David P. Weliky

2.7k total citations
84 papers, 2.4k citations indexed

About

David P. Weliky is a scholar working on Molecular Biology, Spectroscopy and Virology. According to data from OpenAlex, David P. Weliky has authored 84 papers receiving a total of 2.4k indexed citations (citations by other indexed papers that have themselves been cited), including 45 papers in Molecular Biology, 27 papers in Spectroscopy and 26 papers in Virology. Recurrent topics in David P. Weliky's work include HIV Research and Treatment (26 papers), Protein Structure and Dynamics (23 papers) and Lipid Membrane Structure and Behavior (20 papers). David P. Weliky is often cited by papers focused on HIV Research and Treatment (26 papers), Protein Structure and Dynamics (23 papers) and Lipid Membrane Structure and Behavior (20 papers). David P. Weliky collaborates with scholars based in United States, Israel and Greece. David P. Weliky's co-authors include Robert Tycko, Jun Yang, Mercouri G. Kanatzidis, Charles M. Gabrys, Yan Sun, Christian G. Canlas, In Jae Chung, Takeshi Oka, Rong Yang and Takamasa Momose and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and Physical Review Letters.

In The Last Decade

David P. Weliky

83 papers receiving 2.4k citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
David P. Weliky United States	30	1.1k	756	573	465	369	84	2.4k
Tatyana Polenova United States	44	1.4k 1.3×	2.8k 3.7×	1.6k 2.9×	315 0.7×	237 0.6×	141	4.6k
Clyde A. Hutchison United States	30	686 0.6×	611 0.8×	1.2k 2.1×	279 0.6×	344 0.9×	94	3.6k
Hashim M. Al‐Hashimi United States	51	7.8k 7.2×	1.5k 1.9×	913 1.6×	250 0.5×	96 0.3×	173	8.6k
Alexander A. Nevzorov United States	21	932 0.9×	1.0k 1.4×	426 0.7×	73 0.2×	43 0.1×	55	1.7k
Alexander Grishaev United States	29	2.6k 2.4×	758 1.0×	1.2k 2.0×	125 0.3×	23 0.1×	77	3.2k
James L. Baber United States	18	931 0.9×	334 0.4×	319 0.6×	93 0.2×	70 0.2×	30	1.3k
Florence Cordier France	28	1.8k 1.6×	908 1.2×	544 0.9×	77 0.2×	28 0.1×	53	2.6k
David P. Millar United States	39	3.0k 2.7×	270 0.4×	461 0.8×	146 0.3×	76 0.2×	115	4.0k
Rolf Schäfer Germany	32	870 0.8×	102 0.1×	1.5k 2.6×	119 0.3×	304 0.8×	171	4.2k
Joseph E. Curtis United States	34	1.9k 1.7×	324 0.4×	745 1.3×	187 0.4×	16 0.0×	81	3.0k

Countries citing papers authored by David P. Weliky

Since Specialization

Citations

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

Fields of papers citing papers by David P. Weliky

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by David P. Weliky. 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 David P. Weliky. The network helps show where David P. Weliky may publish in the future.

Co-authorship network of co-authors of David P. Weliky

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

All Works

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20 of 20 papers shown

Wolfe, Robert, et al.. (2022). A large HIV gp41 construct with trimer-of-hairpins structure exhibits V2E mutation-dominant attenuation of vesicle fusion and helicity very similar to V2E attenuation of HIV fusion and infection and supports: (1) hairpin stabilization of membrane apposition with larger distance for V2E; and (2) V2E dominance by an antiparallel β sheet with interleaved fusion peptide strands from two gp41 trimers. Biophysical Chemistry. 293. 106933–106933. 1 indexed citations

Ghosh, Ujjayini & David P. Weliky. (2020). 2H nuclear magnetic resonance spectroscopy supports larger amplitude fast motion and interference with lipid chain ordering for membrane that contains β sheet human immunodeficiency virus gp41 fusion peptide or helical hairpin influenza virus hemagglutinin fusion peptide at fusogenic pH. Biochimica et Biophysica Acta (BBA) - Biomembranes. 1862(10). 183404–183404. 8 indexed citations

Jia, Lihui, et al.. (2015). REDOR solid-state NMR as a probe of the membrane locations of membrane-associated peptides and proteins. Journal of Magnetic Resonance. 253. 154–165. 22 indexed citations

Weliky, David P.. (2014). Solid-State NMR Structural Measurements and Models of the HIV and Influenza Fusion Proteins in Membranes. Biophysical Journal. 106(2). 636a–637a. 1 indexed citations

Ghosh, Ujjayini, et al.. (2013). Detection of closed influenza virus hemagglutinin fusion peptide structures in membranes by backbone 13CO-15N rotational-echo double-resonance solid-state NMR. Journal of Biomolecular NMR. 55(2). 139–146. 19 indexed citations

