2022 - Research.com Best Female Scientist Award
2007 - Fellow of the American Association for the Advancement of Science (AAAS)
2001 - Member of the National Academy of Sciences
1997 - Fellow of the American Academy of Arts and Sciences
1996 - AAI-BD Biosciences Investigator Award, American Association of Immunologists
Pamela J. Bjorkman mostly deals with Antibody, Virology, Binding site, Immunology and Major histocompatibility complex. Her work carried out in the field of Antibody brings together such families of science as Ic50 values and Betacoronavirus. Her studies in Virology integrate themes in fields like Epitope and Immunization.
Her Binding site research is multidisciplinary, incorporating perspectives in Antigen, Stereochemistry, Histocompatibility, Protein structure and Peptide. Her Major histocompatibility complex study integrates concerns from other disciplines, such as Receptor and Cell biology. Her study in Receptor is interdisciplinary in nature, drawing from both Immunoglobulin G, Plasma protein binding and Molecular biology.
Pamela J. Bjorkman spends much of her time researching Antibody, Virology, Binding site, Neutralization and Epitope. Pamela J. Bjorkman interconnects Virus, Molecular biology, Immune system and Antigen in the investigation of issues within Antibody. Her work deals with themes such as T cell and T-cell receptor, which intersect with Antigen.
Her Virology study incorporates themes from Immunization, Monoclonal antibody, Glycoprotein and Severe acute respiratory syndrome coronavirus 2. Her Binding site research incorporates elements of Protein structure, Receptor, Biophysics and Stereochemistry. Her work carried out in the field of Neutralization brings together such families of science as Titer, Potency and Avidity.
Pamela J. Bjorkman focuses on Antibody, Virology, Epitope, Neutralization and Virus. The study incorporates disciplines such as Heterologous, Binding site and Antigen in addition to Antibody. Her Binding site research is multidisciplinary, incorporating perspectives in Biophysics and Trimer.
Her Virology research includes themes of Immunization, Immune system, Monoclonal antibody and Severe acute respiratory syndrome coronavirus 2. Pamela J. Bjorkman has researched Epitope in several fields, including Lipid bilayer fusion, Polyclonal antibodies and Glycan. Her Neutralization research is multidisciplinary, incorporating elements of Mutation, Titer, Avidity, Paratope and Coronavirus.
Her scientific interests lie mostly in Antibody, Virology, Epitope, Neutralization and Antigen. Her studies link Immune system with Antibody. Pamela J. Bjorkman interconnects Serology, Betacoronavirus, Glycoprotein and Polyclonal antibodies in the investigation of issues within Virology.
Her Neutralization research includes elements of Mutation, Titer, Immunization and Avidity. As part of the same scientific family, Pamela J. Bjorkman usually focuses on Antigen, concentrating on Immunity and intersecting with Somatic hypermutation and Coronavirus. Neutralizing antibody connects with themes related to Binding site in her study.
This overview was generated by a machine learning system which analysed the scientist’s body of work. If you have any feedback, you can contact us here.
Structure of the human class I histocompatibility antigen, HLA-A2.
P. J. Bjorkman;P. J. Bjorkman;M. A. Saper;B. Samraoui;W. S. Bennett;W. S. Bennett.
T-cell antigen receptor genes and T-cell recognition.
Mark M. Davis;Pamela J. Bjorkman.
The foreign antigen binding site and T cell recognition regions of class I histocompatibility antigens
P. J. Bjorkman;P. J. Bjorkman;P. J. Bjorkman;M. A. Saper;B. Samraoui;W. S. Bennett;W. S. Bennett.
A hypothetical model of the foreign antigen binding site of class II histocompatibility molecules.
Jerry H. Brown;Theodore Jardetzky;Mark A. Saper;Boudjema Samraoui.
Refined structure of the human histocompatibility antigen HLA-A2 at 2.6 Å resolution☆
M.A. Saper;P.J. Bjorkman;D.C. Wiley.
Journal of Molecular Biology (1991)
Convergent antibody responses to SARS-CoV-2 in convalescent individuals.
Davide F. Robbiani;Davide F. Robbiani;Christian Gaebler;Frauke Muecksch;Julio C.C. Lorenzi.
Sequence and structural convergence of broad and potent HIV antibodies that mimic CD4 binding.
Johannes F. Scheid;Hugo Mouquet;Beatrix Ueberheide;Ron Diskin.
Structure, Function, and Diversity of Class I Major Histocompatibility Complex Molecules
Pamela J. Bjorkman;Peter Parham.
Annual Review of Biochemistry (1990)
The hemochromatosis gene product complexes with the transferrin receptor and lowers its affinity for ligand binding
John N. Feder;David M. Penny;Alivelu Irrinki;Vince K. Lee.
Proceedings of the National Academy of Sciences of the United States of America (1998)
Specificity pockets for the side chains of peptide antigens in HLA-Aw68
T. P. J. Garrett;M. A. Saper;P. J. Bjorkman;P. J. Bjorkman;J. L. Strominger.
If you think any of the details on this page are incorrect, let us know.
We appreciate your kind effort to assist us to improve this page, it would be helpful providing us with as much detail as possible in the text box below: