Tom Alber

16.8k total citations · 2 hit papers
131 papers, 13.1k citations indexed

About

Tom Alber is a scholar working on Molecular Biology, Materials Chemistry and Infectious Diseases. According to data from OpenAlex, Tom Alber has authored 131 papers receiving a total of 13.1k indexed citations (citations by other indexed papers that have themselves been cited), including 110 papers in Molecular Biology, 47 papers in Materials Chemistry and 19 papers in Infectious Diseases. Recurrent topics in Tom Alber's work include Enzyme Structure and Function (47 papers), Protein Structure and Dynamics (37 papers) and RNA and protein synthesis mechanisms (36 papers). Tom Alber is often cited by papers focused on Enzyme Structure and Function (47 papers), Protein Structure and Dynamics (37 papers) and RNA and protein synthesis mechanisms (36 papers). Tom Alber collaborates with scholars based in United States, United Kingdom and Switzerland. Tom Alber's co-authors include Peter S. Kim, Pehr B. Harbury, Erin K. O’Shea, Tao Zhang, Juli D. Klemm, James M. Holton, Derek N. Woolfson, James S. Fraser, Ho Leung Ng and Nathaniel Echols and has published in prestigious journals such as Nature, Science and Proceedings of the National Academy of Sciences.

In The Last Decade

Tom Alber

131 papers receiving 12.9k citations

Hit Papers

A Switch Between Two-, Th... 1991 2026 2002 2014 1993 1991 400 800 1.2k

Author Peers

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

Author Last Decade Papers Cites
Tom Alber 10.3k 3.0k 1.4k 1.2k 1.2k 131 13.1k
D.A. Keedy 11.3k 1.1× 3.2k 1.1× 1.3k 0.9× 1.2k 0.9× 1.6k 1.3× 46 16.0k
E.A. Merritt 8.3k 0.8× 2.6k 0.9× 801 0.6× 1.1k 0.8× 1.2k 1.0× 96 12.1k
Laura W. Murray 8.4k 0.8× 2.2k 0.7× 971 0.7× 934 0.8× 1.3k 1.1× 10 11.7k
Elizabeth Potterton 8.9k 0.9× 3.3k 1.1× 970 0.7× 989 0.8× 1.3k 1.1× 8 12.5k
Eugene Krissinel 10.7k 1.0× 4.1k 1.3× 1.1k 0.8× 1.1k 0.9× 1.6k 1.3× 28 15.0k
Stuart McNicholas 9.6k 0.9× 3.6k 1.2× 973 0.7× 1.1k 0.9× 1.4k 1.1× 19 13.4k
Robert M. Immormino 9.2k 0.9× 2.3k 0.8× 992 0.7× 1.1k 0.9× 1.3k 1.1× 34 12.7k
Ronan M. Keegan 8.3k 0.8× 3.3k 1.1× 824 0.6× 841 0.7× 1.1k 0.9× 61 11.6k
Steven J. Ludtke 9.7k 0.9× 2.0k 0.7× 773 0.6× 1.2k 1.0× 1.3k 1.1× 138 13.7k
Sandra W. Cowan 11.5k 1.1× 3.5k 1.1× 803 0.6× 1.5k 1.2× 2.1k 1.8× 16 15.2k

