Vince J. LiCata

1.2k total citations
41 papers, 962 citations indexed

About

Vince J. LiCata is a scholar working on Molecular Biology, Cell Biology and Materials Chemistry. According to data from OpenAlex, Vince J. LiCata has authored 41 papers receiving a total of 962 indexed citations (citations by other indexed papers that have themselves been cited), including 40 papers in Molecular Biology, 11 papers in Cell Biology and 11 papers in Materials Chemistry. Recurrent topics in Vince J. LiCata's work include Protein Structure and Dynamics (15 papers), DNA and Nucleic Acid Chemistry (14 papers) and Hemoglobin structure and function (11 papers). Vince J. LiCata is often cited by papers focused on Protein Structure and Dynamics (15 papers), DNA and Nucleic Acid Chemistry (14 papers) and Hemoglobin structure and function (11 papers). Vince J. LiCata collaborates with scholars based in United States and France. Vince J. LiCata's co-authors include Gary K. Ackers, Norma M. Allewell, Kausiki Datta, David Bernlohr, Chin‐Chi Liu, Natalie Ribarik Coe, Allison J. Richard, Melanie A. Simpson, Ermanna Rovida and Paula M. Dalessio and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and Journal of Molecular Biology.

In The Last Decade

Vince J. LiCata

41 papers receiving 952 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Vince J. LiCata United States 19 797 187 137 97 93 41 962
Margaret A. Daugherty United States 16 748 0.9× 303 1.6× 284 2.1× 105 1.1× 51 0.5× 23 961
Ramaswamy Krishnamoorthi United States 19 652 0.8× 321 1.7× 108 0.8× 100 1.0× 48 0.5× 46 1.0k
S. Donald Emerson United States 17 1.0k 1.3× 342 1.8× 312 2.3× 72 0.7× 100 1.1× 21 1.3k
Teikichi Ikura Japan 21 1.1k 1.4× 178 1.0× 439 3.2× 68 0.7× 265 2.8× 55 1.7k
Y. Mauguen France 10 489 0.6× 115 0.6× 295 2.2× 30 0.3× 79 0.8× 17 652
Patrick Lagüe Canada 21 810 1.0× 122 0.7× 69 0.5× 42 0.4× 141 1.5× 59 1.2k
И. П. Куранова Russia 19 751 0.9× 156 0.8× 339 2.5× 90 0.9× 33 0.4× 91 1.0k
Narendra Narayana United States 16 701 0.9× 60 0.3× 207 1.5× 51 0.5× 70 0.8× 23 888
Hans Tuppy Austria 13 659 0.8× 121 0.6× 82 0.6× 90 0.9× 43 0.5× 27 951
Mária Vas Hungary 21 981 1.2× 182 1.0× 606 4.4× 94 1.0× 38 0.4× 66 1.2k

