Publications

2018

97.
Srivastava G., Moseri A., Kessler N., Arshava B., Naider F. & Anglister J. (2018). Defining specific residue-to-residue interactions between the gp120 bridging sheet and the N-terminal segment of CCR5: applications of transferred NOE NMR.  FEBS Journal. 285:(22)4296-4310.  Abstract
96.
Abayev M., Rodrigues J. P. G. L. M., Srivastava G., Arshava B., Jaremko L., Jaremko M., Naider F., Levitt M. & Anglister J. (2018). The solution structure of monomeric CCL5 in complex with a doubly sulfated N-terminal segment of CCR5.  FEBS Journal. 285:(11)1988-2003.  Abstract
95.
Naider F. & Anglister J. (2018). The Synthesis of Sulfated CCR5 Peptide Surrogates and their Use to Study Receptor-Ligand Interactions.  Protein and Peptide Letters. 25:(12)1124-1136.  Abstract

2017

94.
Moseri A., Srivastava G., Kessler N., Arshava B., Naider F. & Anglister J. (2017). Detection of pair-wise intermolecular interactions in large protein complexes using NMR tr-NOE and specific methyl labeling of HIV-1 gp120 in complex with a CCR5 peptide.  FEBS Journal. 284:196-196.  Abstract
93.
Abayev M., Srivastava G., Arshava B., Naider F. & Anglister J. (2017). Detection of intermolecular transferred-NOE interactions in small and medium size protein complexes: RANTES complexed with a CCR5 N-terminal peptide.  FEBS Journal. 284:(4)586-601.  Abstract
92.
Moseri A., Sinha E., Zommer H., Arshava B., Naider F. & Anglister J. (2017). Immunofocusing using conformationally constrained V3 peptide immunogens improves HIV-1 neutralization.  Vaccine. 35:(2)222-230.  Abstract

2016

91.
Anglister J., Srivastava G. & Naider F. (2016). Detection of intermolecular NOE interactions in large protein complexes.  Progress in Nuclear Magnetic Resonance Spectroscopy. 97:40-56.  Abstract
90.
Srivastava G., Moseri A., Kessler N., Akabayov S. R., Arshava B., Naider F. & Anglister J. (2016). Detection of intermolecular transferred NOEs in large protein complexes using asymmetric deuteration: HIV-1 gp120 in complex with a CCR5 peptide.  FEBS Journal. 283:(22)4084-4096.  Abstract

2015

89.
Moseri A., Biron Z., Arshava B., Scherf T., Naider F. & Anglister J. (2015). The C4 region as a target for HIV entry inhibitors - NMR mapping of the interacting segments of T20 and gp120.  The FEBS journal. 282:(24)4643-57.  Abstract
88.
Abayev M., Moseri A., Tchaicheeyan O., Kessler N., Arshava B., Naider F., Scherf T. & Anglister J. (2015). An extended CCR5 ECL2 peptide forms a helix that binds HIV-1 gp120 through non-specific hydrophobic interactions.  FEBS Journal. 282:(10)1906-1921.  Abstract

2014

87.
Moseri A., Schnur E., Noah E., Zherdev Y., Kessler N., Sinha E. S., Abayev M., Naider F., Scherf T. & Anglister J. (2014). NMR observation of HIV-1 gp120 conformational flexibility resulting from V3 truncation.  FEBS Journal. 281:(13)3019-3031.  Abstract

2013

86.
Moseri A., Tantry S., Arshava B., Naider F. & Anglister J. (2013). Sequential Immunization Approach for the V3 Epitope Using Constrained Peptides.  AIDS Research and Human Retroviruses. 29:(11)A144-A144.  Abstract
85.
Schnur E., Kessler N., Zherdev Y., Noah E., Scherf T., Ding F., Rabinovich S., Arshava B., Kurbatska V., Leonciks A., Tsimanis A., Rosen O., Naider F. & Anglister J. (2013). NMR mapping of RANTES surfaces interacting with CCR5 using linked extracellular domains.  FEBS Journal. 280:(9)2068-2084.  Abstract
84.
Moseri A., Tantry S., Ding F., Naider F. & Anglister J. (2013). Short Communication Synergism Between a CD4-Mimic Peptide and Antibodies Elicited by a Constrained V3 Peptide.  AIDS Research and Human Retroviruses. 29:(4)718-724.  Abstract

