Harry M. Greenblatt

2.8k total citations
46 papers, 2.3k citations indexed

About

Harry M. Greenblatt is a scholar working on Molecular Biology, Pharmacology and Computational Theory and Mathematics. According to data from OpenAlex, Harry M. Greenblatt has authored 46 papers receiving a total of 2.3k indexed citations (citations by other indexed papers that have themselves been cited), including 26 papers in Molecular Biology, 18 papers in Pharmacology and 16 papers in Computational Theory and Mathematics. Recurrent topics in Harry M. Greenblatt's work include Cholinesterase and Neurodegenerative Diseases (17 papers), Computational Drug Discovery Methods (16 papers) and Peptidase Inhibition and Analysis (9 papers). Harry M. Greenblatt is often cited by papers focused on Cholinesterase and Neurodegenerative Diseases (17 papers), Computational Drug Discovery Methods (16 papers) and Peptidase Inhibition and Analysis (9 papers). Harry M. Greenblatt collaborates with scholars based in Israel, United States and Germany. Harry M. Greenblatt's co-authors include Joel L. Sussman, Israel Silman, Gitay Kryger, T. Lewis, G. Shoham, Yaakov Levy, Hay Dvir, Yuan‐Ping Pang, Paul R. Carlier and Dawn M. Wong and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and Nucleic Acids Research.

In The Last Decade

Harry M. Greenblatt

46 papers receiving 2.3k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Harry M. Greenblatt Israel 26 1.1k 1.1k 748 707 352 46 2.3k
Francesco Ortuso Italy 43 1.4k 1.2× 2.0k 1.9× 672 0.9× 2.2k 3.2× 153 0.4× 144 4.8k
Gitay Kryger Israel 13 1.5k 1.3× 1.0k 0.9× 1.0k 1.4× 799 1.1× 437 1.2× 16 2.6k
J. Love United States 14 963 0.8× 1.0k 0.9× 726 1.0× 537 0.8× 257 0.7× 16 2.1k
Caterina Fattorusso Italy 33 566 0.5× 1.3k 1.2× 442 0.6× 1.0k 1.5× 132 0.4× 94 2.8k
Lilly Toker Israel 13 2.3k 2.0× 1.5k 1.4× 1.3k 1.7× 1.1k 1.5× 960 2.7× 19 4.0k
Alessandra Bisi Italy 33 1.6k 1.4× 990 0.9× 1.0k 1.3× 1.5k 2.2× 181 0.5× 120 3.3k
Adriana Bolasco Italy 40 1.1k 1.0× 822 0.8× 339 0.5× 2.4k 3.4× 133 0.4× 62 3.5k
Jia‐Heng Tan China 41 552 0.5× 4.3k 3.9× 283 0.4× 1.1k 1.5× 144 0.4× 146 5.4k
Giulio Poli Italy 27 424 0.4× 1.2k 1.1× 478 0.6× 518 0.7× 115 0.3× 98 2.0k
Li Di United States 13 613 0.5× 767 0.7× 533 0.7× 490 0.7× 65 0.2× 18 2.0k

Countries citing papers authored by Harry M. Greenblatt

Since Specialization
Citations

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

Fields of papers citing papers by Harry M. Greenblatt

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Harry M. Greenblatt. 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 Harry M. Greenblatt. The network helps show where Harry M. Greenblatt may publish in the future.

