World's Best Scientists 2026 revealed!

D-Index & Metrics

Biology and Biochemistry

D-Index
49
Citations
14352
World Ranking
17849
National Ranking
7306

Research.com Recognitions

  • Member of the European Molecular Biology Organization (EMBO)
  • Member of the European Molecular Biology Organization (EMBO)
  • Member of the European Molecular Biology Organization (EMBO)

Overview

Roberto J. Poljak was affiliated with the University of Maryland, College Park in the United States. Their academic career was marked by contributions that aligned with molecular biology and related fields.

Poljak's recognition included membership in the European Molecular Biology Organization (EMBO), reflecting involvement in a broader scientific community dedicated to molecular biology.

Their documented research activities did not include recent published papers, co-authors, or detailed records of publication venues and topics. Specific fields and subfields of study associated with their work were also not listed.

No recorded book publications or detailed records of main topics of work were available for Poljak.

The scholar is deceased. Their professional contributions remain documented primarily through institutional association and acknowledgment by EMBO, positioning them within the landscape of molecular biology research during their active years.

Best Publications

  • Conformations of immunoglobulin hypervariable regions.

    Cyrus Chothia;Cyrus Chothia;Arthur M. Lesk;Anna Tramontano;Michael Levitt;Michael Levitt

  • Three-dimensional structure of an antigen-antibody complex at 2.8 A resolution

    A. G. Amit;R. A. Mariuzza;S. E. V. Phillips;R. J. Poljak

  • Three-Dimensional Structure of Immunoglobulins

    L M Amzel;R J Poljak

  • Bound water molecules and conformational stabilization help mediate an antigen-antibody association.

    T N Bhat;G A Bentley;G Boulot;M I Greene

  • Three-Dimensional Structure of the Fab′ Fragment of a Human Immunoglobulin at 2.8-Å Resolution

    R. J. Poljak;L. M. Amzel;H. P. Avey;B. L. Chen

  • Three-dimensional structure of antibodies.

    P M Alzari;M B Lascombe;R J Poljak

  • The structural basis of antigen-antibody recognition.

    R. A. Mariuzza;S. E. V. Phillips;R. J. Poljak

  • The three dimensional structure of a combining region-ligand complex of immunoglobulin NEW at 3.5-A resolution.

    L. M. Amzel;R. J. Poljak;F. Saul;J. M. Varga

  • Small rearrangements in structures of Fv and Fab fragments of antibody D1.3 on antigen binding.

    T. N. Bhat;G. A. Bentley;T. O. Fischmann;G. Boulot

  • Preliminary refinement and structural analysis of the Fab fragment from human immunoglobulin new at 2.0 A resolution.

    F A Saul;L M Amzel;R J Poljak

  • Three-dimensional structure of an antigen-antibody complex at 6 A resolution.

    A. G. Amit;R. A. Mariuzza;S. E. V. Phillips;R. J. Poljak

  • Production and structure of diabodies

    Roberto J Poljak

  • Three-dimensional structure of an idiotope-anti-idiotope complex.

    G. A. Bentley;G. Boulot;M. M. Riottot;R. J. Poljak

  • The Three-Dimensional Structure of the Fab′ Fragment of a Human Myeloma Immunoglobulin at 2.0-Å Resolution

    R. J. Poljak;L. M. Amzel;B. L. Chen;R. P. Phizackerley

  • Structural features of the reactions between antibodies and protein antigens.

    Bradford C. Braden;Roberto J. Poljak

  • The predicted structure of immunoglobulin D1.3 and its comparison with the crystal structure

    Cyrus Chothia;Cyrus Chothia;Arthur M. Lesk;Arthur M. Lesk;Michael Levitt;Adolfo G. Amit

  • The three-dimensional structure of the aspartyl protease from the HIV-1 isolate BRU.

    S Spinelli;Q Z Liu;P M Alzari;P H Hirel

  • Crystallographic refinement of the three-dimensional structure of the FabD1.3-lysozyme complex at 2.5-A resolution.

    T. O. Fischmann;G. A. Bentley;T. N. Bhat;G. Boulot

  • Molecular basis of antigen mimicry by an anti-idiotope

    Fields Ba;Goldbaum Fa;Ysern X;Ysern X;Poljak Rj

  • Three-dimensional structures of the free and the antigen-complexed Fab from monoclonal anti-lysozyme antibody D44.1.

    B.C Braden;H Souchon;J.L Eisele;G.A Bentley

Frequent Co-Authors

Roy A. Mariuzza
Roy A. Mariuzza University of Maryland, College Park
Pedro M. Alzari
Pedro M. Alzari Institut Pasteur
Simon E. V. Phillips
Simon E. V. Phillips University of Oxford
Alfred Nisonoff
Alfred Nisonoff Brandeis University
Silvia Spinelli
Silvia Spinelli Centre national de la recherche scientifique, CNRS
Cyrus Chothia
Cyrus Chothia MRC Laboratory of Molecular Biology
Michael Levitt
Michael Levitt Stanford University
Pierre Béguin
Pierre Béguin Institut Pasteur
Arthur M. Lesk
Arthur M. Lesk Pennsylvania State University
Mark I. Greene
Mark I. Greene University of Pennsylvania

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