Ze’ev Barak

2.4k total citations
69 papers, 2.0k citations indexed

About

Ze’ev Barak is a scholar working on Molecular Biology, Biochemistry and Clinical Biochemistry. According to data from OpenAlex, Ze’ev Barak has authored 69 papers receiving a total of 2.0k indexed citations (citations by other indexed papers that have themselves been cited), including 43 papers in Molecular Biology, 27 papers in Biochemistry and 19 papers in Clinical Biochemistry. Recurrent topics in Ze’ev Barak's work include Biochemical Acid Research Studies (24 papers), Metabolism and Genetic Disorders (19 papers) and Microbial Metabolic Engineering and Bioproduction (14 papers). Ze’ev Barak is often cited by papers focused on Biochemical Acid Research Studies (24 papers), Metabolism and Genetic Disorders (19 papers) and Microbial Metabolic Engineering and Bioproduction (14 papers). Ze’ev Barak collaborates with scholars based in Israel, Germany and United States. Ze’ev Barak's co-authors include David M. Chipman, Maria Vyazmensky, John V. Schloss, Yair Ben‐Dov, Stanislav Engel, Kai Tittmann, Natan Gollop, Arieh Zaritsky, Alexander Kaplun and Ariel Kushmaro and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and Journal of Molecular Biology.

In The Last Decade

Ze’ev Barak

67 papers receiving 1.9k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Ze’ev Barak Israel 28 1.3k 625 355 306 265 69 2.0k
Diana M. Downs United States 36 2.3k 1.8× 487 0.8× 739 2.1× 974 3.2× 207 0.8× 137 3.5k
Andreas Hartig Austria 29 2.8k 2.2× 255 0.4× 121 0.3× 126 0.4× 308 1.2× 65 3.1k
Bernd Laber Germany 24 1.2k 1.0× 377 0.6× 99 0.3× 570 1.9× 557 2.1× 54 2.1k
Rémi Zallot United States 19 1.2k 0.9× 134 0.2× 81 0.2× 162 0.5× 209 0.8× 26 1.6k
François Lacroute France 33 4.2k 3.2× 254 0.4× 79 0.2× 348 1.1× 1.3k 4.8× 54 4.9k
Ján A. Miernyk United States 32 2.3k 1.8× 736 1.2× 251 0.7× 141 0.5× 1.5k 5.5× 118 3.2k
Michaël Moulin United Kingdom 18 875 0.7× 74 0.1× 57 0.2× 75 0.2× 803 3.0× 19 1.5k
Marı́a C. Mansilla Argentina 21 1.0k 0.8× 221 0.4× 85 0.2× 152 0.5× 136 0.5× 33 1.4k
Marcelle Grenson Belgium 38 4.0k 3.1× 859 1.4× 104 0.3× 340 1.1× 1.2k 4.6× 58 4.7k
Sigrun Reumann Germany 31 2.7k 2.1× 640 1.0× 73 0.2× 68 0.2× 1.1k 4.2× 46 3.2k

Countries citing papers authored by Ze’ev Barak

Since Specialization
Citations

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

Fields of papers citing papers by Ze’ev Barak

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Ze’ev Barak. 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 Ze’ev Barak. The network helps show where Ze’ev Barak may publish in the future.

