Linda Spremulli

5.9k total citations
147 papers, 4.7k citations indexed

About

Linda Spremulli is a scholar working on Molecular Biology, Clinical Biochemistry and Genetics. According to data from OpenAlex, Linda Spremulli has authored 147 papers receiving a total of 4.7k indexed citations (citations by other indexed papers that have themselves been cited), including 140 papers in Molecular Biology, 7 papers in Clinical Biochemistry and 7 papers in Genetics. Recurrent topics in Linda Spremulli's work include RNA and protein synthesis mechanisms (106 papers), RNA modifications and cancer (65 papers) and Mitochondrial Function and Pathology (42 papers). Linda Spremulli is often cited by papers focused on RNA and protein synthesis mechanisms (106 papers), RNA modifications and cancer (65 papers) and Mitochondrial Function and Pathology (42 papers). Linda Spremulli collaborates with scholars based in United States, Japan and India. Linda Spremulli's co-authors include Emine C. Koc, Brooke E. Christian, William Burkhart, Arthur Moseley, Kevin Blackburn, Md. Emdadul Haque, Rajendra K. Agrawal, David W. Russell, Manjuli R. Sharma and Caryl Schwartzbach and has published in prestigious journals such as Cell, Proceedings of the National Academy of Sciences and Nucleic Acids Research.

In The Last Decade

Linda Spremulli

141 papers receiving 4.6k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Linda Spremulli United States 39 4.4k 449 361 199 160 147 4.7k
Laurie S. Kaguni United States 36 3.3k 0.8× 913 2.0× 479 1.3× 158 0.8× 150 0.9× 97 3.8k
Joachim Rassow Germany 38 3.8k 0.9× 521 1.2× 201 0.6× 153 0.8× 224 1.4× 92 4.4k
Catherine Florentz France 41 5.2k 1.2× 401 0.9× 395 1.1× 475 2.4× 51 0.3× 94 5.5k
François Strauss France 23 1.9k 0.4× 122 0.3× 342 0.9× 314 1.6× 71 0.4× 35 2.3k
Piotr P. Stępień Poland 28 2.2k 0.5× 156 0.3× 175 0.5× 250 1.3× 113 0.7× 78 2.6k
Kaye N. Truscott Australia 31 3.8k 0.9× 745 1.7× 235 0.7× 79 0.4× 207 1.3× 50 4.1k
Dmitry Temiakov United States 25 2.2k 0.5× 349 0.8× 374 1.0× 53 0.3× 80 0.5× 42 2.4k
Ernest W. Johns United Kingdom 30 2.4k 0.5× 428 1.0× 359 1.0× 157 0.8× 70 0.4× 44 3.0k
Carolyn K. Suzuki United States 26 2.6k 0.6× 259 0.6× 265 0.7× 100 0.5× 221 1.4× 52 3.2k
Edgar C. Henshaw United States 33 2.8k 0.6× 116 0.3× 348 1.0× 139 0.7× 120 0.8× 55 3.6k

