi, R. Levy, 2003, Protein expression and purification.

NMR mapping of the antigenic determinant recognized by an anti-gp120, human immunodeficiency virus neutralizing antibody.

M. Eisenstein, A. Zvi, R. Levy, 1995, European journal of biochemistry.

Probing hydrogen bonds in the antibody-bound HIV-1 gp120 V3 loop by solid state NMR REDOR measurements

V. Tugarinov, J. Anglister, R. Tycko, 2000, Journal of biomolecular NMR.

NMR identification of calcineurin B residues affected by binding of a calcineurin A peptide

A. Bax, C. Klee, J. Anglister, 1995, FEBS letters.

Nonaromatic amino acids in the combining site region of a monoclonal anti-spin-label antibody.

J. Anglister, H. Mcconnell, T. Frey, 1984, Biochemistry.

Magnetic Resonance Study of the Combining Site Structure of a Monoclonal Anti-Spin-Label Antibody

J. Anglister, 1989 .

Detection of intermolecular transferred‐NOE interactions in small and medium size protein complexes: RANTES complexed with a CCR5 N‐terminal peptide

J. Anglister, F. Naider, B. Arshava, 2017, The FEBS journal.

Contribution of Arginine Residues in the RP135 Peptide Derived from the V3 Loop of gp120 to Its Interaction with the Fv Fragment of the 0.5β HIV-1 Neutralizing Antibody*

A. Horovitz, R. Levy, J. Anglister, 1996, The Journal of Biological Chemistry.

The principal neutralizing determinant of HIV-1IIIB: Conformation of the peptide bound to a neutralizing antibody studied by 2D-NMR

A. Zvi, J. Anglister, 1998, Letters in Peptide Science.

Application of NMR to Conformational Studies of an HIV Peptide Bound to a Neutralizing Antibody

A. Zvi, J. Anglister, 1999 .

NMR-derived model for a peptide-antibody complex.

M. Levitt, J. Anglister, B. Zilber, 1990, Biochemistry.

2D-measurement of proton T 1 ρ relaxation in unlabeled proteins: Mobility changes in α -bungarotoxin upon binding of an acetylcholine receptor peptide.

J. Anglister, J. Chill, Avraham O. Samson, 2008 .

Conformation of the principal neutralizing determinant of human immunodeficiency virus type 1 in complex with an anti-gp120 virus neutralizing antibody studied by two-dimensional nuclear magnetic resonance difference spectroscopy.

A. Zvi, Y. Hayek, J. Anglister, 1997, Biochemistry.

The chemokines CCL5 and CXCL12 exhibit high‐affinity binding to N‐terminal peptides of the non‐cognate receptors CXCR4 and CCR5, respectively

J. Anglister, N. Kessler, T. Scherf, 2023, The FEBS journal.

Allovalency observed by transferred NOE: interactions of sulfated tyrosine residues in the N‐terminal segment of CCR5 with the CCL5 chemokine

L. Kay, J. Anglister, N. Kessler, 2020, The FEBS journal.

The conformation and orientation of a 27-residue CCR5 peptide in a ternary complex with HIV-1 gp120 and a CD4-mimic peptide.

Inbal Ayzenshtat, R. Levy, J. Anglister, 2011, Journal of molecular biology.

The methyl 13C-edited/13C-filtered transferred NOE for studying protein interactions with short linear motifs

L. Kay, J. Anglister, N. Kessler, 2020, Journal of Biomolecular NMR.