Elisha Haas

2.8k total citations
70 papers, 2.4k citations indexed

About

Elisha Haas is a scholar working on Molecular Biology, Materials Chemistry and Cell Biology. According to data from OpenAlex, Elisha Haas has authored 70 papers receiving a total of 2.4k indexed citations (citations by other indexed papers that have themselves been cited), including 59 papers in Molecular Biology, 19 papers in Materials Chemistry and 12 papers in Cell Biology. Recurrent topics in Elisha Haas's work include Protein Structure and Dynamics (28 papers), Enzyme Structure and Function (19 papers) and Spectroscopy and Quantum Chemical Studies (8 papers). Elisha Haas is often cited by papers focused on Protein Structure and Dynamics (28 papers), Enzyme Structure and Function (19 papers) and Spectroscopy and Quantum Chemical Studies (8 papers). Elisha Haas collaborates with scholars based in Israel, United States and Germany. Elisha Haas's co-authors include Izchak Z. Steinberg, Ephraim Katchalski‐Katzir, Dan Amir, Varda Ittah, Harold A. Scheraga, Michael A. Sinev, Vladimir Ratner, Elena V. Sineva, David Gottfried and Ernst Otto Fischer and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and PLoS ONE.

In The Last Decade

Elisha Haas

70 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
Elisha Haas Israel 28 1.9k 757 337 332 232 70 2.4k
G. Krishnamoorthy India 27 2.3k 1.2× 428 0.6× 337 1.0× 279 0.8× 249 1.1× 96 2.9k
Hironari Kamikubo Japan 29 1.7k 0.9× 782 1.0× 320 0.9× 114 0.3× 324 1.4× 101 2.8k
Yelena V. Grinkova United States 28 2.9k 1.6× 525 0.7× 325 1.0× 109 0.3× 516 2.2× 42 4.6k
Rudolf Gilmanshin United States 17 2.6k 1.4× 1.2k 1.6× 427 1.3× 123 0.4× 469 2.0× 26 3.5k
Hagen Hofmann Switzerland 23 2.5k 1.3× 1.1k 1.5× 451 1.3× 428 1.3× 305 1.3× 44 3.0k
Nam Ki Lee South Korea 26 1.8k 1.0× 287 0.4× 333 1.0× 865 2.6× 141 0.6× 59 3.0k
Alessandro Borgia Switzerland 21 2.1k 1.1× 805 1.1× 470 1.4× 295 0.9× 217 0.9× 27 2.5k
Margaret S. Cheung United States 29 2.8k 1.5× 1.5k 2.0× 581 1.7× 131 0.4× 234 1.0× 100 3.6k
Ananya Majumdar United States 36 3.0k 1.6× 462 0.6× 194 0.6× 171 0.5× 554 2.4× 121 3.5k
Kathleen G. Valentine United States 29 1.8k 1.0× 619 0.8× 265 0.8× 155 0.5× 633 2.7× 57 2.5k

Countries citing papers authored by Elisha Haas

Since Specialization
Citations

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

Fields of papers citing papers by Elisha Haas

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Elisha Haas. 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 Elisha Haas. The network helps show where Elisha Haas may publish in the future.

