David S. Libich

1.7k total citations
44 papers, 1.3k citations indexed

About

David S. Libich is a scholar working on Molecular Biology, Materials Chemistry and Spectroscopy. According to data from OpenAlex, David S. Libich has authored 44 papers receiving a total of 1.3k indexed citations (citations by other indexed papers that have themselves been cited), including 41 papers in Molecular Biology, 11 papers in Materials Chemistry and 5 papers in Spectroscopy. Recurrent topics in David S. Libich's work include RNA Research and Splicing (20 papers), Protein Structure and Dynamics (13 papers) and RNA modifications and cancer (11 papers). David S. Libich is often cited by papers focused on RNA Research and Splicing (20 papers), Protein Structure and Dynamics (13 papers) and RNA modifications and cancer (11 papers). David S. Libich collaborates with scholars based in United States, Canada and New Zealand. David S. Libich's co-authors include George Harauz, G. Marius Clore, Christopher M. Hill, Ian R. Bates, Vitali Tugarinov, Christophe Farès, Noboru Ishiyama, Nicolas L. Fawzi, Jinfa Ying and Rodolfo Ghirlando and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and Angewandte Chemie International Edition.

In The Last Decade

David S. Libich

41 papers receiving 1.2k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
David S. Libich United States 23 931 276 214 187 138 44 1.3k
Ian R. Bates Canada 14 568 0.6× 106 0.4× 75 0.4× 150 0.8× 120 0.9× 15 764
Jeffrey Hanson United States 17 826 0.9× 45 0.2× 147 0.7× 82 0.4× 41 0.3× 24 1.4k
François‐Xavier Cantrelle France 23 929 1.0× 78 0.3× 103 0.5× 228 1.2× 13 0.1× 71 1.4k
Stefan Bibow Switzerland 15 1.1k 1.2× 241 0.9× 253 1.2× 237 1.3× 5 0.0× 25 1.5k
Steven Chin United States 24 852 0.9× 132 0.5× 88 0.4× 376 2.0× 31 0.2× 51 1.5k
Godha Rangaraj Canada 22 861 0.9× 105 0.4× 38 0.2× 167 0.9× 123 0.9× 35 1.4k
Peter Brodin Sweden 18 884 0.9× 190 0.7× 267 1.2× 98 0.5× 6 0.0× 28 1.3k
George J. Turner United States 12 651 0.7× 92 0.3× 144 0.7× 201 1.1× 54 0.4× 21 987
Margarida Gairí Spain 17 941 1.0× 173 0.6× 148 0.7× 104 0.6× 5 0.0× 33 1.2k
N. Celestine Sweden 22 1.2k 1.3× 131 0.5× 391 1.8× 266 1.4× 6 0.0× 50 1.4k