Co-authorship network of co-authors of Harry M. Greenblatt

This figure shows the co-authorship network connecting the top 25 collaborators of Harry M. Greenblatt. A scholar is included among the top collaborators of Harry M. Greenblatt 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 Harry M. Greenblatt. Harry M. Greenblatt 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.
Kozell, Anna, Alexey V. Solomonov, Irit Rosenhek‐Goldian, et al.. (2024). Sound-mediated nucleation and growth of amyloid fibrils. Proceedings of the National Academy of Sciences. 121(34). e2315510121–e2315510121. 2 indexed citations
2.
Wang, Xi, Lavi S. Bigman, Harry M. Greenblatt, et al.. (2023). Negatively charged, intrinsically disordered regions can accelerate target search by DNA-binding proteins. Nucleic Acids Research. 51(10). 4701–4712. 35 indexed citations
3.
Wang, Xi, Harry M. Greenblatt, Lavi S. Bigman, et al.. (2021). Dynamic Autoinhibition of the HMGB1 Protein via Electrostatic Fuzzy Interactions of Intrinsically Disordered Regions. Journal of Molecular Biology. 433(18). 167122–167122. 30 indexed citations
4.
Bigman, Lavi S., Harry M. Greenblatt, & Yaakov Levy. (2021). What Are the Molecular Requirements for Protein Sliding along DNA?. The Journal of Physical Chemistry B. 125(12). 3119–3131. 16 indexed citations
5.
Pal, Arumay, Harry M. Greenblatt, & Yaakov Levy. (2020). Prerecognition Diffusion Mechanism of Human DNA Mismatch Repair Proteins along DNA: Msh2-Msh3 versus Msh2-Msh6. Biochemistry. 59(51). 4822–4832. 9 indexed citations
6.
Katz, Michael, et al.. (2019). Variations in Core Packing of GP2 from Old World Mammarenaviruses in their Post-Fusion Conformations Affect Membrane-Fusion Efficiencies. Journal of Molecular Biology. 431(11). 2095–2111. 11 indexed citations
7.
Xu, Yechun, Minjun Li, Harry M. Greenblatt, et al.. (2011). Flexibility of the flap in the active site of BACE1 as revealed by crystal structures and molecular dynamics simulations. Acta Crystallographica Section D Biological Crystallography. 68(1). 13–25. 86 indexed citations
8.
Peleg, Yoav, Tamar Unger, Shira Albeck, et al.. (2008). Crystal structure of YagE, a putative DHDPS‐like protein from Escherichia coli K12. Proteins Structure Function and Bioinformatics. 71(4). 2102–2108. 4 indexed citations
9.
Vitu, Elvira, Einav Gross, Harry M. Greenblatt, et al.. (2008). Yeast Mpd1p Reveals the Structural Diversity of the Protein Disulfide Isomerase Family. Journal of Molecular Biology. 384(3). 631–640. 16 indexed citations
10.
Colletier, Jacques‐Philippe, Didier Fournier, Harry M. Greenblatt, et al.. (2006). Structural insights into substrate traffic and inhibition in acetylcholinesterase. The EMBO Journal. 25(12). 2746–2756. 167 indexed citations
11.
Almog, Orna, et al.. (2003). The 0.93Å Crystal Structure of Sphericase: A Calcium-loaded Serine Protease from Bacillus sphaericus. Journal of Molecular Biology. 332(5). 1071–1082. 31 indexed citations
12.
Greenblatt, Harry M., Israel Silman, & Joel L. Sussman. (2000). Structural studies on vertebrate and invertebrate acetylcholinesterases and their complexes with functional ligands. Drug Development Research. 50(3-4). 573–583. 10 indexed citations
13.
Gilboa, R., Harry M. Greenblatt, A. Spungin‐Bialik, et al.. (2000). Interactions ofStreptomyces griseusaminopeptidase with a methionine product analogue: a structural study at 1.53 Å resolution. Acta Crystallographica Section D Biological Crystallography. 56(5). 551–558. 32 indexed citations
14.
Silman, Israel, Charles B. Millard, Arie Ordentlich, et al.. (1999). A preliminary comparison of structural models for catalytic intermediates of acetylcholinesterase. Chemico-Biological Interactions. 119-120. 43–52. 27 indexed citations
15.
Greenblatt, Harry M., Gitay Kryger, T. Lewis, Israel Silman, & Joel L. Sussman. (1999). Structure of acetylcholinesterase complexed with (−)‐galanthamine at 2.3 Å resolution. FEBS Letters. 463(3). 321–326. 259 indexed citations
16.
Bon, Suzanne, Harry M. Greenblatt, Daniel Van Belle, et al.. (1999). Effect of Mutations within the Peripheral Anionic Site on the Stability of Acetylcholinesterase. Molecular Pharmacology. 55(6). 982–992. 1 indexed citations
17.
Greenblatt, Harry M., H. Feinberg, Paul A. Tucker, & G. Shoham. (1998). Carboxypeptidase A: Native, Zinc-Removed and Mercury-Replaced Forms. Acta Crystallographica Section D Biological Crystallography. 54(3). 289–305. 13 indexed citations
18.
Maras, Bruno, Harry M. Greenblatt, G. Shoham, et al.. (1996). Aminopeptidase from Streptomyces griseus. European Journal of Biochemistry. 236(3). 843–846. 41 indexed citations
19.
Almog, Orna, et al.. (1993). Crystallization and Preliminary Crystallographic Analysis of Streptomyces griseus Aminopeptidase. Journal of Molecular Biology. 230(1). 342–344. 16 indexed citations
20.
Greenblatt, Harry M., Clarence A. Ryan, & M. N. G. James. (1989). Structure of the complex of Streptomyces griseus proteinase B and polypeptide chymotrypsin inhibitor-1 from Russet Burbank potato tubers at 2.1 Å resolution. Journal of Molecular Biology. 205(1). 201–228. 68 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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