Co-authorship network of co-authors of Elisha Haas

This figure shows the co-authorship network connecting the top 25 collaborators of Elisha Haas. A scholar is included among the top collaborators of Elisha Haas 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 Elisha Haas. Elisha Haas 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.
Woodard, Jaie, Kinshuk Raj Srivastava, Grzegorz Nawrocki, et al.. (2018). Intramolecular Diffusion in α-Synuclein: It Depends on How You Measure It. Biophysical Journal. 115(7). 1190–1199. 11 indexed citations
2.
Klement, Reinhard, et al.. (2016). Molecular Dynamics Simulations of Alpha-Synuclein Ensemble FRET Measurements from Different Force Fields. Biophysical Journal. 110(3). 551a–551a. 1 indexed citations
3.
Rahimipour, Shai, et al.. (2015). Resolution of Two Sub-Populations of Conformers and Their Individual Dynamics by Time Resolved Ensemble Level FRET Measurements. PLoS ONE. 10(12). e0143732–e0143732. 12 indexed citations
4.
Orevi, Tomer, et al.. (2013). The loop hypothesis: contribution of early formed specific non-local interactions to the determination of protein folding pathways. Biophysical Reviews. 5(2). 85–98. 16 indexed citations
5.
Haas, Elisha. (2012). Ensemble FRET Methods in Studies of Intrinsically Disordered Proteins. Methods in molecular biology. 895. 467–498. 20 indexed citations
6.
Orevi, Tomer, et al.. (2012). Fast Subdomain Folding Prior to the Global Refolding Transition of E. coli Adenylate Kinase: A Double Kinetics Study. Journal of Molecular Biology. 423(4). 613–623. 18 indexed citations
7.
Orevi, Tomer, et al.. (2011). Early Closure of Loops in the Refolding of Adenylate Kinase: A Possible Key Role for Non Local Interactions in the Initial Folding Steps. Biophysical Journal. 100(3). 211a–211a. 19 indexed citations
8.
9.
Ulman, Abraham, et al.. (2011). Highly active engineered-enzyme oriented monolayers: formation, characterization and sensing applications. Journal of Nanobiotechnology. 9(1). 26–26. 15 indexed citations
10.
Haas, Elisha, et al.. (2011). Time-Resolved FRET Detection of Subtle Temperature-Induced Conformational Biases in Ensembles of α-Synuclein Molecules. Journal of Molecular Biology. 411(1). 234–247. 20 indexed citations
11.
Haas, Elisha, et al.. (2010). Segmental Conformational Disorder and Dynamics in the Intrinsically Disordered Protein α-Synuclein and Its Chain Length Dependence. Journal of Molecular Biology. 405(5). 1267–1283. 57 indexed citations
12.
Orevi, Tomer, et al.. (2008). Early Closure of a Long Loop in the Refolding of Adenylate Kinase: A Possible Key Role of Non-Local Interactions in the Initial Folding Steps. Journal of Molecular Biology. 385(4). 1230–1242. 25 indexed citations
13.
Phillips, Nelson B., et al.. (2006). SRY and Human Sex Determination: The Basic Tail of the HMG Box Functions as a Kinetic Clamp to Augment DNA Bending. Journal of Molecular Biology. 358(1). 172–192. 33 indexed citations
14.
Ittah, Varda, Edith Kahana, Dan Amir, & Elisha Haas. (2004). Applications of time‐resolved resonance energy transfer measurements in studies of the molecular crowding effect. Journal of Molecular Recognition. 17(5). 448–455. 8 indexed citations
15.
Gakamsky, Dmitry M., Daniel M. Davis, Elisha Haas, Jack L. Strominger, & Israel Pecht. (1999). Photophysical Analysis of Class I Major Histocompatibility Complex Protein Assembly Using a Xanthene-Derivatized β2-Microglobulin. Biophysical Journal. 76(3). 1552–1560. 10 indexed citations
16.
Gakamsky, Dmitry M., et al.. (1995). Selective steady-state and time-resolved fluorescence spectroscopy of an HLA-A2-peptide complex. Immunology Letters. 44(2-3). 195–201. 9 indexed citations
17.
Ittah, Varda & Elisha Haas. (1995). Nonlocal Interactions Stabilize Long Range Loops in the Initial Folding Intermediates of Reduced Bovine Pancreatic Trypsin Inhibitor. Biochemistry. 34(13). 4493–4506. 68 indexed citations
18.
19.
Gakamsky, Dmitry M., Gilad Haran, Elisha Haas, et al.. (1994). Picosecond fluorescence spectroscopy of a single-chain class I major histocompatibility complex encoded protein in its peptide loaded and unloaded states. Immunology Letters. 40(2). 125–132. 6 indexed citations
20.
Malkin, Shmuel, et al.. (1976). A novel short‐lived emission from the photosynthetic bacterium Rhodospirilum rubrum. FEBS Letters. 63(2). 299–303. 1 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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