2011

83.
Moseri A., Sagi Y., Arshava B., Naider F. & Anglister J. (2011). Optimization of the V3 Directed Antibody Response: Strategies to Expose the Epitope.  AIDS Research and Human Retroviruses. 27:(10)A44-A44.  Abstract
82.
Nudelman I., Akabayov S. R., Scherf T. & Anglister J. (2011). Observation of Intermolecular Interactions in Large Protein Complexes by 2D-Double Difference Nuclear Overhauser Enhancement Spectroscopy: Application to the 44 kDa Interferon-Receptor Complex.  Journal of the American Chemical Society. 133:(37)14755-14764.  Abstract
81.
Schnur E., Noah E., Ayzenshtat I., Sargsyan H., Inui T., Ding F., Arshava B., Sagi Y., Kessler N., Levy R., Schere T., Naider F. & Anglister J. (2011). The Conformation and Orientation of a 27-Residue CCR5 Peptide in a Ternary Complex with HIV-1 gp120 and a CD4-Mimic Peptide.  Journal of Molecular Biology. 410:(5)778-797.  Abstract

2010

80.
Moseri A., Tantry S., Sagi Y., Arshava B., Naider F. & Anglister J. (2010). An optimally constrained V3 peptide is a better immunogen than its linear homolog or HIV-1 gp120.  Virology. 401:(2)293-304.  Abstract
79.
Rosen O., Moseri A. & Anglister J. (2010). HIV V3 structures as novel HIV immunogens.  FEBS Journal. 277:92-92.  Abstract
78.
Nudelman I., Akabayov S. R., Schnur E., Biron Z., Levy R., Xu Y., Yang D. & Anglister J. (2010). Intermolecular Interactions in a 44 kDa Interferon-Receptor Complex Detected by Asymmetric Reverse-Protonation and Two-Dimensional NOESY.  Biochemistry. 49:(25)5117-5133.  Abstract
77.
Nudelman I., Akabayov S. R., Schnur E., Biron Z., Levy R., Xu Y., Yang D. & Anglister J. (2010). NMR structural studies of the human interferon-alpha 2 complex with human type I Interferon receptor.  FEBS Journal. 277:197-197.  Abstract
76.
Schnur E., Scherf T., Naider F. & Anglister J. (2010). The HIV-1 gp120 interaction with Nt-CCR5-New insights from NMR.  FEBS Journal. 277:240-241.  Abstract
75.
Akabayov S. R., Biron Z., Lamken P., Piehler J. & Anglister J. (2010). NMR Mapping of the IFNAR1-EC Binding Site on IFN alpha 2 Reveals Allosteric Changes in the IFNAR2-EC Binding Site.  Biochemistry. 49:(4)687-695.  Abstract

2009

74.
Mester B., Manor R., Mor A., Arshava B., Rosen O., Ding F., Naider F. & Anglister J. (2009). HIV-1 Peptide Vaccine Candidates: Selecting Constrained V3 Peptides with Highest Affinity to Antibody 447-52D.  Biochemistry. 48:(33)7867-7877.  Abstract
73.
Naider F. & Anglister J. (2009). Peptides in the treatment of AIDS.  Current Opinion in Structural Biology. 19:(4)473-482.  Abstract
72.
Rosen O., Moseri A. & Anglister J. (2009). HIV V3 region structures as novel HIV immunogens.  FEBS Journal. 276:163-163.  Abstract
71.
Mor A., Segal E., Mester B., Arshava B., Rosen O., Ding F., Russo J., Dafni A., Schvartzman F., Scherf T., Naider F. & Anglister J. (2009). Mimicking the Structure of the V3 Epitope Bound to HIV-1 Neutralizing Antibodies.  Biochemistry. 48:(15)3288-3303.  Abstract
70.
Tantry S., Moseri A., Arshava B., Naider F. & Anglister J. (2009). SYNTHESIS AND BIOLOGICAL EVALUATION OF CONSTRAINED V3-PEPTIDE ANTI HIV-1 IMMUNOGENS CONJUGATED TO A T-CELL EPITOPE.  Biopolymers. 92:(4)326-326.  Abstract
69.
Moseri A., Naider F. & Anglister J. (2009). The V3 region of HIV-1: from NMR to vaccine design.  Retrovirology. 6.  Abstract
68.
Rosen O. & Anglister J. (2009). Epitope Mapping of Antibody-Antigen Complexes by Nuclear Magnetic Resonance Spectroscopy.  Epitope Mapping Protocols, Second Edition. 37-57.  Abstract

