Martin Sax

1.8k total citations
35 papers, 1.4k citations indexed

About

Martin Sax is a scholar working on Molecular Biology, Biochemistry and Neurology. According to data from OpenAlex, Martin Sax has authored 35 papers receiving a total of 1.4k indexed citations (citations by other indexed papers that have themselves been cited), including 14 papers in Molecular Biology, 12 papers in Biochemistry and 11 papers in Neurology. Recurrent topics in Martin Sax's work include Biochemical Acid Research Studies (11 papers), Metabolism and Genetic Disorders (8 papers) and Alcoholism and Thiamine Deficiency (8 papers). Martin Sax is often cited by papers focused on Biochemical Acid Research Studies (11 papers), Metabolism and Genetic Disorders (8 papers) and Alcoholism and Thiamine Deficiency (8 papers). Martin Sax collaborates with scholars based in United States, Italy and Netherlands. Martin Sax's co-authors include William Furey, J. Pletcher, S. Swaminathan, Subramanyam Swaminathan, Frank Jordan, Krishnamoorthy Chandrasekhar, Natalia S. Nemeria, Palaniappa Arjunan, Gary Blank and Andrew P. J. Brunskill and has published in prestigious journals such as Nature, Science and Journal of the American Chemical Society.

In The Last Decade

Martin Sax

34 papers receiving 1.3k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Martin Sax United States 17 526 490 424 326 236 35 1.4k
Heidi Erlandsen United States 23 212 0.4× 15 0.0× 1.4k 3.4× 940 2.9× 154 0.7× 39 2.0k
S. E. Ealick United States 12 105 0.2× 64 0.1× 617 1.5× 73 0.2× 10 0.0× 27 808
N.R. Silvaggi United States 20 64 0.1× 203 0.4× 557 1.3× 10 0.0× 53 0.2× 37 1.2k
Vishal Agrawal United States 22 51 0.1× 23 0.0× 872 2.1× 123 0.4× 45 0.2× 45 1.6k
Eliezer Rapaport United States 25 71 0.1× 15 0.0× 1.3k 3.0× 35 0.1× 62 0.3× 51 1.9k
Michael Cardamone Australia 14 33 0.1× 53 0.1× 479 1.1× 83 0.3× 28 0.1× 40 1.0k
Dan Yin United States 18 68 0.1× 20 0.0× 740 1.7× 36 0.1× 27 0.1× 27 1.0k
Linda F. Epstein United States 15 59 0.1× 20 0.0× 518 1.2× 37 0.1× 111 0.5× 23 1.2k
Silvia Ronchi Italy 20 186 0.4× 12 0.0× 536 1.3× 80 0.2× 23 0.1× 62 938
Olivér Ozohanics Hungary 20 79 0.2× 19 0.0× 658 1.6× 69 0.2× 93 0.4× 45 874