Co-authorship network of co-authors of Ze’ev Barak

This figure shows the co-authorship network connecting the top 25 collaborators of Ze’ev Barak. A scholar is included among the top collaborators of Ze’ev Barak 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 Ze’ev Barak. Ze’ev Barak 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.
Yehezkel, Galit, Lakkakula Satish, Ze’ev Barak, et al.. (2024). Root-secreted nucleosides: signaling chemoattractants of rhizosphere bacteria. Frontiers in Plant Science. 15. 1388384–1388384. 6 indexed citations
2.
Yehezkel, Galit, Yael Fridmann‐Sirkis, Ze’ev Barak, et al.. (2023). Blocking an epitope of misfolded SOD1 ameliorates disease phenotype in a model of amyotrophic lateral sclerosis. Brain. 146(11). 4594–4607. 4 indexed citations
3.
Engel, Daniel R., et al.. (2020). Primate differential redoxome (PDR) – A paradigm for understanding neurodegenerative diseases. Redox Biology. 36. 101683–101683. 4 indexed citations
4.
Vyazmensky, Maria, et al.. (2019). Cu/Zn-superoxide dismutase and wild-type like fALS SOD1 mutants produce cytotoxic quantities of H2O2 via cysteine-dependent redox short-circuit. Scientific Reports. 9(1). 10826–10826. 39 indexed citations
5.
6.
Barak, Ze’ev & David M. Chipman. (2011). Allosteric regulation in Acetohydroxyacid Synthases (AHASs) – Different structures and kinetic behavior in isozymes in the same organisms. Archives of Biochemistry and Biophysics. 519(2). 167–174. 24 indexed citations
7.
Kaplun, Alexander, Elad Binshtein, Maria Vyazmensky, et al.. (2008). Glyoxylate carboligase lacks the canonical active site glutamate of thiamine-dependent enzymes. Nature Chemical Biology. 4(2). 113–118. 57 indexed citations
8.
Ben‐Dov, Yair, et al.. (2007). Coral mucus-associated bacterial communities from natural and aquarium environments. FEMS Microbiology Letters. 276(1). 106–113. 108 indexed citations
9.
Kaplun, Alexander, Maria Vyazmensky, Sharon Mendel, et al.. (2006). Structure of the Regulatory Subunit of Acetohydroxyacid Synthase Isozyme III from Escherichia coli. Journal of Molecular Biology. 357(3). 951–963. 65 indexed citations
10.
Vyazmensky, Maria, Stanislav Engel, Alexander Kaplun, et al.. (2005). Acetohydroxyacid synthase isozyme I from Escherichia coli has unique catalytic and regulatory properties. Biochimica et Biophysica Acta (BBA) - General Subjects. 1760(3). 356–363. 45 indexed citations
11.
Kaplun, Alexander, Maria Vyazmensky, Stanislav Engel, et al.. (2005). Monitoring the acetohydroxy acid synthase reaction and related carboligations by circular dichroism spectroscopy. Analytical Biochemistry. 342(1). 126–133. 21 indexed citations
12.
Engel, Stanislav, Maria Vyazmensky, Ahuva Bar-Ilan, et al.. (2004). Role of a Conserved Arginine in the Mechanism of Acetohydroxyacid Synthase. Journal of Biological Chemistry. 279(23). 24803–24812. 47 indexed citations
13.
Einav, Monica, et al.. (2003). Acetohydroxyacid synthase from Mycobacterium avium and its inhibition by sulfonylureas and imidazolinones. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1649(1). 97–105. 45 indexed citations
14.
Engel, Stanislav, Maria Vyazmensky, Shimona Geresh, Ze’ev Barak, & David M. Chipman. (2003). Acetohydroxyacid synthase: A new enzyme for chiral synthesis of R‐phenylacetylcarbinol. Biotechnology and Bioengineering. 83(7). 833–840. 60 indexed citations
15.
Mendel, Sharon, et al.. (2002). The N-terminal Domain of the Regulatory Subunit is Sufficient for Complete Activation of Acetohydroxyacid Synthase III from Escherichia coli. Journal of Molecular Biology. 325(2). 275–284. 28 indexed citations
16.
Barak, Ze’ev, Dale Lindsley, & Jonathan Gallant. (1996). On the Mechanism of Leftward Frameshifting at Several Hungry Codons. Journal of Molecular Biology. 256(4). 676–684. 36 indexed citations
17.
Manasherob, Robert, Yair Ben‐Dov, Arieh Zaritsky, & Ze’ev Barak. (1994). Protozoan-Enhanced Toxicity of Bacillus thuringiensis var. israelensis δ-Endotoxin against Aedes aegypti Larvae. Journal of Invertebrate Pathology. 63(3). 244–248. 7 indexed citations
18.
Zaritsky, Arieh, et al.. (1992). Digestibility by and pathogenicity of the protozoa Tetrahymena pyriformis to larvae of Aedes aegypti. Journal of Invertebrate Pathology. 59(3). 332–334. 1 indexed citations
19.
Zaritsky, Arieh, et al.. (1991). Bioencapsulation and delivery to mosquito larvae of Bacillus thuringiensis H14 toxicity by Tetrahymena pyriformis. Journal of Invertebrate Pathology. 58(3). 455–457. 5 indexed citations
20.
Chipman, David M., et al.. (1990). Determination of products of acetohydroxy acid synthase by the colorimetric method, revisited. Analytical Biochemistry. 191(1). 96–99. 22 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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