2008

67.
Moseri A. & Anglister J. (2008). HIV-1 V3 Peptides Constrained to their Native Conformation as Vaccine Candidates.  AIDS Research and Human Retroviruses. 24:95-95.  Abstract
66.
Rosen O., Moseri A. & Anglister J. (2008). HIV V3 Region Structures as Novel HIV Immunogens.  AIDS Research and Human Retroviruses. 24:93-93.  Abstract
65.
Noah E., Biron Z., Naider F., Arshava B. & Anglister J. (2008). 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.  Biochemistry. 47:(26)6782-6792.  Abstract
64.
Rosen O., Samson A. O. & Anglister J. (2008). Correlated mutations at gp120 positions 322 and 440: Implications for gp120 structure.  Proteins-Structure Function And Bioinformatics. 71:(3)1066-1070.  Abstract
63.
Schnur E., Turkov M., Kahn R., Gordon D., Gurevitz M. & Anglister J. (2008). NMR analysis of interaction of Lqh alpha IT scorpion toxin with a peptide corresponding to the D4/S3-S4 loop of insect para voltage-gated sodium channel.  Biochemistry. 47:(3)911-921.  Abstract

2007

62.
Anglister J., Rosen O., Sharon M., Tugarinov V., Kessler N. & Levy R. (2007). NMR structures of the HIV-1 v3 region suggest a mechanism for the virus phenotype conversion.  Journal of biomolecular structure & dynamics. 24:(6)670-670.  Abstract
61.
Anglister J., Goldberg E., Gordon D. & Gurevitz M. (2007). NMR mapping of scorpion-toxin binding-site for a peptide derived from the D4/S3-S4 loop of a voltage gated sodium channel.  Biopolymers. 88:(4)630-630.  Abstract

2006

60.
Quadt-Akabayov S. R., Chill J. H., Levy R., Kessler N. & Anglister J. (2006). Determination of the human type I interferon receptor binding site on human interferon-alpha 2 by cross saturation and an NMR-based model of the complex.  Protein Science. 15:(11)2656-2668.  Abstract
59.
Rosen O., Sharon M., Quadt-Akabayov S. R. & Anglister J. (2006). Molecular switch for alternative conformations of the HIV-1V3 region: Implications for phenotype conversion.  Proceedings of the National Academy of Sciences of the United States of America. 103:(38)13950-13955.  Abstract
58.
Garcia J., Dumy P., Rosen O. & Anglister J. (2006). Stabilization of the biologically active conformation of the principal neutralizing determinant of HIV-1(III)B containing a cis-proline surrogate: H-1 NMR and molecular modeling study.  Biochemistry. 45:(13)4284-4294.  Abstract
57.
Rosen O., Samson A., Sharon M., Zolla-Pazner S. & Anglister J. (2006). HIV-1 coreceptor selectivity: Structural analogy between HIV-1V3 regions and chemokine beta-hairpins is not the explanation - Response to matters arising.  Structure. 14:(4)649-651.

