Samuel J. Landry

3.7k total citations
72 papers, 3.0k citations indexed

About

Samuel J. Landry is a scholar working on Molecular Biology, Immunology and Materials Chemistry. According to data from OpenAlex, Samuel J. Landry has authored 72 papers receiving a total of 3.0k indexed citations (citations by other indexed papers that have themselves been cited), including 54 papers in Molecular Biology, 24 papers in Immunology and 20 papers in Materials Chemistry. Recurrent topics in Samuel J. Landry's work include Heat shock proteins research (28 papers), Protein Structure and Dynamics (23 papers) and Enzyme Structure and Function (20 papers). Samuel J. Landry is often cited by papers focused on Heat shock proteins research (28 papers), Protein Structure and Dynamics (23 papers) and Enzyme Structure and Function (20 papers). Samuel J. Landry collaborates with scholars based in United States, Switzerland and Canada. Samuel J. Landry's co-authors include Lila M. Gierasch, Costa Georgopoulos, Karol Maskos, J.F. Hunt, J. Deisenhofer, Arthur J. Weaver, Robert L. Jordan, Roger McMacken, A.J. Richardson and Olivier Fayet and has published in prestigious journals such as Nature, Proceedings of the National Academy of Sciences and Journal of Biological Chemistry.

In The Last Decade

Samuel J. Landry

70 papers receiving 2.9k citations

Peers — A (Enhanced Table)

Peers by citation overlap · career bar shows stage (early→late) cites · hero ref

Name h Career Trend Papers Cites
Samuel J. Landry United States 29 2.3k 886 638 268 174 72 3.0k
Craig M. Ogata United States 24 2.3k 1.0× 861 1.0× 465 0.7× 275 1.0× 223 1.3× 49 3.4k
Surajit Bhattacharjya Singapore 34 2.3k 1.0× 223 0.3× 738 1.2× 167 0.6× 75 0.4× 104 3.3k
Johan Kemmink Netherlands 30 2.0k 0.9× 411 0.5× 205 0.3× 563 2.1× 124 0.7× 69 2.7k
Rolf Misselwitz Germany 26 1.2k 0.5× 210 0.2× 519 0.8× 138 0.5× 191 1.1× 77 2.2k
Shang‐Te Danny Hsu Taiwan 37 3.3k 1.5× 457 0.5× 387 0.6× 267 1.0× 257 1.5× 151 4.3k
Fábio C. L. Almeida Brazil 32 1.9k 0.8× 180 0.2× 233 0.4× 145 0.5× 196 1.1× 137 2.9k
André Matagne Belgium 28 2.3k 1.0× 472 0.5× 366 0.6× 164 0.6× 274 1.6× 103 3.7k
Peter M. Hwang Canada 24 2.4k 1.1× 382 0.4× 308 0.5× 181 0.7× 279 1.6× 50 3.1k
Alla Gustchina United States 37 1.7k 0.8× 452 0.5× 465 0.7× 172 0.6× 368 2.1× 94 3.2k
Christine Schubert Wright United States 24 1.8k 0.8× 432 0.5× 446 0.7× 175 0.7× 74 0.4× 34 2.3k

Countries citing papers authored by Samuel J. Landry

Since Specialization
Citations

This map shows the geographic impact of Samuel J. Landry'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 Samuel J. Landry with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Samuel J. Landry more than expected).

Fields of papers citing papers by Samuel J. Landry

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Samuel J. Landry. 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 Samuel J. Landry. The network helps show where Samuel J. Landry may publish in the future.

Co-authorship network of co-authors of Samuel J. Landry

This figure shows the co-authorship network connecting the top 25 collaborators of Samuel J. Landry. A scholar is included among the top collaborators of Samuel J. Landry based on the total number of citations received by their joint publications. Widths of edges represent the number of papers authors have co-authored together. Node borders signify the number of papers an author published with Samuel J. Landry. Samuel J. Landry is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

