Ingrid C. Deckman

2.0k total citations
26 papers, 1.1k citations indexed

About

Ingrid C. Deckman is a scholar working on Molecular Biology, Genetics and Virology. According to data from OpenAlex, Ingrid C. Deckman has authored 26 papers receiving a total of 1.1k indexed citations (citations by other indexed papers that have themselves been cited), including 12 papers in Molecular Biology, 7 papers in Genetics and 6 papers in Virology. Recurrent topics in Ingrid C. Deckman's work include Virus-based gene therapy research (6 papers), Herpesvirus Infections and Treatments (6 papers) and RNA and protein synthesis mechanisms (6 papers). Ingrid C. Deckman is often cited by papers focused on Virus-based gene therapy research (6 papers), Herpesvirus Infections and Treatments (6 papers) and RNA and protein synthesis mechanisms (6 papers). Ingrid C. Deckman collaborates with scholars based in United States, Germany and Netherlands. Ingrid C. Deckman's co-authors include David E. Draper, P.J. McCann, Richard J. Colonno, Christine Debouck, Donald R. O’Boyle, Carolyn L. DiIanni, Sandra Feuer DiTusa, Thomas D. Meek, Jay C. Brown and Warren Hurlburt and has published in prestigious journals such as Nucleic Acids Research, Journal of Biological Chemistry and Journal of Molecular Biology.

In The Last Decade

Ingrid C. Deckman

26 papers receiving 1.1k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Ingrid C. Deckman United States 20 530 412 208 203 141 26 1.1k
Kurt Morgenstern United States 13 849 1.6× 515 1.3× 112 0.5× 117 0.6× 293 2.1× 19 1.8k
Gary W. Smythers United States 18 845 1.6× 181 0.4× 240 1.2× 324 1.6× 173 1.2× 33 1.4k
Alan M. Schultz United States 18 849 1.6× 235 0.6× 308 1.5× 476 2.3× 168 1.2× 27 1.5k
Yoshinao Kubo Japan 18 296 0.6× 244 0.6× 158 0.8× 210 1.0× 162 1.1× 69 1.1k
S.W. Ember United Kingdom 12 457 0.9× 216 0.5× 174 0.8× 234 1.2× 87 0.6× 15 853
Colin E. McVey Portugal 13 604 1.1× 180 0.4× 165 0.8× 122 0.6× 58 0.4× 26 891
Valeri Metelev Russia 17 942 1.8× 163 0.4× 132 0.6× 370 1.8× 150 1.1× 51 1.4k
William Markland United States 20 1.1k 2.0× 441 1.1× 137 0.7× 95 0.5× 288 2.0× 31 2.0k
Larry J. Ross United States 21 737 1.4× 249 0.6× 201 1.0× 145 0.7× 445 3.2× 32 1.6k
Dawn Nowlin United States 15 497 0.9× 477 1.2× 216 1.0× 54 0.3× 99 0.7× 21 1.2k

Countries citing papers authored by Ingrid C. Deckman

Since Specialization
Citations

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

Fields of papers citing papers by Ingrid C. Deckman

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Ingrid C. Deckman. 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 Ingrid C. Deckman. The network helps show where Ingrid C. Deckman may publish in the future.

