Wayne A. Hendrickson
Impact in
- Virology top 0.05%
- HIV Research and Treatment
- Immunology top 0.1%
- Immune Cell Function and Interaction
Papers in
-
- Protein Structure and Dynamics 78
- RNA and protein synthesis mechanisms 24
- Glycosylation and Glycoproteins Research 21
-
- Enzyme Structure and Function 98
- Co-authors
- Peter D. Kwong (23 shared papers)Joseph Sodroski (20 shared papers)Richard T. Wyatt (12 shared papers)Raymond W. Sweet (11 shared papers)James E. Robinson (6 shared papers)William I. Weis (4 shared papers)Kurt Drickamer (4 shared papers)Stevan R. Hubbard (4 shared papers)
- Journals
- Proceedings of the National Academy of Sciences (33 papers)Structure (22 papers)Nature (20 papers)Journal of Biological Chemistry (19 papers)Science (19 papers)
- Partner nations
- United StatesGermanyFrance
In The Last Decade
Wayne A. Hendrickson
313 papers receiving 33.2k citations
Wayne A. Hendrickson's Hit Papers
Peers
Comparison fields: 5 of 186
- Virology 6.2k
- Immunology 6.4k
- Molecular Biology 20.7k
- Cell Biology 4.1k
- Structural Biology 316
Countries citing papers authored by Wayne A. Hendrickson
This map shows the geographic impact of Wayne A. Hendrickson's research. It shows the number of citations coming from papers published by authors working in each country. You can also color the map by specialization and compare the number of citations received by Wayne A. Hendrickson with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Wayne A. Hendrickson more than expected).
Fields of papers citing papers by Wayne A. Hendrickson
This network shows the impact of papers produced by Wayne A. Hendrickson. Nodes represent research fields, and links connect fields that are likely to share authors. Colored nodes show fields that tend to cite the papers produced by Wayne A. Hendrickson. The network helps show where Wayne A. Hendrickson may publish in the future.
Co-authors
The 25 scholars most cited alongside Wayne A. Hendrickson, linked wherever they have co-authored with each other. Click a name or a connecting line to browse the papers they share.
All Works
Showing the 20 most-cited of 319 papers — load more, or switch the sort, to bring in the rest.
| # | Work | ||
|---|---|---|---|
| 1 | Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody Hit paper breakdown → | 1998 | 2398 |
| 2 | Structural Analysis of Substrate Binding by the Molecular Chaperone DnaK Hit paper breakdown → | 1996 | 1056 |
| 3 | The antigenic structure of the HIV gp120 envelope glycoprotein Hit paper breakdown → | 1998 | 1019 |
| 4 | Structural basis of cell-cell adhesion by cadherins Hit paper breakdown → | 1995 | 1007 |
| 5 | Determination of Macromolecular Structures from Anomalous Diffraction of Synchrotron Radiation Hit paper breakdown → | 1991 | 994 |
| 6 | Crystal structure of the tyrosine kinase domain of the human insulin receptor Hit paper breakdown → | 1994 | 922 |
| 7 | Selenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD): a vehicle for direct determination of three‐dimensional structure. Hit paper breakdown → | 1990 | 884 |
| 8 | Structure of a C-type mannose-binding protein complexed with an oligosaccharide Hit paper breakdown → | 1992 | 787 |
| 9 | A Conserved HIV gp120 Glycoprotein Structure Involved in Chemokine Receptor Binding Hit paper breakdown → | 1998 | 691 |
| 10 | Stereochemically restrained refinement of macromolecular structures Hit paper breakdown → | 1985 | 577 |
| 11 | Structure of the hydrophobic protein crambin determined directly from the anomalous scattering of sulphur Hit paper breakdown → | 1981 | 559 |
| 12 | Crystal structure of core streptavidin determined from multiwavelength anomalous diffraction of synchrotron radiation. Hit paper breakdown → | 1989 | 523 |
| 13 | Structure of the Calcium-Dependent Lectin Domain from a Rat Mannose-Binding Protein Determined by MAD Phasing Hit paper breakdown → | 1991 | 507 |
| 14 | Crystal structure of an HIV-binding recombinant fragment of human CD4 Hit paper breakdown → | 1990 | 488 |
| 15 | 2005 | 485 | |
| 16 | 1993 | 462 | |
| 17 | 1992 | 459 | |
| 18 | 1990 | 442 | |
| 19 | 1984 | 437 | |
| 20 | 2002 | 427 |
About Wayne A. Hendrickson
Wayne A. Hendrickson is a scholar working on Molecular Biology, Materials Chemistry, Cell Biology, Virology and Radiology, Nuclear Medicine and Imaging, having authored 319 papers that have together received 34.4k indexed citations. Recurring topics across this work include Enzyme Structure and Function (98 papers), Protein Structure and Dynamics (78 papers), HIV Research and Treatment (36 papers), Hemoglobin structure and function (34 papers), Monoclonal and Polyclonal Antibodies Research (32 papers), RNA and protein synthesis mechanisms (24 papers), Glycosylation and Glycoproteins Research (21 papers) and Immune Cell Function and Interaction (20 papers). The work is most often cited by research in Virology (6.2k citations), Immunology (6.4k citations), Molecular Biology (20.7k citations), Cell Biology (4.1k citations) and Structural Biology (316 citations). Wayne A. Hendrickson has collaborated with scholars based in United States, Germany and France. Frequent co-authors include Peter D. Kwong, Joseph Sodroski, Richard T. Wyatt, Raymond W. Sweet, James E. Robinson, William I. Weis, Kurt Drickamer, Stevan R. Hubbard, Lei Wei and Craig M. Ogata. Their work appears in journals such as Proceedings of the National Academy of Sciences, Structure, Nature, Journal of Biological Chemistry and Science.
Rankless uses publication and citation data sourced from OpenAlex, an open and comprehensive bibliographic database. While OpenAlex provides broad and valuable coverage of the global research landscape, it—like all bibliographic datasets—has inherent limitations. These include incomplete records, variations in author disambiguation, differences in journal indexing, and delays in data updates. As a result, some metrics and network relationships displayed in Rankless may not fully capture the entirety of a scholar's output or impact.