2005

56.
Biron Z., Khare S., Quadt S., Hayek Y., Naider F. & Anglister J. (2005). The 2F5 epitope is helical in the HIV-1 entry inhibitor T-20.  Biochemistry. 44:(41)13602-13611.  Abstract
55.
Sharon M., Rosen O. & Anglister J. (2005). NMR studies of V3 peptide complexes with antibodies suggest a mechanism for HIV-1 co-receptor selectivity.  Current Opinion In Drug Discovery & Development. 8:(5)601-612.  Abstract
54.
Samson A., Chill J. & Anglister J. (2005). Two-dimensional measurement of proton T-1p relaxation in unlabeled proteins: Mobility changes in alpha-bungarotoxin upon binding of an acetylcholine receptor peptide.  Biochemistry. 44:(32)10926-10934.  Abstract
53.
Rosen O., Chill J., Sharon M., Kessler N., Mester B., Zolla-Pazner S. & Anglister J. (2005). Induced fit in HIV-neutralizing antibody complexes: Evidence for alternative conformations of the gp120 V3 loop and the molecular basis for broad neutralization.  Biochemistry. 44:(19)7250-7258.  Abstract
52.
Sargsyan H., Arshava B., Cano P., Inui T., Anglister J. & Naider F. (2005). An efficient and facile synthesis of a sulfated tyrosine-containing peptide: Synthesis of an analog of the N-terminal peptide of CCR5.  Biopolymers. 80:(4)535-535.  Abstract
51.
Cano P., Inui T., Arshava B., Ayzenshtat I., Anglister J. & Naider F. (2005). Synthesis and NMR analysis of CCR5 and CXCR4 peptides containing tyrosine sulfate.  Biopolymers. 80:(4)526-526.  Abstract

2004

50.
Chill J., Quadt S. & Anglister J. (2004). NMR backbone dynamics of the human type I interferon binding subunit, a representative cytokine receptor.  Biochemistry. 43:(31)10127-10137.  Abstract

2003

49.
Chill J., Quadt S., Levy R., Schreiber G. & Anglister J. (2003). The human type I interferon receptor: NMR structure reveals the molecular basis of ligand binding.  Structure. 11:(7)791-802.  Abstract
48.
Kessler N., Zvi A., Ji M., Sharon M., Rosen O., Levy R., Gorny M., Zolla-Pazner S. & Anglister J. (2003). Expression, purification, and isotope labeling of the Fv of the human HIV-1 neutralizing antibody 447-52D for NMR studies.  Protein Expression and Purification. 29:(2)291-303.  Abstract
47.
Sharon M., Kessler N., Levy R., Zolla-Pazner S., Gorlach M. & Anglister J. (2003). Alternative conformations of HIV-1V3 loops mimic beta hairpins in chemokines, suggesting a mechanism for coreceptor selectivity.  Structure. 11:(2)225-236.  Abstract

2002

46.
Biron Z., Khare S., Samson A., Hayek Y., Naider F. & Anglister J. (2002). A monomeric 3(10)-helix is formed in water by a 13-residue peptide representing the neutralizing determinant of HIV-1 on gp41.  Biochemistry. 41:(42)12687-12696.  Abstract
45.
Samson A., Scherf T., Eisenstein M., Chill J. & Anglister J. (2002). The mechanism for acetylcholine receptor inhibition by alpha-neurotoxins and species-specific resistance to alpha-bungarotoxin revealed by NMR.  Neuron. 35:(2)319-332.  Abstract
44.
Nivasch R., Chill J. & Anglister J. (2002). NMR-based homology model of the interferon alpha receptor.  ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY. 223:U302-U303.  Abstract
43.
Yao Y., Wang J., Viroonchatapan N., Samson A., Chill J., Rothe E., Anglister J. & Wang Z. (2002). Yeast expression and NMR analysis of the extracellular domain of muscle nicotinic acetylcholine receptor alpha subunit.  Journal of Biological Chemistry. 277:(15)12613-12621.  Abstract
42.
Sharon M., Gorlach M., Levy R., Hayek Y. & Anglister J. (2002). Expression, purification, and isotope labeling of a gp120 V3 peptide and production of a Fab from a HIV-1 neutralizing antibody for NMR studies.  Protein Expression and Purification. 24:(3)374-383.  Abstract
41.
Chill J., Nivasch R., Levy R., Albeck S., Schreiber G. & Anglister J. (2002). The human interferon receptor: NMR-based modeling, mapping of the IFN-alpha 2 binding site, and observed ligand-induced tightening.  Biochemistry. 41:(11)3575-3585.  Abstract

2001

40.
Samson A., Chill J., Rodriguez E., Scherf T. & Anglister J. (2001). NMR mapping and secondary structure determination of the major acetylcholine receptor alpha-subunit determinant interacting with alpha-bungarotoxin.  Biochemistry. 40:(18)5464-5473.  Abstract

