Jeff Abramson

6.8k total citations · 1 hit paper
65 papers, 5.1k citations indexed

About

Jeff Abramson is a scholar working on Molecular Biology, Spectroscopy and Materials Chemistry. According to data from OpenAlex, Jeff Abramson has authored 65 papers receiving a total of 5.1k indexed citations (citations by other indexed papers that have themselves been cited), including 57 papers in Molecular Biology, 10 papers in Spectroscopy and 10 papers in Materials Chemistry. Recurrent topics in Jeff Abramson's work include Mitochondrial Function and Pathology (18 papers), Ion channel regulation and function (11 papers) and Enzyme Structure and Function (9 papers). Jeff Abramson is often cited by papers focused on Mitochondrial Function and Pathology (18 papers), Ion channel regulation and function (11 papers) and Enzyme Structure and Function (9 papers). Jeff Abramson collaborates with scholars based in United States, Sweden and India. Jeff Abramson's co-authors include So Iwata, H. Ronald Kaback, И. Н. Смирнова, G. Verner, Vladimir N. Kasho, Ernest M. Wright, Duilio Cascio, Gisela Larsson, Margareta Svensson-Ek and Rachna Ujwal and has published in prestigious journals such as Nature, Science and Proceedings of the National Academy of Sciences.

In The Last Decade

Jeff Abramson

65 papers receiving 5.1k citations

Hit Papers

align trajectories sort by overperformance

What are hit papers?

Hit papers significantly outperform the citation benchmark for their cohort. A paper qualifies if it has ≥500 total citations, achieves ≥1.5× the top-1% citation threshold for papers in the same subfield and year (this is the minimum needed to enter the top 1%, not the average within it), or reaches the top citation threshold in at least one of its specific research topics.

Structure and Mechanism of the Lactose Permease of Escherichia coli

2003 1.1k citations Jeff Abramson, И. Н. Смирнова et al. Science profile →

Author Peers

Peers are selected by citation overlap in the author's most active subfields. citations · hero ref

Author						Papers	Cites
Jeff Abramson	4.0k	950	562	482	446	65	5.1k
Matthias Quick	2.5k 0.6×	1.1k 1.2×	388 0.7×	466 1.0×	265 0.6×	85	3.8k
Carola Hunte	5.6k 1.4×	502 0.5×	432 0.8×	247 0.5×	444 1.0×	94	6.8k
Olga Boudker	2.3k 0.6×	1.3k 1.3×	273 0.5×	477 1.0×	396 0.9×	43	3.4k
Robert R. Rando	6.5k 1.6×	1.3k 1.4×	397 0.7×	416 0.9×	662 1.5×	199	8.0k
Judit Ovádi	3.6k 0.9×	476 0.5×	248 0.4×	365 0.8×	452 1.0×	150	5.5k
Ferdinand Hucho	4.4k 1.1×	1.3k 1.3×	332 0.6×	164 0.3×	268 0.6×	180	6.0k
И. Н. Смирнова	2.2k 0.5×	262 0.3×	736 1.3×	532 1.1×	614 1.4×	91	3.1k
Leonard M. Hjelmeland	3.4k 0.8×	553 0.6×	267 0.5×	313 0.6×	186 0.4×	97	5.5k
Kenneth Neet	3.0k 0.7×	1.1k 1.2×	193 0.3×	251 0.5×	588 1.3×	114	4.4k
Jens Peter Andersen	5.8k 1.4×	516 0.5×	388 0.7×	419 0.9×	214 0.5×	150	6.9k

Countries citing papers authored by Jeff Abramson

Since Specialization

Citations

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

Fields of papers citing papers by Jeff Abramson

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Jeff Abramson

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

All Works

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20 of 20 papers shown

Elgeti, Matthias, Aviv Paz, Thorsten Althoff, et al.. (2023). Membrane potential accelerates sugar uptake by stabilizing the outward facing conformation of the Na/glucose symporter vSGLT. Nature Communications. 14(1). 7511–7511. 8 indexed citations

Ngo, Van A., María Queralt-Martín, Lucie Bergdoll, et al.. (2022). The Single Residue K12 Governs the Exceptional Voltage Sensitivity of Mitochondrial Voltage-Dependent Anion Channel Gating. Journal of the American Chemical Society. 144(32). 14564–14577. 7 indexed citations

Besterman, Aaron D., Thorsten Althoff, Peter Elfferich, et al.. (2021). Functional and structural analyses of novel Smith-Kingsmore Syndrome-Associated MTOR variants reveal potential new mechanisms and predictors of pathogenicity. PLoS Genetics. 17(7). e1009651–e1009651. 9 indexed citations

