Marvin L. Hackert

3.3k total citations
74 papers, 2.7k citations indexed

About

Marvin L. Hackert is a scholar working on Molecular Biology, Materials Chemistry and Biochemistry. According to data from OpenAlex, Marvin L. Hackert has authored 74 papers receiving a total of 2.7k indexed citations (citations by other indexed papers that have themselves been cited), including 40 papers in Molecular Biology, 27 papers in Materials Chemistry and 25 papers in Biochemistry. Recurrent topics in Marvin L. Hackert's work include Enzyme Structure and Function (24 papers), Amino Acid Enzymes and Metabolism (15 papers) and Polyamine Metabolism and Applications (15 papers). Marvin L. Hackert is often cited by papers focused on Enzyme Structure and Function (24 papers), Amino Acid Enzymes and Metabolism (15 papers) and Polyamine Metabolism and Applications (15 papers). Marvin L. Hackert collaborates with scholars based in United States, India and Switzerland. Marvin L. Hackert's co-authors include Lester J. Reed, S.R. Ernst, Marcos Antônio de Oliveira, Cory Momany, Robert A. Jacobson, Geoffrey C. Ford, Andrew D. Kern, Michael G. Rossmann, Margaret Adams and Manfred Buehner and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and Journal of Biological Chemistry.

In The Last Decade

Marvin L. Hackert

73 papers receiving 2.6k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Marvin L. Hackert United States 26 1.8k 971 715 424 375 74 2.7k
Florence Lederer France 33 3.3k 1.9× 622 0.6× 653 0.9× 246 0.6× 582 1.6× 145 4.2k
Ann Ginsburg United States 31 2.1k 1.2× 901 0.9× 1.2k 1.6× 322 0.8× 484 1.3× 88 3.3k
Herman Schreuder Germany 32 1.7k 1.0× 384 0.4× 527 0.7× 170 0.4× 198 0.5× 81 3.1k
Johan N. Jansonius Switzerland 39 3.7k 2.1× 1.4k 1.5× 2.3k 3.2× 373 0.9× 206 0.5× 68 4.8k
Victor L. Davidson United States 43 4.9k 2.8× 1.2k 1.2× 830 1.2× 203 0.5× 805 2.1× 223 5.9k
Geoffrey C. Ford United Kingdom 20 1.9k 1.1× 511 0.5× 1.2k 1.7× 275 0.6× 381 1.0× 38 2.9k
Kenneth W. Olsen United States 21 2.1k 1.2× 260 0.3× 868 1.2× 203 0.5× 634 1.7× 75 3.0k
Marino Martinez‐Carrion United States 32 2.0k 1.1× 892 0.9× 1.0k 1.4× 537 1.3× 357 1.0× 126 3.0k
Edith Wilson Miles United States 39 4.7k 2.7× 1.5k 1.5× 3.0k 4.2× 285 0.7× 503 1.3× 120 6.0k
Kai Tittmann Germany 37 1.7k 1.0× 1.8k 1.9× 444 0.6× 970 2.3× 177 0.5× 102 3.6k

Countries citing papers authored by Marvin L. Hackert

Since Specialization
Citations

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

Fields of papers citing papers by Marvin L. Hackert

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Marvin L. Hackert. 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 Marvin L. Hackert. The network helps show where Marvin L. Hackert may publish in the future.