2000

39.
Froy O., Zilberberg N., Chejanovsky N., Anglister J., Loret E., Shaanan B., Gordon D. & Gurevitz M. (2000). Scorpion neurotoxins: structure/function relationships and application in agriculture.  Pest Management Science. 56:(5)472-474.  Abstract
38.
Tugarinov V., Zvi A., Levy R., Hayek Y., Matsushita S. & Anglister J. (2000). NMR structure of an anti-gp120 antibody complex with a V3 peptide reveals a surface important for co-receptor binding.  Structure with Folding & design. 8:(4)385-395.  Abstract
37.
Balbach J., Yang J., Weliky D., Steinbach P., Tugarinov V., Anglister J. & Tycko R. (2000). Probing hydrogen bonds in the antibody-bound HIV-1 gp120 V3 loop by solid state NMR REDOR measurements.  Journal of Biomolecular NMR. 16:(4)313-327.  Abstract
36.
Zvi A., Tugarinov V., Faiman G., Horovitz A. & Anglister J. (2000). A model of a gp120 V3 peptide in complex with an HIV-neutralizing antibody based on NMR and mutant cycle-derived constraints.  FEBS Journal. 267:(3)767-779.  Abstract
35.
Tugarinov V. & Anglister J. (2000). Solution structure of an antibody-bound HIV-1(IIIB)V3 peptide: A cis proline turn linking two beta-hairpin strands.  Journal of biomolecular structure & dynamics. 57-63.  Abstract

1999

34.
Sharon M., Oren Z., Shai Y. & Anglister J. (1999). 2D-NMR and ATR-FTIR study of the structure of a cell-selective diastereomer of melittin and its orientation in phospholipids.  Biochemistry. 38:(46)15305-15316.  Abstract
33.
Tugarinov V., Zvi A., Levy R. & Anglister J. (1999). A cis proline turn linking two beta-hairpin strands in the solution structure of an antibody-bound HIV-1(IIIB) V3 peptide.  Nature Structural Biology. 6:(4)331-335.  Abstract
32.
Weliky D., Bennett A., Zvi A., Anglister J., Steinbach P. & Tycko R. (1999). Solid-state NMR evidence for an antibody-dependent conformation of the V3 loop of HIV-1 gp120.  Nature Structural Biology. 6:(2)141-145.  Abstract
31.
Tugarinov V., Levy R., Dahan-Schokoroy A. & Anglister J. (1999). Letter to the Editor: Backbone and C-beta assignments of the anti-gp120 antibody Fv fragment complexed with an antigenic peptide.  Journal of Biomolecular NMR. 13:(2)193-194.
30.
Zvi A. & Anglister J. (1999). Application of NMR to conformational studies of an HIV peptide bound to a neutralizing antibody.  Nmr In Supramolecular Chemistry. 526:117-132.  Abstract

1998

29.
Zvi A. & Anglister J. (1998). The principal neutralizing determinant of HIV-1(IIIB): Conformation Of the peptide bound to a neutralizing antibody studied by 2D-NMR.  International Journal of Peptide Research and Therapeutics. 5:(6-May)357-364.  Abstract

1997

28.
Zvi A., Feigelson D., Hayek Y. & Anglister J. (1997). 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.  Biochemistry. 36:(28)8619-8627.  Abstract
27.
Scherf T., Balass M., Fuchs S., KatchalskiKatzir E. & Anglister J. (1997). Three-dimensional solution structure of the complex of alpha-bungarotoxin with a library-derived peptide.  Proceedings of the National Academy of Sciences of the United States of America. 94:(12)6059-6064.  Abstract
26.
Tugarinov V., Kustanovich I., Zilberberg N., Gurevitz M. & Anglister J. (1997). Solution structures of a highly insecticidal recombinant scorpion alpha-toxin and a mutant with increased activity.  Biochemistry. 36:(9)2414-2424.  Abstract

1996

25.
Faiman G., Levy R., Anglister J. & Horovitz A. (1996). Contribution of arginine residues in the RP135 peptide derived from the V3 loop of gp120 to its interaction with the Fv fragment of the 0.5 beta HIV-1 neutralizing antibody.  Journal of Biological Chemistry. 271:(23)13829-13833.  Abstract