Martynowycz, Michael W., et al.. (2020). MicroED structure of lipid-embedded mammalian mitochondrial voltage-dependent anion channel. Proceedings of the National Academy of Sciences. 117(51). 32380–32385. 29 indexed citations

Queralt-Martín, María, Lucie Bergdoll, Oscar Teijido, et al.. (2020). A lower affinity to cytosolic proteins reveals VDAC3 isoform-specific role in mitochondrial biology. The Journal of General Physiology. 152(2). 46 indexed citations

Queralt-Martín, María, Lucie Bergdoll, Jeff Abramson, et al.. (2019). Human VDAC3 Forms VDAC1-Type Anionic Channels that are High-Conducting, Permeable to Metabolites, and Regulated by Cytosolic Proteins. Biophysical Journal. 116(3). 155a–155a. 1 indexed citations

Paz, Aviv, Derek P. Claxton, Kelli Kazmier, et al.. (2018). Conformational transitions of the sodium-dependent sugar transporter, vSGLT. Proceedings of the National Academy of Sciences. 115(12). E2742–E2751. 31 indexed citations

Queralt-Martín, María, Lucie Bergdoll, Daniel Jacobs, et al.. (2018). Assessing the role of residue E73 and lipid headgroup charge in VDAC1 voltage gating. Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1860(1). 22–29. 31 indexed citations

Hoogerheide, David P., Sergei Y. Noskov, Daniel Jacobs, et al.. (2017). Structural features and lipid binding domain of tubulin on biomimetic mitochondrial membranes. Proceedings of the National Academy of Sciences. 114(18). E3622–E3631. 34 indexed citations

10.

Bisignano, Paola, Chakrapani Kalyanaraman, Chiara E. Ghezzi, et al.. (2017). Structural Insights into Sodium-Dependent Sugar Transporters and their Inhibition Mechanism. Biophysical Journal. 112(3). 128a–128a. 2 indexed citations

11.

Choudhary, Om Prakash, Aviv Paz, Joshua L. Adelman, et al.. (2014). Characterizing ATP Permeation through the Voltage-Dependent Anion Channel VDAC. Biophysical Journal. 106(2). 147a–148a. 1 indexed citations

12.

Srikanth, Sonal, et al.. (2012). Junctate is a Ca ² ⁺ -sensing structural component of Orai1 and stromal interaction molecule 1 (STIM1). Proceedings of the National Academy of Sciences. 109(22). 8682–8687. 95 indexed citations

13.

Choudhary, Om Prakash, Joshua L. Adelman, Jeff Abramson, & Michael Grabe. (2012). Characterizing ATP Permeation through mVDAC1 using Markov State Models (MSMs). Biophysical Journal. 102(3). 550a–550a. 2 indexed citations

14.

Choe, Seungho, John M. Rosenberg, Jeff Abramson, Ernest M. Wright, & Michael Grabe. (2011). Water Permeation Through the Sodium-Dependent Galactose Cotransporter VSGLT. Biophysical Journal. 100(3). 248a–248a. 1 indexed citations

15.

Choudhary, Om Prakash, et al.. (2010). The Electrostatics of VDAC: Implications in Selectivity and Gating. Biophysical Journal. 98(3). 53a–53a. 1 indexed citations

16.

Ujwal, Rachna, Duilio Cascio, Jacques‐Philippe Colletier, et al.. (2008). The crystal structure of mouse VDAC1 at 2.3 Å resolution reveals mechanistic insights into metabolite gating. Proceedings of the National Academy of Sciences. 105(46). 17742–17747. 449 indexed citations

17.

Faham, Salem, Akira Watanabe, Duilio Cascio, et al.. (2008). The Crystal Structure of a Sodium Galactose Transporter Reveals Mechanistic Insights into Na ⁺ /Sugar Symport. Science. 321(5890). 810–814. 420 indexed citations

18.

Abramson, Jeff, И. Н. Смирнова, Vladimir N. Kasho, et al.. (2003). Structure and Mechanism of the Lactose Permease of Escherichia coli. Science. 301(5633). 610–615. 1138 indexed citations breakdown →

19.

Jormakka, Mika, Susanna Törnroth‐Horsefield, Jeff Abramson, Bernadette Byrne, & So Iwata. (2001). Purification and crystallization of the respiratory complex formate dehydrogenase-N fromEscherichia coli. Acta Crystallographica Section D Biological Crystallography. 58(1). 160–162. 29 indexed citations

20.

Iwata, So, Mårten Wikström, Jeff Abramson, et al.. (2000). The structure of the ubiquinol oxidase from Escherichia coli and its ubiquinone binding site.. Nature Structural Biology. 7(10). 910–917. 322 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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