G. Shoham

4.5k total citations
123 papers, 3.7k citations indexed

About

G. Shoham is a scholar working on Molecular Biology, Biotechnology and Materials Chemistry. According to data from OpenAlex, G. Shoham has authored 123 papers receiving a total of 3.7k indexed citations (citations by other indexed papers that have themselves been cited), including 64 papers in Molecular Biology, 43 papers in Biotechnology and 32 papers in Materials Chemistry. Recurrent topics in G. Shoham's work include Enzyme Production and Characterization (43 papers), Biofuel production and bioconversion (26 papers) and Enzyme Structure and Function (25 papers). G. Shoham is often cited by papers focused on Enzyme Production and Characterization (43 papers), Biofuel production and bioconversion (26 papers) and Enzyme Structure and Function (25 papers). G. Shoham collaborates with scholars based in Israel, United States and Germany. G. Shoham's co-authors include Yuval Shoham, Mark Rozenberg, Arthur P. Grollman, Dmitry O. Zharkov, Timor Baasov, G. Golan, Gennady Zolotnitsky, Valery Belakhov, Rui Fausto and Igor Reva 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

G. Shoham

121 papers receiving 3.6k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
G. Shoham Israel 34 2.0k 1.2k 1.0k 687 583 123 3.7k
Bijan Ranjbar Iran 34 2.6k 1.3× 695 0.6× 636 0.6× 301 0.4× 777 1.3× 162 4.2k
J. Sanz‐Aparicio Spain 34 1.6k 0.8× 883 0.7× 604 0.6× 765 1.1× 341 0.6× 152 3.1k
Olga Abián Spain 34 3.3k 1.6× 443 0.4× 614 0.6× 514 0.7× 486 0.8× 129 4.5k
Antoni Planas Spain 37 2.7k 1.3× 2.0k 1.6× 1.0k 1.0× 1.5k 2.2× 297 0.5× 145 4.3k
Uwe Linne Germany 44 3.8k 1.9× 409 0.3× 499 0.5× 577 0.8× 447 0.8× 126 5.9k
S. Kamitori Japan 33 1.5k 0.7× 563 0.5× 191 0.2× 642 0.9× 602 1.0× 120 3.1k
Terese Bergfors Sweden 25 2.1k 1.1× 448 0.4× 528 0.5× 313 0.5× 547 0.9× 40 2.9k
Hak‐Sung Kim South Korea 31 3.1k 1.5× 358 0.3× 882 0.9× 253 0.4× 1.0k 1.7× 152 4.3k
Bjørn Dalhus Norway 34 2.2k 1.1× 398 0.3× 396 0.4× 300 0.4× 400 0.7× 94 3.4k
Maarten R. Egmond Netherlands 42 3.6k 1.8× 294 0.2× 336 0.3× 824 1.2× 522 0.9× 137 5.5k

Countries citing papers authored by G. Shoham

Since Specialization
Citations

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

Fields of papers citing papers by G. Shoham

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of G. Shoham

This figure shows the co-authorship network connecting the top 25 collaborators of G. Shoham. A scholar is included among the top collaborators of G. Shoham 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 G. Shoham. G. Shoham 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.
Minetti, Conceição A.S.A., David P. Remeta, Radha Bonala, et al.. (2024). Structural and mechanistic insights into the transport of aristolochic acids and their active metabolites by human serum albumin. Journal of Biological Chemistry. 300(7). 107358–107358. 7 indexed citations
2.
Lansky, Shifra, Xevi Biarnés, Dina Schneidman‐Duhovny, et al.. (2022). Integrative structure determination reveals functional global flexibility for an ultra-multimodular arabinanase. Communications Biology. 5(1). 465–465. 4 indexed citations
3.
Mousa, Reem, et al.. (2021). Diselenide crosslinks for enhanced and simplified oxidative protein folding. Communications Chemistry. 4(1). 30–30. 26 indexed citations
4.
Lansky, Shifra, et al.. (2017). Structural basis for enzyme bifunctionality – the case of Gan1D from Geobacillus stearothermophilus. FEBS Journal. 284(22). 3931–3953. 9 indexed citations
5.
Alalouf, Onit, et al.. (2011). A New Family of Carbohydrate Esterases Is Represented by a GDSL Hydrolase/Acetylxylan Esterase from Geobacillus stearothermophilus. Journal of Biological Chemistry. 286(49). 41993–42001. 51 indexed citations
6.
Libster, Dima, Paul Ben Ishai, Abraham Aserin, G. Shoham, & Nissim Garti. (2008). Molecular interactions in reverse hexagonal mesophase in the presence of Cyclosporin A. International Journal of Pharmaceutics. 367(1-2). 115–126. 30 indexed citations
7.
Almog, Orna, Ana González‐García, Marlene Mekel, et al.. (2008). The crystal structures of the psychrophilic subtilisin S41 and the mesophilic subtilisin Sph reveal the same calcium‐loaded state. Proteins Structure Function and Bioinformatics. 74(2). 489–496. 24 indexed citations
8.
Gilboa, R., et al.. (2007). Catalytic mechanism of SGAP, a double‐zinc aminopeptidase from Streptomyces griseus. FEBS Journal. 274(15). 3864–3876. 15 indexed citations
9.
Ben‐David, Alon, et al.. (2006). The Structure of an Inverting GH43 β-Xylosidase from Geobacillus stearothermophilus with its Substrate Reveals the Role of the Three Catalytic Residues. Journal of Molecular Biology. 359(1). 97–109. 127 indexed citations
10.
Golan, G., Dmitry O. Zharkov, Arthur P. Grollman, et al.. (2006). Structure of T4 Pyrimidine Dimer Glycosylase in a Reduced Imine Covalent Complex with Abasic Site-containing DNA. Journal of Molecular Biology. 362(2). 241–258. 24 indexed citations
11.
Rozenberg, Mark, G. Shoham, Igor Reva, & Rui Fausto. (2005). A correlation between the proton stretching vibration red shift and the hydrogen bond length in polycrystalline amino acids and peptides. Physical Chemistry Chemical Physics. 7(11). 2376–2376. 97 indexed citations
12.
Niefind, Karsten, et al.. (2005). Crystallization and preliminary crystallographic analysis of a family 43 β-D-xylosidase fromGeobacillus stearothermophilusT-6. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 61(12). 1054–1057. 4 indexed citations
13.
Rozenberg, Mark, Christiane Jung, & G. Shoham. (2004). Low temperature FTIR spectra and hydrogen bonds in polycrystalline cytidine. Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy. 60(10). 2369–2375. 18 indexed citations
14.
Rozenberg, Mark, Christiane Jung, & G. Shoham. (2004). Low-temperature FTIR spectra and hydrogen bonds in polycrystalline adenosine and uridine. Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy. 61(4). 733–741. 17 indexed citations
15.
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
16.
Rozenberg, Mark, G. Shoham, Igor Reva, & Rui Fausto. (2003). Low temperature FTIR spectroscopy and hydrogen bonding in cytosine polycrystals. Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy. 60(1-2). 463–470. 55 indexed citations
17.
Bravman, Tsafrir, Gennady Zolotnitsky, Smadar Shulami, et al.. (2001). Stereochemistry of family 52 glycosyl hydrolases: a β‐xylosidase from Bacillus stearothermophilus T‐6 is a retaining enzyme. FEBS Letters. 495(1-2). 39–43. 37 indexed citations
18.
Mechaly, Adva, et al.. (2000). Overproduction and characterization of seleno-methionine xylanase T-6. Journal of Biotechnology. 78(1). 83–86. 22 indexed citations
19.
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
20.
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

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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