1995

24.
Anglister J., REN H., KLEE C. & BAX A. (1995). NMR IDENTIFICATION OF CALCINEURIN-B RESIDUES AFFECTED BY BINDING OF A CALCINEURIN-A PEPTIDE.  FEBS Letters. 375:(2-Jan)108-112.  Abstract
23.
ZVI A., KUSTANOVICH I., HAYEK Y., MATSUSHITA S. & Anglister J. (1995). THE PRINCIPAL NEUTRALIZING DETERMINANT OF HIV-1 LOCATED IN V3 OF GP120 FORMS A 12-RESIDUE LOOP BY INTERNAL HYDROPHOBIC INTERACTIONS.  FEBS Letters. 368:(2)267-270.  Abstract
22.
Shoham M., Scherf T., Anglister J., LEVITT M., MERRITT E. & HOL W. (1995). STRUCTURAL DIVERSITY IN A CONSERVED CHOLERA-TOXIN EPITOPE INVOLVED IN GANGLIOSIDE BINDING.  Protein Science. 4:(5)841-848.  Abstract
21.
ZVI A., KUSTANOVICH I., FEIGELSON D., Levy R., Eisenstein M., MATSUSHITA S., RICHALETSECORDEL P., REGENMORTEL M. & Anglister J. (1995). NMR MAPPING OF THE ANTIGENIC DETERMINANT RECOGNIZED BY AN ANTI-GP120, HUMAN-IMMUNODEFICIENCY-VIRUS NEUTRALIZING ANTIBODY.  FEBS Journal. 229:(1)178-187.  Abstract
20.
Scherf T., HILLER R. & Anglister J. (1995). NMR OBSERVATION OF INTERACTIONS IN THE COMBINING SITE REGION OF AN ANTIBODY USING A SPIN-LABELED PEPTIDE ANTIGEN AND NOESY DIFFERENCE SPECTROSCOPY.  FASEB Journal. 9:(1)120-126.  Abstract
19.
Anglister J., Scherf T., ZILBER B. & Levy R. (1995). 2-DIMENSIONAL NMR-STUDIES OF THE INTERACTIONS BETWEEN A PEPTIDE OF CHOLERA-TOXIN AND MONOCLONAL-ANTIBODIES.  Biopolymers. 37:(6)383-389.  Abstract

1994

18.
Anglister J., GRZESIEK S., WANG A., REN H., KLEE C. & BAX A. (1994). H-1, C-13, N-15 NUCLEAR-MAGNETIC-RESONANCE BACKBONE ASSIGNMENTS AND SECONDARY STRUCTURE OF HUMAN CALCINEURIN-B.  Biochemistry. 33:(12)3540-3547.  Abstract

1993

17.
Anglister J., Scherf T., ZILBER B., Levy R., ZVI A., HILLER R. & FEIGELSON D. (1993). 2-DIMENSIONAL NMR INVESTIGATIONS OF THE INTERACTIONS OF ANTIBODIES WITH PEPTIDE ANTIGENS.  FASEB Journal. 7:(12)1154-1162.  Abstract
16.
Scherf T. & Anglister J. (1993). A T(1-RHO)-FILTERED 2-DIMENSIONAL TRANSFERRED NOE SPECTRUM FOR STUDYING ANTIBODY INTERACTIONS WITH PEPTIDE ANTIGENS.  Biophysical Journal. 64:(3)754-761.  Abstract

1992

15.
Scherf T., HILLER R., Naider F., LEVITT M. & Anglister J. (1992). INDUCED PEPTIDE CONFORMATIONS IN DIFFERENT ANTIBODY COMPLEXES - MOLECULAR MODELING OF THE 3-DIMENSIONAL STRUCTURE OF PEPTIDE ANTIBODY COMPLEXES USING NMR-DERIVED DISTANCE RESTRAINTS.  Biochemistry. 31:(30)6884-6897.  Abstract
14.
ZVI A., HILLER R. & Anglister J. (1992). SOLUTION CONFORMATION OF A PEPTIDE CORRESPONDING TO THE PRINCIPAL NEUTRALIZING DETERMINANT OF HIV-1(IIIB) - A 2-DIMENSIONAL NMR-STUDY.  Biochemistry. 31:(30)6972-6979.  Abstract

1991

13.
Anglister J. & Naider F. (1991). NUCLEAR-MAGNETIC-RESONANCE FOR STUDYING PEPTIDE ANTIBODY COMPLEXES BY TRANSFERRED NUCLEAR OVERHAUSER EFFECT DIFFERENCE SPECTROSCOPY.  Methods in Enzymology. 203:228-241.