Countries citing papers authored by David S. Libich

Since Specialization
Citations

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

Fields of papers citing papers by David S. Libich

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of David S. Libich

This figure shows the co-authorship network connecting the top 25 collaborators of David S. Libich. A scholar is included among the top collaborators of David S. Libich 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 S. Libich. David S. Libich 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.
Xu, Xiaoping, et al.. (2025). Molecular basis of EWS interdomain self‐association and its role in condensate formation. Protein Science. 34(10). e70316–e70316.
2.
Montalbano, Mauro, Gabriela D. A. Guardia, Adam Kosti, et al.. (2025). SERBP1 interacts with PARP1 and is present in PARylation-dependent protein complexes regulating splicing, cell division, and ribosome biogenesis. eLife. 13. 3 indexed citations
3.
Li, Wenjing, Jeffrey N. Katz, Neelam Sharma, et al.. (2025). Distinct roles of the two BRCA2 DNA-binding domains in DNA damage repair and replication fork preservation. Cell Reports. 44(5). 115654–115654.
4.
Xu, Xiaoping, et al.. (2025). The 1H, 15N and 13C backbone resonance assignments of the N-terminal (1-149) domain of Serpine mRNA Binding Protein 1 (SERBP1). Biomolecular NMR Assignments. 19(1). 101–107. 1 indexed citations
5.
Libich, David S., et al.. (2024). Hijacking the BAF complex: the mechanistic interplay of ARID1A and EWS::FLI1 in Ewing sarcoma. Molecular Oncology. 19(4). 961–964. 1 indexed citations
6.
Lei, Xiufen, Mauro Montalbano, Gabriela D. A. Guardia, et al.. (2024). SERBP1 interacts with PARP1 and is present in PARylation-dependent protein complexes regulating splicing, cell division, and ribosome biogenesis. eLife. 13. 2 indexed citations
7.
Libich, David S., et al.. (2024). Squishy to crusty: Biophysics reveal the molecular details of FUS droplet maturation. Structure. 32(7). 854–855.
8.
Libich, David S., et al.. (2023). Enhancing the Conformational Stability of the cl-Par-4 Tumor Suppressor via Site-Directed Mutagenesis. Biomolecules. 13(4). 667–667. 2 indexed citations
9.
Xu, Xiaoping, et al.. (2021). The 1H, 15N and 13C resonance assignments of the C-terminal domain of Serpine mRNA binding protein 1 (SERBP1). Biomolecular NMR Assignments. 15(2). 461–466. 4 indexed citations
10.
Xu, Xiaoping, et al.. (2021). Structural Characterization of the RNA-Binding Protein SERBP1 Reveals Intrinsic Disorder and Atypical RNA Binding Modes. Frontiers in Molecular Biosciences. 8. 744707–744707. 23 indexed citations
11.
Tugarinov, Vitali, David S. Libich, Virginia Meyer, Julien Roche, & G. Marius Clore. (2015). The Energetics of a Three‐State Protein Folding System Probed by High‐Pressure Relaxation Dispersion NMR Spectroscopy. Angewandte Chemie International Edition. 54(38). 11157–11161. 23 indexed citations
12.
Fawzi, Nicolas L., David S. Libich, Jinfa Ying, Vitali Tugarinov, & G. Marius Clore. (2014). Characterizing Methyl‐Bearing Side Chain Contacts and Dynamics Mediating Amyloid β Protofibril Interactions Using 13Cmethyl‐DEST and Lifetime Line Broadening. Angewandte Chemie International Edition. 53(39). 10345–10349. 42 indexed citations
13.
Harauz, George & David S. Libich. (2009). The Classic Basic Protein of Myelin – Conserved Structural Motifs and the Dynamic Molecular Barcode Involved in Membrane Adhesion and Protein-Protein Interactions. Current Protein and Peptide Science. 10(3). 196–215. 57 indexed citations
14.
Libich, David S. & George Harauz. (2008). Backbone Dynamics of the 18.5kDa Isoform of Myelin Basic Protein Reveals Transient α-Helices and a Calmodulin-Binding Site. Biophysical Journal. 94(12). 4847–4866. 44 indexed citations
15.
Farès, Christophe, David S. Libich, & George Harauz. (2006). Solution NMR structure of an immunodominant epitope of myelin basic protein. FEBS Journal. 273(3). 601–614. 35 indexed citations
16.
Libich, David S., Christopher M. Hill, Jeffery D. Haines, & George Harauz. (2003). Myelin basic protein has multiple calmodulin-binding sites. Biochemical and Biophysical Research Communications. 308(2). 313–319. 27 indexed citations
17.
Kaur, Jaspreet, David S. Libich, Celia W. Campagnoni, et al.. (2003). Expression and properties of the recombinant murine Golli‐myelin basic protein isoform J37. Journal of Neuroscience Research. 71(6). 777–784. 15 indexed citations
18.
Hill, Christopher M., et al.. (2003). Terminal deletion mutants of myelin basic protein: new insights into self-association and phospholipid interactions. Micron. 34(1). 25–37. 22 indexed citations
19.
20.
Libich, David S. & George Harauz. (2002). Interactions of the 18.5-kDa isoform of myelin basic protein with Ca2+-calmodulin: in vitro studies using fluorescence microscopy and spectroscopy. Biochemistry and Cell Biology. 80(4). 395–406. 23 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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