Countries citing papers authored by Tom Alber

Since Specialization
Citations

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

Fields of papers citing papers by Tom Alber

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Tom Alber

This figure shows the co-authorship network connecting the top 25 collaborators of Tom Alber. A scholar is included among the top collaborators of Tom Alber 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 Tom Alber. Tom Alber 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.
Kerns, S. Jordan, Roman V. Agafonov, Youngjin Cho, et al.. (2015). The energy landscape of adenylate kinase during catalysis. Nature Structural & Molecular Biology. 22(2). 124–131. 134 indexed citations
2.
Katibah, George E., Ho Jun Lee, John Huizar, et al.. (2013). tRNA Binding, Structure, and Localization of the Human Interferon-Induced Protein IFIT5. Molecular Cell. 49(4). 743–750. 65 indexed citations
3.
Prigozhin, Daniil M., et al.. (2012). Structure of the Sensor Domain of Mycobacterium tuberculosis PknH Receptor Kinase Reveals a Conserved Binding Cleft. Journal of Molecular Biology. 422(4). 488–494. 17 indexed citations
4.
Lang, P. Therese, Ho Leung Ng, James S. Fraser, et al.. (2010). Automated electron‐density sampling reveals widespread conformational polymorphism in proteins. Protein Science. 19(7). 1420–1431. 129 indexed citations
5.
He, Nanhai, Min Liu, Joanne Hsu, et al.. (2010). HIV-1 Tat and Host AFF4 Recruit Two Transcription Elongation Factors into a Bifunctional Complex for Coordinated Activation of HIV-1 Transcription. Molecular Cell. 38(3). 428–438. 321 indexed citations
6.
Jäger, Stefanie, Natali Gulbahce, Peter Cimermančič, et al.. (2010). Purification and characterization of HIV–human protein complexes. Methods. 53(1). 13–19. 44 indexed citations
7.
Lin, Michael Z., Michael R. McKeown, Ho Leung Ng, et al.. (2009). Autofluorescent Proteins with Excitation in the Optical Window for Intravital Imaging in Mammals. Chemistry & Biology. 16(11). 1169–1179. 203 indexed citations
8.
Greenstein, Andrew E., et al.. (2009). Interdomain Communication in the Mycobacterium tuberculosis Environmental Phosphatase Rv1364c. Journal of Biological Chemistry. 284(43). 29828–29835. 11 indexed citations
9.
Bertin, Aurélie, Michael A. McMurray, Patricia Grob, et al.. (2008). Saccharomyces cerevisiae septins: Supramolecular organization of heterooligomers and the mechanism of filament assembly. Proceedings of the National Academy of Sciences. 105(24). 8274–8279. 236 indexed citations
10.
Soellner, Matthew B., et al.. (2007). Fragment-Based Substrate Activity Screening Method for the Identification of Potent Inhibitors of the Mycobacterium tuberculosis Phosphatase PtpB. Journal of the American Chemical Society. 129(31). 9613–9615. 94 indexed citations
11.
Grundner, Christoph, Dominique Perrin, Rob Hooft van Huijsduijnen, et al.. (2007). Structural Basis for Selective Inhibition of Mycobacterium tuberculosis Protein Tyrosine Phosphatase PtpB. Structure. 15(4). 499–509. 83 indexed citations
12.
Fraser, James S., John P. Merlie, Nathaniel Echols, et al.. (2007). An atypical receiver domain controls the dynamic polar localization of the Myxococcus xanthus social motility protein FrzS. Molecular Microbiology. 65(2). 319–332. 32 indexed citations
13.
Grundner, Christoph, Ho Leung Ng, & Tom Alber. (2005). Mycobacterium tuberculosis Protein Tyrosine Phosphatase PtpB Structure Reveals a Diverged Fold and a Buried Active Site. Structure. 13(11). 1625–1634. 60 indexed citations
14.
Grundner, Christoph, Laurie M. Gay, & Tom Alber. (2005). Mycobacterium tuberculosis serine/threonine kinases PknB, PknD, PknE, and PknF phosphorylate multiple FHA domains. Protein Science. 14(7). 1918–1921. 71 indexed citations
15.
Ng, Ho Leung, et al.. (2004). An Alternate Conformation and a Third Metal in PstP/Ppp, the M. tuberculosis PP2C-Family Ser/Thr Protein Phosphatase. Structure. 12(11). 1947–1954. 84 indexed citations
16.
Versele, Matthias, Vı́ctor J. Cid, Shirin Bahmanyar, et al.. (2004). Protein–Protein Interactions Governing Septin Heteropentamer Assembly and Septin Filament Organization inSaccharomyces cerevisiae. Molecular Biology of the Cell. 15(10). 4568–4583. 127 indexed citations
17.
Good, Matthew C., Andrew E. Greenstein, Tracy A. Young, Ho Leung Ng, & Tom Alber. (2004). Sensor Domain of the Mycobacterium tuberculosis Receptor Ser/Thr Protein Kinase, PknD, forms a Highly Symmetric β Propeller. Journal of Molecular Biology. 339(2). 459–469. 60 indexed citations
18.
Holton, James M., et al.. (2001). Covariance analysis of RNA recognition motifs identifies functionally linked amino acids. Journal of Molecular Biology. 310(4). 793–800. 12 indexed citations
19.
Alber, Tom. (2000). The last days of crystallography. Structure. 8(9). R187–R188. 2 indexed citations
20.
Alber, Tom. (1992). Structure of the leucine zipper. Current Opinion in Genetics & Development. 2(2). 205–210. 239 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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