1990

12.
ZILBER B., Scherf T., LEVITT M. & Anglister J. (1990). NMR-DERIVED MODEL FOR A PEPTIDE-ANTIBODY COMPLEX.  Biochemistry. 29:(43)10032-10041.
11.
Anglister J. (1990). USE OF DEUTERIUM LABELING IN NMR-STUDIES OF ANTIBODY COMBINING SITE STRUCTURE.  Quarterly Reviews of Biophysics. 23:(2)175-203.
10.
Anglister J. & ZILBER B. (1990). ANTIBODIES AGAINST A PEPTIDE OF CHOLERA-TOXIN DIFFERING IN CROSS-REACTIVITY WITH THE TOXIN DIFFER IN THEIR SPECIFIC INTERACTIONS WITH THE PEPTIDE AS OBSERVED BY H-1-NMR SPECTROSCOPY.  Biochemistry. 29:(4)921-928.

1989

9.
Levy R., ASSULIN O., Scherf T., LEVITT M. & Anglister J. (1989). PROBING ANTIBODY DIVERSITY BY 2D NMR - COMPARISON OF AMINO-ACID SEQUENCES, PREDICTED STRUCTURES, AND OBSERVED ANTIBODY ANTIGEN INTERACTIONS IN COMPLEXES OF 2 ANTIPEPTIDE ANTIBODIES.  Biochemistry. 28:(18)7168-7175.
8.
Anglister J., Levy R. & Scherf T. (1989). INTERACTIONS OF ANTIBODY AROMATIC RESIDUES WITH A PEPTIDE OF CHOLERA-TOXIN OBSERVED BY TWO-DIMENSIONAL TRANSFERRED NUCLEAR OVERHAUSER EFFECT DIFFERENCE SPECTROSCOPY.  Biochemistry. 28:(8)3360-3365.

1988

7.
FREY T., Anglister J. & MCCONNELL H. (1988). LINE-SHAPE ANALYSIS OF NMR DIFFERENCE SPECTRA OF AN ANTI-SPIN-LABEL ANTIBODY.  Biochemistry. 27:(14)5161-5165.
6.
Anglister J., JACOB C., ASSULIN O., AST G., PINKER R. & Arnon R. (1988). NMR-STUDY OF THE COMPLEXES BETWEEN A SYNTHETIC PEPTIDE DERIVED FROM THE B-SUBUNIT OF CHOLERA-TOXIN AND 3 MONOCLONAL-ANTIBODIES AGAINST IT.  Biochemistry. 27:(2)717-724.

1987

5.
Anglister J., BOND M., FREY T., LEAHY D., LEVITT M., MCCONNELL H., RULE G., TOMASELLO J. & WHITTAKER M. (1987). CONTRIBUTION OF TRYPTOPHAN RESIDUES TO THE COMBINING SITE OF A MONOCLONAL ANTI DINITROPHENYL SPIN-LABEL ANTIBODY.  Biochemistry. 26:(19)6058-6064.

1983

4.
Anglister J. & STEINBERG I. (1983). RESONANCE RAYLEIGH LIGHT-SCATTERING OF SOME PORPHYRINS IN SOLUTION - INTENSITIES AND DEPOLARIZATION RATIOS.  Chemical Physics. 75:(3)443-452.
3.
Anglister J. & STEINBERG I. (1983). RESONANCE RAYLEIGH-SCATTERING OF CYANINE DYES IN SOLUTION.  Journal of Chemical Physics. 78:(9)5358-5368.

1981

2.
Anglister J. & STEINBERG I. (1981). MEASUREMENT OF THE DEPOLARIZATION RATIO OF RAYLEIGH-SCATTERING AT ABSORPTION-BANDS.  Journal of Chemical Physics. 74:(2)786-791.

1979

1.
Anglister J. & STEINBERG I. (1979). DEPOLARIZED RAYLEIGH LIGHT-SCATTERING IN ABSORPTION-BANDS MEASURED IN LYCOPENE SOLUTION.  Chemical Physics Letters. 65:(1)50-54.