Co-authorship network of co-authors of Ingrid C. Deckman

This figure shows the co-authorship network connecting the top 25 collaborators of Ingrid C. Deckman. A scholar is included among the top collaborators of Ingrid C. Deckman 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 Ingrid C. Deckman. Ingrid C. Deckman 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.
Kervinen, Jukka, Carl Crysler, Shariff Bayoumy, et al.. (2010). Potency variation of small-molecule chymase inhibitors across species. Biochemical Pharmacology. 80(7). 1033–1041. 21 indexed citations
2.
Darrow, Andrew L., Matthew W. Olson, Xin Hong, et al.. (2010). A novel fluorogenic substrate for the measurement of endothelial lipase activity. Journal of Lipid Research. 52(2). 374–382. 22 indexed citations
3.
Kranz, James K., Winnie Chan, Geoffrey T. Struble, et al.. (2007). Enhancing Recombinant Protein Quality and Yield by Protein Stability Profiling. SLAS DISCOVERY. 12(3). 418–428. 71 indexed citations
4.
Schalk‐Hihi, Céline, Hongchang Ma, Geoffrey T. Struble, et al.. (2006). Protein Engineering of the Colony-stimulating Factor-1 Receptor Kinase Domain for Structural Studies. Journal of Biological Chemistry. 282(6). 4085–4093. 10 indexed citations
5.
Schubert, Carsten J., Céline Schalk‐Hihi, Geoffrey T. Struble, et al.. (2006). Crystal Structure of the Tyrosine Kinase Domain of Colony-stimulating Factor-1 Receptor (cFMS) in Complex with Two Inhibitors. Journal of Biological Chemistry. 282(6). 4094–4101. 56 indexed citations
6.
Kervinen, Jukka, Hongchang Ma, Shariff Bayoumy, et al.. (2006). Effect of construct design on MAPKAP kinase-2 activity, thermodynamic stability and ligand-binding affinity. Archives of Biochemistry and Biophysics. 449(1-2). 47–56. 15 indexed citations
7.
Qiao, Lei, Christian A. Baumann, Carl Crysler, et al.. (2005). Discovery, SAR, and X-ray structure of novel biaryl-based dipeptidyl peptidase IV inhibitors. Bioorganic & Medicinal Chemistry Letters. 16(1). 123–128. 34 indexed citations
8.
Rudolph, Matthias, Carl R. Illig, Nalin L. Subasinghe, et al.. (2002). Design and Synthesis of 4,5-Disubstituted-thiophene-2-amidines as Potent Urokinase Inhibitors. Bioorganic & Medicinal Chemistry Letters. 12(3). 491–495. 23 indexed citations
9.
Stebbins, Jeffrey W., Eric M. Towler, Mike Tennant, Ingrid C. Deckman, & Christine Debouck. (1997). The 80’s loop (residues 78 to 85) is important for the differential activity of retroviral proteases 1 1Edited by A. R. Fresht. Journal of Molecular Biology. 267(3). 467–475. 10 indexed citations
10.
Stebbins, Jeffrey W., Ingrid C. Deckman, Susan B. Richardson, & Christine Debouck. (1996). A Heterologous Substrate Assay for the HIV-1 Protease Engineered inEscherichia coli. Analytical Biochemistry. 242(1). 90–94. 8 indexed citations
11.
Yamanaka, Gregory, Carolyn L. DiIanni, Donald R. O’Boyle, et al.. (1995). Stimulation of the Herpes Simplex Virus Type I Protease by Antichaeotrophic Salts. Journal of Biological Chemistry. 270(50). 30168–30172. 29 indexed citations
12.
Debouck, Christine, et al.. (1993). Inhibitor binding to the Phe53Trp mutant of HIV-1 protease promotes conformational changes detectable by spectrofluorometry. Biochemistry. 32(14). 3557–3563. 35 indexed citations
13.
DiIanni, Carolyn L., Diana Drier, Ingrid C. Deckman, et al.. (1993). Identification of the herpes simplex virus-1 protease cleavage sites by direct sequence analysis of autoproteolytic cleavage products.. Journal of Biological Chemistry. 268(3). 2048–2051. 75 indexed citations
14.
Deckman, Ingrid C., Jeffrey S. Culp, Michael D. Minnich, et al.. (1992). Use of protein unfolding studies to determine the conformational and dimeric stabilities of HIV-1 and SIV proteases. Biochemistry. 31(39). 9491–9501. 78 indexed citations
15.
Deckman, Ingrid C., Michael D. Minnich, Jeffrey S. Culp, et al.. (1991). Purification and biochemical characterization of recombinant simian immunodeficiency virus protease and comparison to human immunodeficiency virus type 1 protease. Biochemistry. 30(34). 8424–8434. 42 indexed citations
16.
Reff, Mitchell E., et al.. (1989). Alterations in the pre-mRNA topology of the bovine growth hormone polyadenylation region decrease poly(A) site efficiency. Nucleic Acids Research. 17(17). 6983–6998. 17 indexed citations
17.
Draper, David E., et al.. (1988). [13] Physical studies of ribosomal protein—RNA interactions. Methods in enzymology on CD-ROM/Methods in enzymology. 164. 203–220. 51 indexed citations
18.
Deckman, Ingrid C. & David E. Draper. (1987). S4-α mRNA translation regulation complex. Journal of Molecular Biology. 196(2). 323–332. 49 indexed citations
19.
Deckman, Ingrid C., David E. Draper, & Mark S. Thomas. (1987). S4-α mRNA translation repression complex. Journal of Molecular Biology. 196(2). 313–322. 29 indexed citations
20.
Deckman, Ingrid C. & David E. Draper. (1985). Specific interaction between ribosomal protein S4 and the .alpha. operon messenger RNA. Biochemistry. 24(27). 7860–7865. 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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