John J. Portman

1.7k total citations · 1 hit paper
20 papers, 1.5k citations indexed

About

John J. Portman is a scholar working on Molecular Biology, Materials Chemistry and Atomic and Molecular Physics, and Optics. According to data from OpenAlex, John J. Portman has authored 20 papers receiving a total of 1.5k indexed citations (citations by other indexed papers that have themselves been cited), including 17 papers in Molecular Biology, 13 papers in Materials Chemistry and 6 papers in Atomic and Molecular Physics, and Optics. Recurrent topics in John J. Portman's work include Protein Structure and Dynamics (15 papers), Enzyme Structure and Function (12 papers) and Spectroscopy and Quantum Chemical Studies (5 papers). John J. Portman is often cited by papers focused on Protein Structure and Dynamics (15 papers), Enzyme Structure and Function (12 papers) and Spectroscopy and Quantum Chemical Studies (5 papers). John J. Portman collaborates with scholars based in United States and Japan. John J. Portman's co-authors include Peter G. Wolynes, Benjamin A. Shoemaker, Shoji Takada, Swarnendu Tripathi, Brett Ellman, Robert J. Twieg, Tongye Shen, Chenghang Zong, Golam Mustafa and Hamza Balci and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Physical Review Letters and The Journal of Chemical Physics.

In The Last Decade

John J. Portman

20 papers receiving 1.4k citations

Hit Papers

Speeding molecular recognition by using the folding funne... 2000 2026 2008 2017 2000 250 500 750
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.

  1. Speeding molecular recognition by using the folding funnel: The fly-casting mechanism
    2000 821 citations Benjamin A. Shoemaker, John J. Portman et al. Proceedings of the National Academy of Sciences profile →

Peers

John J. Portman
David Shaw United States
Kei-ichi Okazaki Japan
Madeleine B. Borgia Switzerland
Athi N. Naganathan India
Monique M. Tirion United States
Mourad Sadqi United States
Vincent A. Voelz United States
Arjan van der Vaart United States
Houbi Nguyen United States
Jaewoon Jung Japan
David Shaw United States
John J. Portman
Citations per year, relative to John J. Portman John J. Portman (= 1×) peers David Shaw

Countries citing papers authored by John J. Portman

Since Specialization
Citations

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

Fields of papers citing papers by John J. Portman

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by John J. Portman. 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 John J. Portman. The network helps show where John J. Portman may publish in the future.

Co-authorship network of co-authors of John J. Portman

This figure shows the co-authorship network connecting the top 25 collaborators of John J. Portman. A scholar is included among the top collaborators of John J. Portman 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 John J. Portman. John J. Portman 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.
Portman, John J., et al.. (2023). Vanishing tails and a resilient mesophase: columnar liquid crystals in the limit of short tails. Materials Advances. 4(18). 4129–4137. 11 indexed citations
2.
Mustafa, Golam, et al.. (2022). Emerging accessibility patterns in long telomeric overhangs. Proceedings of the National Academy of Sciences. 119(30). e2202317119–e2202317119. 9 indexed citations
3.
Twieg, Robert J., et al.. (2022). Structure and dynamics of tail-free discotic liquid crystals: Simulations of fluorinated triphenylene. The Journal of Chemical Physics. 157(13). 134901–134901. 7 indexed citations
4.
Portman, John J., et al.. (2016). Comparing allosteric transitions in the domains of calmodulin through coarse-grained simulations. The Journal of Chemical Physics. 144(10). 105102–105102. 4 indexed citations
5.
Tripathi, Swarnendu & John J. Portman. (2013). Allostery and Folding of the N-terminal Receiver Domain of Protein NtrC. The Journal of Physical Chemistry B. 117(42). 13182–13193. 6 indexed citations
6.
Tripathi, Swarnendu & John J. Portman. (2011). Conformational flexibility and the mechanisms of allosteric transitions in topologically similar proteins. The Journal of Chemical Physics. 135(7). 75104–75104. 10 indexed citations
7.
Portman, John J.. (2010). Cooperativity and protein folding rates. Current Opinion in Structural Biology. 20(1). 11–15. 22 indexed citations
8.
Tripathi, Swarnendu & John J. Portman. (2009). Inherent flexibility determines the transition mechanisms of the EF-hands of calmodulin. Proceedings of the National Academy of Sciences. 106(7). 2104–2109. 59 indexed citations
9.
Yaron, David, Jodi L. Davenport, Michael Karabinos, et al.. (2008). Cross-disciplinary molecular science education in introductory science courses. 70–73. 1 indexed citations
10.
Tripathi, Swarnendu & John J. Portman. (2008). Inherent flexibility and protein function: The open/closed conformational transition in the N-terminal domain of calmodulin. The Journal of Chemical Physics. 128(20). 205104–205104. 22 indexed citations
11.
Portman, John J., et al.. (2008). Capillarity-like growth of protein folding nuclei. Proceedings of the National Academy of Sciences. 105(32). 11164–11169. 10 indexed citations
12.
Shen, Tongye, Chenghang Zong, John J. Portman, & Peter G. Wolynes. (2008). Variationally Determined Free Energy Profiles for Structural Models of Proteins:  Characteristic Temperatures for Folding and Trapping. The Journal of Physical Chemistry B. 112(19). 6074–6082. 6 indexed citations
13.
Portman, John J., et al.. (2007). Excluded volume, local structural cooperativity, and the polymer physics of protein folding rates. Proceedings of the National Academy of Sciences. 104(26). 10841–10846. 20 indexed citations
14.
Portman, John J.. (2003). Non-Gaussian dynamics from a simulation of a short peptide: Loop closure rates and effective diffusion coefficients. The Journal of Chemical Physics. 118(5). 2381–2391. 53 indexed citations
15.
Portman, John J., Shoji Takada, & Peter G. Wolynes. (2001). Microscopic theory of protein folding rates. II. Local reaction coordinates and chain dynamics. The Journal of Chemical Physics. 114(11). 5082–5096. 143 indexed citations
16.
Portman, John J., Shoji Takada, & Peter G. Wolynes. (2001). Microscopic theory of protein folding rates. I. Fine structure of the free energy profile and folding routes from a variational approach. The Journal of Chemical Physics. 114(11). 5069–5081. 94 indexed citations
17.
Shoemaker, Benjamin A., John J. Portman, & Peter G. Wolynes. (2000). Speeding molecular recognition by using the folding funnel: The fly-casting mechanism. Proceedings of the National Academy of Sciences. 97(16). 8868–8873. 821 indexed citations breakdown →
18.
Portman, John J. & Peter G. Wolynes. (1999). Complementary Variational Approximations for Intermittency and Reaction Dynamics in Fluctuating Environments. The Journal of Physical Chemistry A. 103(49). 10602–10610. 33 indexed citations
19.
Portman, John J., Shoji Takada, & Peter G. Wolynes. (1998). Variational Theory for Site Resolved Protein Folding Free Energy Surfaces. Physical Review Letters. 81(23). 5237–5240. 102 indexed citations
20.
Takada, Shoji, John J. Portman, & Peter G. Wolynes. (1997). An elementary mode coupling theory of random heteropolymer dynamics. Proceedings of the National Academy of Sciences. 94(6). 2318–2321. 18 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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