20 of 20 papers shown
1.
Wu, Eric, et al.. (2024). pH-Responsive Peptide Nanoparticles Deliver Macromolecules to Cells via Endosomal Membrane Nanoporation. ACS Nano. 18(50). 33922–33936. 2 indexed citations
2.
Landry, Samuel J., et al.. (2024). GPU Acceleration for Markov Chain Monte Carlo Sampling. 1–8.
3.
Park, Hee‐Won, et al.. (2019). Deimmunizing substitutions in Pseudomonas exotoxin domain III perturb antigen processing without eliminating T-cell epitopes. Journal of Biological Chemistry. 294(12). 4667–4681. 19 indexed citations
4.
Landry, Samuel J., et al.. (2017). Structural Basis for CD4+ T Cell Epitope Dominance in Arbo-Flavivirus Envelope Proteins: A Meta-Analysis. Viral Immunology. 30(7). 479–489. 7 indexed citations
5.
Mayer, Matthias P., et al.. (2017). The Hsp40 J‐domain modulates Hsp70 conformation and ATPase activity with a semi‐elliptical spring. Protein Science. 26(9). 1838–1851. 19 indexed citations
6.
Robinson, James E., et al.. (2010). Influence of Disulfide-Stabilized Structure on the Specificity of Helper T-Cell and Antibody Responses to HIV Envelope Glycoprotein gp120. Journal of Virology. 84(7). 3303–3311. 18 indexed citations
7.
Li, Hualin, Chong‐Feng Xu, Steven P. Blais, et al.. (2009). Proximal Glycans Outside of the Epitopes Regulate the Presentation of HIV-1 Envelope gp120 Helper Epitopes. The Journal of Immunology. 182(10). 6369–6378. 37 indexed citations
8.
Landry, Samuel J., et al.. (2008). Three dimensional structure directs T-cell epitope dominance associated with allergy. Clinical and Molecular Allergy. 6(1). 9–9. 9 indexed citations
9.
Curiel, Tyler J., Cindy Morris, Michael J. Brumlik, et al.. (2004). Peptides Identified through Phage Display Direct Immunogenic Antigen to Dendritic Cells. The Journal of Immunology. 172(12). 7425–7431. 84 indexed citations
10.
Shewmaker, Frank, Michael J. Kerner, Manajit Hayer‐Hartl, et al.. (2004). A mobile loop order–disorder transition modulates the speed of chaperonin cycling. Protein Science. 13(8). 2139–2148. 16 indexed citations
11.
Kleen, Thomas O., Robert Asaad, Samuel J. Landry, Bernhard O. Boehm, & Magdalena Tary‐Lehmann. (2004). Tc1 effector diversity shows dissociated expression of granzyme B and interferon-γ in HIV infection. AIDS. 18(3). 383–392. 29 indexed citations
12.
Dai, Guixiang, et al.. (2002). Structural Basis for Helper T-cell and Antibody Epitope Immunodominance in Bacteriophage T4 Hsp10. Journal of Biological Chemistry. 277(1). 161–168. 35 indexed citations
13.
Shewmaker, Frank, Karol Maskos, Carlos Simmerling, & Samuel J. Landry. (2001). The Disordered Mobile Loop of GroES Folds into a Defined β-Hairpin upon Binding GroEL. Journal of Biological Chemistry. 276(33). 31257–31264. 31 indexed citations
14.
Landry, Samuel J.. (2000). Helper T-cell Epitope Immunodominance Associated with Structurally Stable Segments of Hen Egg Lysozyme and HIV gp120. Journal of Theoretical Biology. 203(3). 189–201. 20 indexed citations
15.
Landry, Samuel J., et al.. (2000). Domain-specific spectroscopy of 5-hydroxytryptophan-containing variants of Escherichia coli DnaJ. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1480(1-2). 267–277. 1 indexed citations
16.
Maskos, Karol, et al.. (1998). Role of the J-domain in the cooperation of Hsp40 with Hsp70. Proceedings of the National Academy of Sciences. 95(11). 6108–6113. 231 indexed citations
17.
Richardson, A.J., Samuel J. Landry, & Costa Georgopoulos. (1998). The ins and outs of a molecular chaperone machine. Trends in Biochemical Sciences. 23(4). 138–143. 92 indexed citations
18.
Landry, Samuel J. & Lila M. Gierasch. (1994). Polypeptide Interactions with Molecular Chaperones and their Relationship to In Vivo Protein Folding. Annual Review of Biophysics and Biomolecular Structure. 23(1). 645–669. 73 indexed citations
19.
Landry, Samuel J. & Lila M. Gierasch. (1991). The chaperonin GroEL binds a polypeptide in an .alpha.-helical conformation. Biochemistry. 30(30). 7359–7362. 150 indexed citations
20.
Politzer, Peter, et al.. (1982). Proposed procedure for using electrostatic potentials to predict and interpret nucleophilic processes. The Journal of Physical Chemistry. 86(24). 4767–4771. 65 indexed citations

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.

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