Sara M. Vaiana

472 total citations
17 papers, 343 citations indexed

About

Sara M. Vaiana is a scholar working on Molecular Biology, Pulmonary and Respiratory Medicine and Physiology. According to data from OpenAlex, Sara M. Vaiana has authored 17 papers receiving a total of 343 indexed citations (citations by other indexed papers that have themselves been cited), including 15 papers in Molecular Biology, 3 papers in Pulmonary and Respiratory Medicine and 3 papers in Physiology. Recurrent topics in Sara M. Vaiana's work include Protein Structure and Dynamics (10 papers), Alzheimer's disease research and treatments (3 papers) and Enzyme Structure and Function (3 papers). Sara M. Vaiana is often cited by papers focused on Protein Structure and Dynamics (10 papers), Alzheimer's disease research and treatments (3 papers) and Enzyme Structure and Function (3 papers). Sara M. Vaiana collaborates with scholars based in United States, Italy and United Kingdom. Sara M. Vaiana's co-authors include M. B. Palma‐Vittorelli, M. U. Palma, Emanuele Amadio, Mauro Manno, Robert B. Best, William A. Eaton, James Hofrichter, Wai‐Ming Yau, Giovanna Ghirlanda and Pier Luigi San Biagio and has published in prestigious journals such as Nucleic Acids Research, PLoS ONE and Biophysical Journal.

In The Last Decade

Sara M. Vaiana

16 papers receiving 341 citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Sara M. Vaiana United States	10	237	88	76	48	31	17	343
William F. Weiss United States	10	540 2.3×	24 0.3×	107 1.4×	37 0.8×	60 1.9×	17	619
Harold E. Frey Canada	9	297 1.3×	63 0.7×	46 0.6×	15 0.3×	74 2.4×	10	435
Zhaoqian Su United States	11	221 0.9×	37 0.4×	59 0.8×	17 0.4×	24 0.8×	41	357
Aritz B. García‐Arribas Spain	14	426 1.8×	123 1.4×	33 0.4×	12 0.3×	53 1.7×	27	526
H.T. Gaud United States	10	251 1.1×	48 0.5×	34 0.4×	54 1.1×	13 0.4×	12	387
Daxian Shan United States	7	291 1.2×	19 0.2×	40 0.5×	13 0.3×	27 0.9×	10	407
Marina R. Kasimova Denmark	13	432 1.8×	17 0.2×	63 0.8×	30 0.6×	37 1.2×	17	580
Jes Kristian Jacobsen Denmark	6	203 0.9×	13 0.1×	110 1.4×	15 0.3×	52 1.7×	7	361
Balakrishnan S. Moorthy United States	12	587 2.5×	22 0.3×	59 0.8×	37 0.8×	104 3.4×	17	721
T. N. Murugova Russia	11	214 0.9×	21 0.2×	68 0.9×	8 0.2×	36 1.2×	33	344

Countries citing papers authored by Sara M. Vaiana

Since Specialization

Citations

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

Fields of papers citing papers by Sara M. Vaiana

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Sara M. Vaiana. 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 Sara M. Vaiana. The network helps show where Sara M. Vaiana may publish in the future.

Co-authorship network of co-authors of Sara M. Vaiana

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

All Works

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17 of 17 papers shown

Kolář, Michal H., et al.. (2022). Folding of VemP into translation-arresting secondary structure is driven by the ribosome exit tunnel. Nucleic Acids Research. 50(4). 2258–2269. 8 indexed citations

Nagy, Gábor, et al.. (2022). A proposed mechanism for Vibrio export monitoring polypeptide folding in the ribosome exit tunnel. Biophysical Journal. 121(3). 202a–202a.

Roy, Anindya, et al.. (2015). Slow Internal Dynamics and Charge Expansion in the Disordered Protein CGRP: A Comparison with Amylin. Biophysical Journal. 109(5). 1038–1048. 23 indexed citations

Roy, Anindya, et al.. (2014). Structure and Internal Dynamics of Calcitonin Family Peptides: Implications for Amyloid Formation. Biophysical Journal. 106(2). 687a–687a. 1 indexed citations

Tsen, Shaw-Wei D., David H. Kingsley, Karen V. Kibler, et al.. (2014). Pathogen Reduction in Human Plasma Using an Ultrashort Pulsed Laser. PLoS ONE. 9(11). e111673–e111673. 8 indexed citations

Shinde, Sandip S., et al.. (2013). Cyclic N Terminal Fragment of Amylin Forms Non Amyloid Fibers: Implications for Intra- and Inter-Molecular Interactions in Amylin. Biophysical Journal. 104(2). 389a–390a. 1 indexed citations

Shinde, Sandip S., et al.. (2013). Cyclic N-Terminal Loop of Amylin Forms Non Amyloid Fibers. Biophysical Journal. 105(7). 1661–1669. 8 indexed citations

Conlon, Jennifer, et al.. (2012). Conformational dynamics of human IAPP monomers. Biophysical Chemistry. 167. 1–7. 24 indexed citations

Kaur, Parminder, et al.. (2012). Hydrophobicity of methylated DNA as a possible mechanism for gene silencing. Physical Biology. 9(6). 65001–65001. 29 indexed citations

10.

Tsen, Shaw-Wei D., Qiang Fu, Stuart Lindsay, et al.. (2011). Studies of inactivation of encephalomyocarditis virus, M13 bacteriophage, and Salmonella typhimurium by using a visible femtosecond laser: insight into the possible inactivation mechanisms. Journal of Biomedical Optics. 16(7). 78003–78003. 32 indexed citations

11.

Tsen, K. T., Shaw-Wei D. Tsen, Qiang Fu, et al.. (2010). Photonic approach to the selective inactivation of viruses with a near-infrared ultrashort pulsed laser. Proceedings of SPIE, the International Society for Optical Engineering/Proceedings of SPIE. 7561. 75610W–75610W. 3 indexed citations

12.

Vaiana, Sara M., Robert B. Best, Wai‐Ming Yau, William A. Eaton, & James Hofrichter. (2009). Evidence for a Partially Structured State of the Amylin Monomer. Biophysical Journal. 97(11). 2948–2957. 43 indexed citations

13.

Vaiana, Sara M., et al.. (2004). Effect of T‐R conformational change on sickle‐cell hemoglobin interactions and aggregation. Proteins Structure Function and Bioinformatics. 58(2). 426–438. 14 indexed citations

14.

Vaiana, Sara M., Emanuele Amadio, M. B. Palma‐Vittorelli, & M. U. Palma. (2004). Irreversible formation of intermediate BSA oligomers requires and induces conformational changes. Proteins Structure Function and Bioinformatics. 55(4). 1053–1062. 41 indexed citations

15.

Vaiana, Sara M., M. B. Palma‐Vittorelli, & M. U. Palma. (2003). Time scale of protein aggregation dictated by liquid‐liquid demixing. Proteins Structure Function and Bioinformatics. 51(1). 147–153. 31 indexed citations

16.

Vaiana, Sara M., Mauro Manno, Emanuele Amadio, M. B. Palma‐Vittorelli, & M. U. Palma. (2001). The Role of Solvent in Protein Folding and in Aggregation. Journal of Biological Physics. 27(2-3). 133–145. 34 indexed citations

17.

Biagio, Pier Luigi San, Vincenzo Martorana, Emanuele Amadio, et al.. (1999). Interacting processes in protein coagulation. Proteins Structure Function and Bioinformatics. 37(1). 116–120. 43 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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