Countries citing papers authored by Martin Sax

Since Specialization
Citations

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

Fields of papers citing papers by Martin Sax

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Martin Sax

This figure shows the co-authorship network connecting the top 25 collaborators of Martin Sax. A scholar is included among the top collaborators of Martin Sax 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 Martin Sax. Martin Sax 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.
Chandrasekhar, Krishnamoorthy, Junjie Wang, Palaniappa Arjunan, et al.. (2013). Insight to the Interaction of the Dihydrolipoamide Acetyltransferase (E2) Core with the Peripheral Components in the Escherichia coli Pyruvate Dehydrogenase Complex via Multifaceted Structural Approaches. Journal of Biological Chemistry. 288(21). 15402–15417. 43 indexed citations
2.
Kumaran, D., Subramaniam Eswaramoorthy, William Furey, et al.. (2008). Domain Organization in Clostridium botulinum Neurotoxin Type E Is Unique: Its Implication in Faster Translocation. Journal of Molecular Biology. 386(1). 233–245. 136 indexed citations
3.
4.
Chandrasekhar, Krishnamoorthy, Palaniappa Arjunan, Martin Sax, et al.. (2006). Active-site changes in the pyruvate dehydrogenase multienzyme complex E1 apoenzyme component fromEscherichia coliobserved at 2.32 Å resolution. Acta Crystallographica Section D Biological Crystallography. 62(11). 1382–1386. 12 indexed citations
5.
Arjunan, Palaniappa, Krishnamoorthy Chandrasekhar, Martin Sax, et al.. (2004). Structural Determinants of Enzyme Binding Affinity:  The E1 Component of Pyruvate Dehydrogenase from Escherichia coli in Complex with the Inhibitor Thiamin Thiazolone Diphosphate,. Biochemistry. 43(9). 2405–2411. 39 indexed citations
6.
Arjunan, Palaniappa, Natalia S. Nemeria, Andrew P. J. Brunskill, et al.. (2002). Structure of the Pyruvate Dehydrogenase Multienzyme Complex E1 Component fromEscherichia coliat 1.85 Å Resolution,. Biochemistry. 41(16). 5213–5221. 113 indexed citations
7.
Umland, Timothy C., Lavinia M. Wingert, S. Swaminathan, James J. Schmidt, & Martin Sax. (1998). Crystallization and preliminary X-ray analysis of tetanus neurotoxin C fragment. Acta Crystallographica Section D Biological Crystallography. 54(2). 273–275. 9 indexed citations
8.
Lebeda, Frank J., Timothy C. Umland, Martin Sax, & Mark A. Olson. (1998). Accuracy of Secondary Structure and Solvent Accessibility Predictions for a Clostridial Neurotoxin C-Fragment. Journal of Protein Chemistry. 17(4). 311–318. 4 indexed citations
9.
Swaminathan, S., William Furey, J. Pletcher, & Martin Sax. (1995). Residues defining Vβ specificity in staphylococcal enterotoxins. Nature Structural Biology. 2(8). 680–686. 51 indexed citations
10.
Umland, Timothy C., S. Swaminathan, Gurmukh Singh, et al.. (1994). Structure of a human Clara cell phospholipid-binding protein–ligand complex at 1. 9 Å resolution. Nature Structural Biology. 1(8). 538–545. 61 indexed citations
11.
Dyda, Fred, et al.. (1993). Catalytic centers in the thiamin diphosphate dependent enzyme pyruvate decarboxylase at 2.4-.ANG. resolution. Biochemistry. 32(24). 6165–6170. 174 indexed citations
12.
Umland, Timothy C., S. Swaminathan, William Furey, et al.. (1992). Refined structure of rat Clara cell 17 kDa protein at 3·0 Å resolution. Journal of Molecular Biology. 224(2). 441–448. 38 indexed citations
13.
Swaminathan, S., William Furey, J. Pletcher, & Martin Sax. (1992). Crystal structure of staphylococcal enterotoxin B, a superantigen. Nature. 359(6398). 801–806. 245 indexed citations
14.
15.
Sax, Martin, et al.. (1990). Free-solution isoelectric focusing for the purification of Staphylococcus aureus enterotoxin C1. Protein Expression and Purification. 1(2). 97–103. 1 indexed citations
16.
Rose, John P., et al.. (1988). Crystals of modified bovine neurophysin II. European Journal of Biochemistry. 174(1). 145–147. 6 indexed citations
17.
Shin, Whanchul, J. Pletcher, & Martin Sax. (1979). Stereochemistry of intermediates in thiamin catalysis. 3. Crystal structure of DL-2-(.alpha.-hydroxybenzyl)oxythiamin chloride hydrochloride trihydrate, an inhibitor adduct. Journal of the American Chemical Society. 101(15). 4365–4371. 18 indexed citations
18.
Wang, Bi‐Cheng, et al.. (1979). Crystals of a bovine neurophysin II-dipeptide amide complex. Journal of Molecular Biology. 127(2). 241–242. 11 indexed citations
19.
Tait, A. Martin, et al.. (1975). Crystal and molecular structure of bis(8-amino-2-methylquinoline)nitratonickel(II) nitrate. Journal of the Chemical Society Dalton Transactions. 2494–2494. 1 indexed citations
20.
Sax, Sylvan M, et al.. (1963). A Study of Malignolipin Picrate. Journal of Biological Chemistry. 238(11). 3817–3819. 4 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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