Countries citing papers authored by Vince J. LiCata

Since Specialization
Citations

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

Fields of papers citing papers by Vince J. LiCata

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Vince J. LiCata

This figure shows the co-authorship network connecting the top 25 collaborators of Vince J. LiCata. A scholar is included among the top collaborators of Vince J. LiCata 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 Vince J. LiCata. Vince J. LiCata 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.
LiCata, Vince J., et al.. (2013). Enthalpic switch-points and temperature dependencies of DNA binding and nucleotide incorporation by Pol I DNA polymerases. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1834(10). 2133–2138. 7 indexed citations
2.
Yang, Yanling & Vince J. LiCata. (2011). Interactions of replication versus repair DNA substrates with the Pol I DNA polymerases from Escherichia coli and Thermus aquaticus. Biophysical Chemistry. 159(1). 188–193. 4 indexed citations
3.
LiCata, Vince J. & Chin‐Chi Liu. (2010). Analysis of Free Energy Versus Temperature Curves in Protein Folding and Macromolecular Interactions. Methods in enzymology on CD-ROM/Methods in enzymology. 488. 219–238. 23 indexed citations
4.
Datta, Kausiki, et al.. (2010). Thermodynamics of the DNA Structural Selectivity of the Pol I DNA Polymerases from Escherichia coli and Thermus aquaticus. Biophysical Journal. 98(12). 3015–3024. 14 indexed citations
5.
Liu, Chin‐Chi, Allison J. Richard, Kausiki Datta, & Vince J. LiCata. (2008). Prevalence of Temperature-Dependent Heat Capacity Changes in Protein-DNA Interactions. Biophysical Journal. 94(8). 3258–3265. 24 indexed citations
6.
Richard, Allison J., et al.. (2006). Thermal stability landscape for Klenow DNA polymerase as a function of pH and salt concentration. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1764(10). 1546–1552. 14 indexed citations
7.
Datta, Kausiki, et al.. (2005). Temperature Dependence and Thermodynamics of Klenow Polymerase Binding to Primed-Template DNA. Biophysical Journal. 90(5). 1739–1751. 55 indexed citations
8.
Schoeffler, Allyn J., et al.. (2004). Extreme free energy of stabilization of Taq DNA polymerase. Proteins Structure Function and Bioinformatics. 54(4). 616–621. 6 indexed citations
9.
Schoeffler, Allyn J., et al.. (2003). Salt Modulates the Stability and Lipid Binding Affinity of the Adipocyte Lipid-binding Proteins. Journal of Biological Chemistry. 278(35). 33268–33275. 10 indexed citations
10.
Datta, Kausiki & Vince J. LiCata. (2003). Salt Dependence of DNA binding by Thermus aquaticusand Escherichia coli DNA Polymerases. Journal of Biological Chemistry. 278(8). 5694–5701. 53 indexed citations
11.
Simpson, Melanie A., Vince J. LiCata, Natalie Ribarik Coe, & David Bernlohr. (1999). Biochemical and biophysical analysis of the intracellular lipid binding proteins of adipocytes. PubMed. 192(1-2). 33–40. 40 indexed citations
12.
Simpson, Melanie A., Vince J. LiCata, Natalie Ribarik Coe, & David Bernlohr. (1999). Biochemical and biophysical analysis of the intracellular lipid binding proteins of adipocytes. Molecular and Cellular Biochemistry. 192(1-2). 33–40. 36 indexed citations
13.
LiCata, Vince J. & Norma M. Allewell. (1998). [3] Measuring hydration changes of proteins in solution: Applications of osmotic stress and structure-based calculations. Methods in enzymology on CD-ROM/Methods in enzymology. 295. 42–62. 19 indexed citations
14.
LiCata, Vince J. & Norma M. Allewell. (1997). Is substrate inhibition a consequence of allostery in aspartate transcarbamylase?. Biophysical Chemistry. 64(1-3). 225–234. 64 indexed citations
15.
LiCata, Vince J. & Gary K. Ackers. (1995). Long-Range, Small Magnitude Nonadditivity of Mutational Effects in Proteins. Biochemistry. 34(10). 3133–3139. 97 indexed citations
16.
Allewell, Norma M. & Vince J. LiCata. (1995). [28] Thermodynamic approaches to understanding aspartate transcarbamylase. Methods in enzymology on CD-ROM/Methods in enzymology. 259. 608–628. 8 indexed citations
17.
Bromberg, Sarina, et al.. (1994). Ligation alters the pathway of urea‐induced denaturation of the catalytic trimer of Escherichia coli aspartate transcarbamylase. Protein Science. 3(8). 1236–1244. 5 indexed citations
18.
LiCata, Vince J., Paula M. Dalessio, & Gary K. Ackers. (1993). Single‐site modifications of half‐ligated hemoglobin reveal autonomous dimer cooperativity within a quaternary T tetramer. Proteins Structure Function and Bioinformatics. 17(3). 279–296. 27 indexed citations
19.
LiCata, Vince J., et al.. (1991). Experimental resolution of cooperative free energies for the ten ligation species of cobalt(II)/iron(II)-carbon monoxide hemoglobin. Biochemistry. 30(29). 7254–7262. 24 indexed citations
20.

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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