Louis Carlacci

965 total citations
24 papers, 830 citations indexed

About

Louis Carlacci is a scholar working on Molecular Biology, Materials Chemistry and Physical and Theoretical Chemistry. According to data from OpenAlex, Louis Carlacci has authored 24 papers receiving a total of 830 indexed citations (citations by other indexed papers that have themselves been cited), including 16 papers in Molecular Biology, 7 papers in Materials Chemistry and 5 papers in Physical and Theoretical Chemistry. Recurrent topics in Louis Carlacci's work include Protein Structure and Dynamics (13 papers), Enzyme Structure and Function (7 papers) and Glycosylation and Glycoproteins Research (4 papers). Louis Carlacci is often cited by papers focused on Protein Structure and Dynamics (13 papers), Enzyme Structure and Function (7 papers) and Glycosylation and Glycoproteins Research (4 papers). Louis Carlacci collaborates with scholars based in United States. Louis Carlacci's co-authors include Harry F. King, Kuo‐Chen Chou, Gerald M. Maggiora, Pratibha Chopra, Paras N. Prasad, Kuo‐Chen Chou, S. Walter Englander, Kuo‐Chen Chou, Kuo Chen Chou and James McIver and has published in prestigious journals such as Journal of the American Chemical Society, The Journal of Chemical Physics and Journal of Molecular Biology.

In The Last Decade

Louis Carlacci

24 papers receiving 783 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Louis Carlacci United States 14 409 208 129 129 116 24 830
P. Roychowdhury India 11 316 0.8× 147 0.7× 143 1.1× 64 0.5× 77 0.7× 35 680
Thomas J. Thamann United States 16 458 1.1× 197 0.9× 104 0.8× 55 0.4× 37 0.3× 33 879
P. Lagant France 16 305 0.7× 101 0.5× 85 0.7× 55 0.4× 150 1.3× 42 664
Zelek S. Herman United States 15 767 1.9× 113 0.5× 57 0.4× 76 0.6× 78 0.7× 29 1.2k
S. S. Rajan India 20 589 1.4× 193 0.9× 143 1.1× 93 0.7× 26 0.2× 89 1.1k
Milan Hodošček Slovenia 13 253 0.6× 134 0.6× 143 1.1× 27 0.2× 270 2.3× 38 730
P. Dupuis France 16 283 0.7× 192 0.9× 74 0.6× 237 1.8× 88 0.8× 40 834
Stefano Pieraccini Italy 21 393 1.0× 234 1.1× 277 2.1× 73 0.6× 185 1.6× 73 1.1k
Boris Weiss‐López Chile 15 219 0.5× 83 0.4× 268 2.1× 94 0.7× 90 0.8× 59 697
Christopher D. Syme United Kingdom 18 595 1.5× 195 0.9× 45 0.3× 156 1.2× 111 1.0× 21 1.4k

Countries citing papers authored by Louis Carlacci

Since Specialization
Citations

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

Fields of papers citing papers by Louis Carlacci

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Louis Carlacci

This figure shows the co-authorship network connecting the top 25 collaborators of Louis Carlacci. A scholar is included among the top collaborators of Louis Carlacci 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 Louis Carlacci. Louis Carlacci 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.
Carlacci, Louis, Rebecca P. Danam, Evaristus Enongene, et al.. (2011). The Safety and Regulation of Natural Products Used as Foods and Food Ingredients. Toxicological Sciences. 123(2). 333–348. 129 indexed citations
2.
Carlacci, Louis, Charles B. Millard, & Mark A. Olson. (2004). Conformational energy landscape of the acyl pocket loop in acetylcholinesterase: a Monte Carlo-generalized Born model study. Biophysical Chemistry. 111(2). 143–157. 10 indexed citations
3.
Carlacci, Louis. (2001). Prediction of a 12-residue loop in bovine pancreatic trypsin inhibitor: Effects of buried water. Biopolymers. 58(4). 359–373. 2 indexed citations
4.
Carlacci, Louis & Arthur S. Edison. (2000). Computational analysis of two similar neuropeptides yields distinct conformational ensembles. Proteins Structure Function and Bioinformatics. 40(3). 367–377. 4 indexed citations
5.
Carlacci, Louis. (2000). Conformational analysis of a farnesyltransferase peptide inhibitor, CVIM. Journal of Computer-Aided Molecular Design. 14(4). 369–382. 4 indexed citations
6.
Carlacci, Louis. (1998). Conformational analysis of [Met5]-enkephalin: Solvation and ionization considerations. Journal of Computer-Aided Molecular Design. 12(2). 195–213. 12 indexed citations
7.
Carlacci, Louis & S. Walter Englander. (1996). Loop problem in proteins: Developments on Monte Carlo simulated annealing approach. Journal of Computational Chemistry. 17(8). 1002–1012. 22 indexed citations
8.
Carlacci, Louis & S. Walter Englander. (1993). The loop problem in proteins: A monte carlo simulated annealing approach. Biopolymers. 33(8). 1271–1286. 31 indexed citations
9.
Chou, Kuo‐Chen, et al.. (1992). An energy‐based approach to packing the 7‐helix bundle of bacteriorhodopsin. Protein Science. 1(6). 810–827. 34 indexed citations
10.
Carlacci, Louis, et al.. (1991). Geometric and energy parameters in lysine-retinal chromophores. Protein Engineering Design and Selection. 4(8). 885–889. 5 indexed citations
11.
Carlacci, Louis, Kuo Chen Chou, & Gerald M. Maggiora. (1991). A heuristic approach to predicting the tertiary structure of bovine somatotropin. Biochemistry. 30(18). 4389–4398. 68 indexed citations
12.
Chou, Kuo‐Chen & Louis Carlacci. (1991). Simulated annealing approach to the study of protein structures. Protein Engineering Design and Selection. 4(6). 661–667. 69 indexed citations
13.
Chou, Kuo‐Chen & Louis Carlacci. (1991). Energetic approach to the folding of α/β barrels. Proteins Structure Function and Bioinformatics. 9(4). 280–295. 56 indexed citations
14.
Carlacci, Louis & Kuo‐Chen Chou. (1990). Electrostatic interactions between loops and α-helices in four-helix bundle proteins. Protein Engineering Design and Selection. 4(2). 225–227. 14 indexed citations
15.
Carlacci, Louis & Kuo‐Chen Chou. (1990). Energetic approach to the folding of four α-helices connected sequentially. Protein Engineering Design and Selection. 3(6). 509–514. 22 indexed citations
16.
Chou, Kuo‐Chen, Armin Heckel, George Némethy, et al.. (1990). Energetics of the structure and chain tilting of antiparallel β‐barrels in proteins. Proteins Structure Function and Bioinformatics. 8(1). 14–22. 21 indexed citations
17.
Chou, Kuo‐Chen, Louis Carlacci, & Gerald M. Maggiora. (1990). Conformational and geometrical properties of idealized β-barrels in proteins. Journal of Molecular Biology. 213(2). 315–326. 37 indexed citations
18.
Carlacci, Louis & Kuo‐Chen Chou. (1990). Monte carlo method applied in the search for low‐energy conformations of βαβαβ structures. Biopolymers. 30(1-2). 135–150. 8 indexed citations
19.
20.
Carlacci, Louis & James McIver. (1986). A rotationally invariant orbital transformation. The Journal of Chemical Physics. 85(1). 634–636. 2 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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