Co-authorship network of co-authors of Marvin L. Hackert

This figure shows the co-authorship network connecting the top 25 collaborators of Marvin L. Hackert. A scholar is included among the top collaborators of Marvin L. Hackert 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 Marvin L. Hackert. Marvin L. Hackert 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.
Czerwiński, Robert, et al.. (2010). Kinetic and structural characterization of DmpI from Helicobacter pylori and Archaeoglobus fulgidus, two 4-oxalocrotonate tautomerase family members. Bioorganic Chemistry. 38(6). 252–259. 2 indexed citations
2.
Hoffman, David W., et al.. (2005). Solution Structure of a Conserved Domain of Antizyme:  A Protein Regulator of Polyamines,. Biochemistry. 44(35). 11777–11785. 19 indexed citations
3.
Hackert, Marvin L.. (2004). BioAdviser 1.0 -- High Performance Molecular Rendering and Analysis Software (Book). Journal of the American Chemical Society. 126(1). 407. 1 indexed citations
4.
Oliveira, Marcos Antônio de, et al.. (2000). Crystal structure of human ornithine decarboxylase at 2.1 å resolution: structural insights to antizyme binding. Journal of Molecular Biology. 295(1). 7–16. 118 indexed citations
5.
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Kern, Andrew D., Marcos Antônio de Oliveira, Philip Coffino, & Marvin L. Hackert. (1999). Structure of mammalian ornithine decarboxylase at 1.6 Å resolution: stereochemical implications of PLP-dependent amino acid decarboxylases. Structure. 7(5). 567–581. 128 indexed citations
7.
Vitali, Jacqueline, et al.. (1999). Three-dimensional structure of the Gly121Tyr dimeric form of ornithine decarboxylase from Lactobacillus 30a. Acta Crystallographica Section D Biological Crystallography. 55(12). 1978–1985. 13 indexed citations
8.
Knapp, James E., Marcos Antônio de Oliveira, Qiang Xie, et al.. (1999). The Structural and Functional Analysis of the Hemoglobin D Component from Chicken. Journal of Biological Chemistry. 274(10). 6411–6420. 53 indexed citations
9.
Knapp, James E., et al.. (1998). Crystal structure of the truncated cubic core component of the Escherichia coli 2-oxoglutarate dehydrogenase multienzyme complex. Journal of Molecular Biology. 280(4). 655–668. 61 indexed citations
10.
Kern, Andrew D., Marcos Antônio de Oliveira, Ning‐Leh Chang, et al.. (1996). Crystallization of a mammalian ornithine decarboxylase. Proteins Structure Function and Bioinformatics. 24(2). 266–268. 4 indexed citations
11.
Momany, Cory, S.R. Ernst, Ratna Ghosh, Ning‐Leh Chang, & Marvin L. Hackert. (1995). Crystallographic Structure of a PLP-Dependent Ornithine Decarboxylase fromLactobacillus30a to 3.0 Å Resolution. Journal of Molecular Biology. 252(5). 643–655. 101 indexed citations
12.
Mitchell, David, et al.. (1995). Three-dimensional structure of a hemichrome hemoglobin fromCaudina arenicola. Acta Crystallographica Section D Biological Crystallography. 51(5). 647–653. 4 indexed citations
13.
Mitchell, David, et al.. (1995). X-ray structure determination of a dimeric hemoglobin fromCaudina arenicola. Acta Crystallographica Section D Biological Crystallography. 51(5). 760–766. 4 indexed citations
14.
Mitchell, David, et al.. (1994). Crystallization of biosynthetic arginine decarboxylase from Escherichia coli. Acta Crystallographica Section D Biological Crystallography. 50(2). 175–177. 6 indexed citations
15.
Kolatkar, Prasanna R., Marvin L. Hackert, & Austen Riggs. (1994). Structural Analysis of Urechis caupo Hemoglobin. Journal of Molecular Biology. 237(1). 87–97. 12 indexed citations
16.
Kolatkar, Prasanna R., S.R. Ernst, Marvin L. Hackert, et al.. (1992). Structure determination and refinement of homotetrameric hemoglobin from Urechis caupo at 2.5 Å resolution. Acta Crystallographica Section B Structural Science. 48(2). 191–199. 16 indexed citations
17.
18.
Gallagher, Timothy, Michael J. Taylor, S.R. Ernst, Marvin L. Hackert, & N. S. Poonia. (1991). Dipotassium and sodium/potassium crystalline picrate complexes with the crown ether 6,7,9,10,12,13,20,21,23,24,26,27-dodecahydrodibenzo[b,n][1,4,7,10,13,16,19,22]octaoxacyclotetracosin (dibenzo-24-crown-8). Acta Crystallographica Section B Structural Science. 47(3). 362–368. 9 indexed citations
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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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