Farah Javid-Majd

446 total citations
10 papers, 382 citations indexed

About

Farah Javid-Majd is a scholar working on Molecular Biology, Biochemistry and Materials Chemistry. According to data from OpenAlex, Farah Javid-Majd has authored 10 papers receiving a total of 382 indexed citations (citations by other indexed papers that have themselves been cited), including 8 papers in Molecular Biology, 5 papers in Biochemistry and 4 papers in Materials Chemistry. Recurrent topics in Farah Javid-Majd's work include Biochemical and Molecular Research (7 papers), Amino Acid Enzymes and Metabolism (4 papers) and Enzyme Structure and Function (4 papers). Farah Javid-Majd is often cited by papers focused on Biochemical and Molecular Research (7 papers), Amino Acid Enzymes and Metabolism (4 papers) and Enzyme Structure and Function (4 papers). Farah Javid-Majd collaborates with scholars based in United States and New Zealand. Farah Javid-Majd's co-authors include John S. Blanchard, Subray S. Hegde, Steven L. Roderick, M.W. Vetting, Frank M. Raushel, Michelle Stapleton, Leisha S. Mullins, Brent A. Hanks, Catherine E. Goodfellow and Edward N. Baker and has published in prestigious journals such as Journal of Biological Chemistry, Journal of Molecular Biology and Biochemistry.

In The Last Decade

Farah Javid-Majd

10 papers receiving 378 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Farah Javid-Majd United States 8 304 118 86 56 42 10 382
Hookang Im South Korea 11 281 0.9× 119 1.0× 65 0.8× 33 0.6× 41 1.0× 17 449
Heinrich Delbrück Germany 12 280 0.9× 90 0.8× 50 0.6× 172 3.1× 52 1.2× 14 508
Genevieve L. Evans New Zealand 13 367 1.2× 132 1.1× 97 1.1× 84 1.5× 53 1.3× 23 506
Sook‐Kyung Kim South Korea 13 317 1.0× 45 0.4× 43 0.5× 31 0.6× 34 0.8× 32 513
Mark Mabanglo Canada 13 399 1.3× 71 0.6× 57 0.7× 24 0.4× 23 0.5× 19 558
Philip C. Bourne United States 11 272 0.9× 97 0.8× 63 0.7× 40 0.7× 18 0.4× 21 381
Leonardo Astolfi Rosado Brazil 16 366 1.2× 68 0.6× 93 1.1× 14 0.3× 57 1.4× 27 482
Enea Salsi United States 12 451 1.5× 87 0.7× 42 0.5× 12 0.2× 58 1.4× 14 537
Kimberly D. Grimes United States 8 224 0.7× 37 0.3× 48 0.6× 30 0.5× 29 0.7× 9 354
Ellene H. Mashalidis United States 10 380 1.3× 49 0.4× 85 1.0× 70 1.3× 60 1.4× 13 531

Countries citing papers authored by Farah Javid-Majd

Since Specialization
Citations

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

Fields of papers citing papers by Farah Javid-Majd

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Farah Javid-Majd. 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 Farah Javid-Majd. The network helps show where Farah Javid-Majd may publish in the future.

Co-authorship network of co-authors of Farah Javid-Majd

This figure shows the co-authorship network connecting the top 25 collaborators of Farah Javid-Majd. A scholar is included among the top collaborators of Farah Javid-Majd 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 Farah Javid-Majd. Farah Javid-Majd is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

10 of 10 papers shown
1.
Javid-Majd, Farah, et al.. (2008). The 1.25 Å resolution structure of phosphoribosyl-ATP pyrophosphohydrolase fromMycobacterium tuberculosis. Acta Crystallographica Section D Biological Crystallography. 64(6). 627–635. 14 indexed citations
2.
Goodfellow, Catherine E., et al.. (2005). The Crystal Structure of TrpD, a Metabolic Enzyme Essential for Lung Colonization by Mycobacterium tuberculosis, in Complex with its Substrate Phosphoribosylpyrophosphate. Journal of Molecular Biology. 355(4). 784–797. 41 indexed citations
3.
Ye, Sheng, et al.. (2005). Kinetic and Structural Characterization of Phosphofructokinase from Lactobacillus bulgaricus. Biochemistry. 44(46). 15280–15286. 15 indexed citations
4.
Pierrat, Olivier A., Farah Javid-Majd, & Frank M. Raushel. (2002). Dissection of the Conduit for Allosteric Control of Carbamoyl Phosphate Synthetase by Ornithine. Archives of Biochemistry and Biophysics. 400(1). 26–33. 6 indexed citations
5.
Vetting, M.W., Subray S. Hegde, Farah Javid-Majd, John S. Blanchard, & Steven L. Roderick. (2002). Aminoglycoside 2′-N-acetyltransferase from Mycobacterium tuberculosis in complex with coenzyme A and aminoglycoside substrates. Nature Structural Biology. 9(9). 653–658. 115 indexed citations
6.
Hegde, Subray S., Farah Javid-Majd, & John S. Blanchard. (2001). Overexpression and Mechanistic Analysis of Chromosomally Encoded Aminoglycoside 2′-N-Acetyltransferase (AAC(2′)-Ic) fromMycobacterium tuberculosis. Journal of Biological Chemistry. 276(49). 45876–45881. 61 indexed citations
7.
Javid-Majd, Farah, Leisha S. Mullins, Frank M. Raushel, & Michelle Stapleton. (2000). The Differentially Conserved Residues of Carbamoyl-Phosphate Synthetase. Journal of Biological Chemistry. 275(7). 5073–5080. 5 indexed citations
8.
Javid-Majd, Farah & John S. Blanchard. (2000). Mechanistic Analysis of the argE-Encoded N-Acetylornithine Deacetylase. Biochemistry. 39(6). 1285–1293. 47 indexed citations
9.
10.
Stapleton, Michelle, et al.. (1996). Role of Conserved Residues within the Carboxy Phosphate Domain of Carbamoyl Phosphate Synthetase. Biochemistry. 35(45). 14352–14361. 48 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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