Countries citing papers authored by Linda Spremulli

Since Specialization
Citations

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

Fields of papers citing papers by Linda Spremulli

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Linda Spremulli

This figure shows the co-authorship network connecting the top 25 collaborators of Linda Spremulli. A scholar is included among the top collaborators of Linda Spremulli 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 Linda Spremulli. Linda Spremulli 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.
2.
Koripella, Ravi Kiran, Manjuli R. Sharma, Kalpana Bhargava, et al.. (2020). Structures of the human mitochondrial ribosome bound to EF-G1 reveal distinct features of mitochondrial translation elongation. Nature Communications. 11(1). 3830–3830. 36 indexed citations
3.
Kaushal, P.S., Manjuli R. Sharma, T.M. Booth, et al.. (2014). Cryo-EM structure of the small subunit of the mammalian mitochondrial ribosome. Proceedings of the National Academy of Sciences. 111(20). 7284–7289. 55 indexed citations
4.
Nallagatla, Subba Rao, Saikat Ghosh, Suresh D. Sharma, et al.. (2013). Native Tertiary Structure and Nucleoside Modifications Suppress tRNA’s Intrinsic Ability to Activate the Innate Immune Sensor PKR. PLoS ONE. 8(3). e57905–e57905. 27 indexed citations
5.
Yassin, Aymen S., Md. Emdadul Haque, Partha P. Datta, et al.. (2011). Insertion domain within mammalian mitochondrial translation initiation factor 2 serves the role of eubacterial initiation factor 1. Proceedings of the National Academy of Sciences. 108(10). 3918–3923. 46 indexed citations
6.
Christian, Brooke E., et al.. (2010). Analysis of the functional consequences of lethal mutations in mitochondrial translational elongation factors. Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease. 1802(7-8). 692–698. 9 indexed citations
7.
Haque, Md. Emdadul, et al.. (2010). Properties of the C-terminal Tail of Human Mitochondrial Inner Membrane Protein Oxa1L and Its Interactions with Mammalian Mitochondrial Ribosomes. Journal of Biological Chemistry. 285(36). 28353–28362. 40 indexed citations
8.
Wilkinson, Kevin A., et al.. (2008). Lack of secondary structure characterizes the 5′ ends of mammalian mitochondrial mRNAs. RNA. 14(5). 862–871. 47 indexed citations
9.
Datta, Partha P., et al.. (2008). A Single Mammalian Mitochondrial Translation Initiation Factor Functionally Replaces Two Bacterial Factors. Molecular Cell. 29(2). 180–190. 78 indexed citations
10.
Jeppesen, Mads Gravers, Tomáš Navrátil, Linda Spremulli, & Jens Nyborg. (2004). Crystal Structure of the Bovine Mitochondrial Elongation Factor Tu·Ts Complex. Journal of Biological Chemistry. 280(6). 5071–5081. 39 indexed citations
11.
Sharma, Manjuli R., Emine C. Koc, Partha P. Datta, et al.. (2003). Structure of the Mammalian Mitochondrial Ribosome Reveals an Expanded Functional Role for Its Component Proteins. Cell. 115(1). 97–108. 269 indexed citations
12.
Koc, Emine C., William Burkhart, Kevin Blackburn, et al.. (2001). The Large Subunit of the Mammalian Mitochondrial Ribosome. Journal of Biological Chemistry. 276(47). 43958–43969. 214 indexed citations
13.
Zhang, Yuelin, et al.. (1998). Mutational Analysis of the Roles of Residues in Escherichia coli Elongation Factor Ts in the Interaction with Elongation Factor Tu. Journal of Biological Chemistry. 273(8). 4556–4562. 34 indexed citations
14.
Zhang, Yuelin, et al.. (1997). Role of Domains in Escherichia coli and Mammalian Mitochondrial Elongation Factor Ts in the Interaction with Elongation Factor Tu. Journal of Biological Chemistry. 272(35). 21956–21963. 21 indexed citations
15.
Spremulli, Linda, et al.. (1991). Chloroplast translational initiation factor 3. Purification and characterization of multiple forms from Euglena gracilis.. Journal of Biological Chemistry. 266(26). 17079–17083. 7 indexed citations
16.
17.
Erion, Jack L., et al.. (1980). Euglena gracilis chloroplast EF-Ts. Evidence that it is a nuclear-coded gene product.. Journal of Biological Chemistry. 255(13). 6018–6019. 35 indexed citations
18.
Spremulli, Linda, Ben J. Walthall, S R Lax, & Joanne M. Ravel. (1979). Partial purification of the factors required for the initiation of protein synthesis in wheat germ.. Journal of Biological Chemistry. 254(1). 143–148. 28 indexed citations
19.
Russell, David W. & Linda Spremulli. (1979). Purification and characterization of a ribosome dissociation factor (eukaryotic initiation factor 6) from wheat germ.. Journal of Biological Chemistry. 254(18). 8796–8800. 73 indexed citations
20.
Brown, Betty A., et al.. (1977). Repression of the tyrosine, lysine, and methionine biosynthetic pathways in a hisT mutant of Salmonella typhimurium. Journal of Bacteriology. 129(2). 1168–1170. 7 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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