Tristram‐Nagle, Stephanie, et al.. (2011). HIV Fusion Peptide Penetrates, Disorders and Softens T-Cell Membrane Mimics. Biophysical Journal. 100(3). 186a–186a. 1 indexed citations

Weliky, David P., et al.. (2011). Solid-State Nuclear Magnetic Resonance (NMR) Spectroscopy of Human Immunodeficiency Virus gp41 Protein That Includes the Fusion Peptide: NMR Detection of Recombinant Fgp41 in Inclusion Bodies in Whole Bacterial Cells and Structural Characterization of Purified and Membrane-Associated Fgp41. Biochemistry. 50(46). 10013–10026. 17 indexed citations

Sackett, Kelly, Richard M. Epand, Richard M. Epand, et al.. (2010). Comparative Analysis of Membrane-Associated Fusion Peptide Secondary Structure and Lipid Mixing Function of HIV gp41 Constructs that Model the Early Pre-Hairpin Intermediate and Final Hairpin Conformations. Journal of Molecular Biology. 397(1). 301–315. 38 indexed citations

Tristram‐Nagle, Stephanie, et al.. (2010). HIV Fusion Peptide Penetrates, Disorders, and Softens T-Cell Membrane Mimics. Journal of Molecular Biology. 402(1). 139–153. 69 indexed citations

10.

Sackett, Kelly, et al.. (2009). Hairpin Folding of HIV gp41 Abrogates Lipid Mixing Function at Physiologic pH and Inhibits Lipid Mixing by Exposed gp41 Constructs. Biochemistry. 48(12). 2714–2722. 24 indexed citations

11.

Yang, Jun, et al.. (2007). Solid-State Nuclear Magnetic Resonance Measurements of HIV Fusion Peptide to Lipid Distances Reveal the Intimate Contact of β Strand Peptide with Membranes and the Proximity of the Ala-14−Gly-16 Region with Lipid Headgroups. Biochemistry. 46(17). 4997–5008. 17 indexed citations

12.

Qiang, Wei, et al.. (2007). Investigation of finite-pulse radiofrequency-driven recoupling methods for measurement of intercarbonyl distances in polycrystalline and membrane-associated HIV fusion peptide samples. Magnetic Resonance in Chemistry. 45(S1). S247–S260. 6 indexed citations

13.

Yang, Rong, Mary Prorok, Francis Castellino, & David P. Weliky. (2004). A Trimeric HIV-1 Fusion Peptide Construct Which Does Not Self-Associate in Aqueous Solution and Which Has 15-Fold Higher Membrane Fusion Rate. Journal of the American Chemical Society. 126(45). 14722–14723. 53 indexed citations

14.

Weliky, David P., et al.. (2003). 15N-CPMAS nuclear magnetic resonance spectroscopy and biological stability of soil organic nitrogen in whole soil and particle-size fractions. Organic Geochemistry. 34(12). 1635–1650. 20 indexed citations

15.

Canlas, Christian G., Mercouri G. Kanatzidis, & David P. Weliky. (2003). ³¹P Solid State NMR Studies of Metal Selenophosphates Containing [P₂Se₆]⁴^-, [P₄Se₁₀]⁴^-, [PSe₄]³^-, [P₂Se₇]⁴^-, and [P₂Se₉]⁴^- Ligands. Inorganic Chemistry. 42(11). 3399–3405. 17 indexed citations

16.

Rangan, K. Kasthuri, Pantelis N. Trikalitis, Christian P. Canlas, et al.. (2002). Hexagonal Pore Organization in Mesostructured Metal Tin Sulfides Built with [Sn₂S₆]^4- Cluster. Nano Letters. 2(5). 513–517. 56 indexed citations

17.

Yang, Jun, Charles M. Gabrys, & David P. Weliky. (2001). Solid-State Nuclear Magnetic Resonance Evidence for an Extended β Strand Conformation of the Membrane-Bound HIV-1 Fusion Peptide. Biochemistry. 40(27). 8126–8137. 97 indexed citations

18.

Tycko, Robert, David P. Weliky, & Alan E. Berger. (1996). Investigation of molecular structure in solids by two-dimensional NMR exchange spectroscopy with magic angle spinning. The Journal of Chemical Physics. 105(18). 7915–7930. 87 indexed citations

19.

Momose, Takamasa, et al.. (1994). Condon modulation spectroscopy of solid hydrogen and measurement of the temperature dependence of theQ1(0) transition. Physical Review Letters. 72(25). 3957–3960. 24 indexed citations

20.

Pursell, Christopher J., et al.. (1990). Infrared–microwave double resonance spectroscopy of molecular ions: HN+2. The Journal of Chemical Physics. 93(1). 87–93. 10 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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