Natalie A. Glavas

1.3k total citations
16 papers, 1.0k citations indexed

About

Natalie A. Glavas is a scholar working on Molecular Biology, Materials Chemistry and Pediatrics, Perinatology and Child Health. According to data from OpenAlex, Natalie A. Glavas has authored 16 papers receiving a total of 1.0k indexed citations (citations by other indexed papers that have themselves been cited), including 12 papers in Molecular Biology, 8 papers in Materials Chemistry and 4 papers in Pediatrics, Perinatology and Child Health. Recurrent topics in Natalie A. Glavas's work include Enzyme Structure and Function (8 papers), Biochemical and Molecular Research (6 papers) and Amino Acid Enzymes and Metabolism (4 papers). Natalie A. Glavas is often cited by papers focused on Enzyme Structure and Function (8 papers), Biochemical and Molecular Research (6 papers) and Amino Acid Enzymes and Metabolism (4 papers). Natalie A. Glavas collaborates with scholars based in Canada, United States and Sweden. Natalie A. Glavas's co-authors include Philip D. Bragg, Joseph A. Beavo, Suhail Ahmad, X. Charlene Tang, Wim G. J. Hol, S. Turley, Scott H. Soderling, Sergio E. Martinez, Albert Y. Wu and Matthew Waldbrook and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and Nature Biotechnology.

In The Last Decade

Natalie A. Glavas

16 papers receiving 1.0k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Natalie A. Glavas Canada 14 801 261 218 134 134 16 1.0k
Angela Harper United Kingdom 11 472 0.6× 221 0.8× 680 3.1× 38 0.3× 26 0.2× 13 1.2k
Rodolfo García Argentina 10 288 0.4× 45 0.2× 254 1.2× 22 0.2× 36 0.3× 18 644
Carla Luzi Italy 13 291 0.4× 271 1.0× 107 0.5× 24 0.2× 75 0.6× 21 595
Masanori Iwama Japan 16 657 0.8× 37 0.1× 121 0.6× 151 1.1× 68 0.5× 57 930
Paola Martelli Italy 16 284 0.4× 44 0.2× 38 0.2× 57 0.4× 16 0.1× 48 693
Allen J. Duplantier United States 17 433 0.5× 159 0.6× 127 0.6× 122 0.9× 9 0.1× 28 892
Leonard S. Jacob United States 8 398 0.5× 326 1.2× 114 0.5× 59 0.4× 5 0.0× 15 673
Erica Miraglia Italy 10 233 0.3× 82 0.3× 73 0.3× 14 0.1× 33 0.2× 11 643
Haim Tsubery Israel 15 364 0.5× 172 0.7× 79 0.4× 91 0.7× 19 0.1× 23 736
David C. Emery United Kingdom 13 501 0.6× 45 0.2× 65 0.3× 82 0.6× 77 0.6× 20 994

Countries citing papers authored by Natalie A. Glavas

Since Specialization
Citations

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

Fields of papers citing papers by Natalie A. Glavas

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Natalie A. Glavas. 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 Natalie A. Glavas. The network helps show where Natalie A. Glavas may publish in the future.

Co-authorship network of co-authors of Natalie A. Glavas

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

All Works

16 of 16 papers shown
1.
Scott, Monisha G., Edie Dullaghan, Neeloffer Mookherjee, et al.. (2007). An anti-infective peptide that selectively modulates the innate immune response. Nature Biotechnology. 25(4). 465–472. 317 indexed citations
2.
Dua, Rajiv, et al.. (2004). 587 Development of proximity based assay to detect and quantify erbB (or Her) receptor dimerization in formalin fixed-paraffin embedded tissue sections. European Journal of Cancer Supplements. 2(8). 178–178. 1 indexed citations
3.
Martinez, Sergio E., Albert Y. Wu, Natalie A. Glavas, et al.. (2002). The two GAF domains in phosphodiesterase 2A have distinct roles in dimerization and in cGMP binding. Proceedings of the National Academy of Sciences. 99(20). 13260–13265. 206 indexed citations
4.
Glavas, Natalie A., et al.. (2001). T cell activation up-regulates cyclic nucleotide phosphodiesterases 8A1 and 7A3. Proceedings of the National Academy of Sciences. 98(11). 6319–6324. 90 indexed citations
5.
Soderling, Scott H., et al.. (2000). Cloning and characterization of PDE7B, a cAMP-specific phosphodiesterase. Proceedings of the National Academy of Sciences. 97(1). 472–476. 117 indexed citations
6.
Bragg, Philip D., Natalie A. Glavas, & Cynthia Hou. (1997). Mutation of Conserved Residues in the NADP(H)-Binding Domain of the Proton Translocating Pyridine Nucleotide Transhydrogenase ofEscherichia coli. Archives of Biochemistry and Biophysics. 338(1). 57–66. 22 indexed citations
7.
Glavas, Natalie A., Huiying Hou, & Philip D. Bragg. (1995). Organization in the Membrane of the N-Terminal Proton-Translocating Domain of the β Subunit of the Pyridine Nucleotide Transhydrogenase of Escherichia coli. Biochemical and Biophysical Research Communications. 214(1). 230–238. 15 indexed citations
8.
Glavas, Natalie A. & Philip D. Bragg. (1995). The mechanism of hydride transfer between NADH and 3-acetylpyridine adenine dinucleotide by the pyridine nucleotide transhydrogenase of Escherichia coli. Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1231(3). 297–303. 31 indexed citations
9.
Glavas, Natalie A., Cynthia Hou, & Philip D. Bragg. (1995). Involvement of histidine-91 of the .beta. subunit in proton translocation by the pyridine nucleotide transhydrogenase of Escherichia coli. Biochemistry. 34(23). 7694–7702. 29 indexed citations
10.
11.
Ahmad, Suhail, Natalie A. Glavas, & Philip D. Bragg. (1993). Assembly of Multimeric Proteins. Journal of Molecular Biology. 234(1). 8–13. 14 indexed citations
12.
Hultman, Thomas, et al.. (1993). Site-directed mutagenesis of tyrosine residues at nicotinamide nucleotide binding sites of Escherichia coli transhydrogenase. Biochemistry. 32(48). 13237–13244. 26 indexed citations
13.
Glavas, Natalie A., Suhail Ahmad, Philip D. Bragg, Torbjörn Olausson, & Jan Rydström. (1993). Identification of N,N'-dicyclohexylcarbodiimide-reactive glutamic and aspartic acid residues in Escherichia coli transhydrogenase and the exchange of these by site-specific mutagenesis. Journal of Biological Chemistry. 268(19). 14125–14130. 25 indexed citations
14.
Ahmad, Suhail, Natalie A. Glavas, & Philip D. Bragg. (1992). A mutation at Gly314 of the β subunit of the Escherichia coli pyridine nucleotide transhydrogenase abolishes activity and affects the NADP(H)‐induced conformational change. European Journal of Biochemistry. 207(2). 733–739. 50 indexed citations
15.
Ahmad, Suhail, Natalie A. Glavas, & Philip D. Bragg. (1992). Subunit interactions involved in the assembly of pyridine nucleotide transhydrogenase in the membranes of Escherichia coli.. Journal of Biological Chemistry. 267(10). 7007–7012. 13 indexed citations
16.
Glavas, Natalie A., et al.. (1991). Topological analysis of the pyridine nucleotide transhydrogenase of Escherichia coli using proteolytic enzymes. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1080(1). 19–28. 51 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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