C. Craig Hyde

2.2k total citations · 1 hit paper
20 papers, 1.9k citations indexed

About

C. Craig Hyde is a scholar working on Molecular Biology, Materials Chemistry and Infectious Diseases. According to data from OpenAlex, C. Craig Hyde has authored 20 papers receiving a total of 1.9k indexed citations (citations by other indexed papers that have themselves been cited), including 14 papers in Molecular Biology, 10 papers in Materials Chemistry and 4 papers in Infectious Diseases. Recurrent topics in C. Craig Hyde's work include Enzyme Structure and Function (10 papers), Protein Structure and Dynamics (8 papers) and Biochemical and Molecular Research (6 papers). C. Craig Hyde is often cited by papers focused on Enzyme Structure and Function (10 papers), Protein Structure and Dynamics (8 papers) and Biochemical and Molecular Research (6 papers). C. Craig Hyde collaborates with scholars based in United States and Switzerland. C. Craig Hyde's co-authors include Edith Wilson Miles, David R. Davies, Salman Ahmed, Eduardo A. Padlan, Timothy C. Mueser, Nancy G. Nossal, Zhongning Yang, Sangkee Rhee, Stephen J. Stahl and Elena Alberdi and has published in prestigious journals such as Cell, Journal of Biological Chemistry and Nature Biotechnology.

In The Last Decade

C. Craig Hyde

20 papers receiving 1.8k citations

Hit Papers

align trajectories

What are hit papers?

Hit papers significantly outperform the citation benchmark for their cohort. A paper qualifies if it has ≥500 total citations, achieves ≥1.5× the top-1% citation threshold for papers in the same subfield and year (this is the minimum needed to enter the top 1%, not the average within it), or reaches the top citation threshold in at least one of its specific research topics.

Three-dimensional structure of the tryptophan synthase alpha 2 beta 2 multienzyme complex from Salmonella typhimurium.

1988 603 citations C. Craig Hyde, Salman Ahmed et al. Journal of Biological Chemistry profile →

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
C. Craig Hyde United States	19	1.5k	754	270	244	232	20	1.9k
Frédéric Dardel France	34	2.0k 1.3×	202 0.3×	149 0.6×	172 0.7×	147 0.6×	76	2.4k
Jay Painter United States	5	1.4k 0.9×	501 0.7×	68 0.3×	55 0.2×	175 0.8×	9	1.9k
Timothy C. Mueser United States	20	1.0k 0.7×	196 0.3×	67 0.2×	210 0.9×	203 0.9×	47	1.4k
Soumya S. Ray United States	27	1.4k 1.0×	272 0.4×	52 0.2×	236 1.0×	332 1.4×	41	2.2k
Denise M. Lowe United Kingdom	11	1.0k 0.7×	289 0.4×	49 0.2×	199 0.8×	217 0.9×	18	1.4k
Thomas Womack Netherlands	3	1.3k 0.9×	393 0.5×	69 0.3×	32 0.1×	159 0.7×	3	1.8k
François Hoh France	22	1.0k 0.7×	171 0.2×	41 0.2×	207 0.8×	183 0.8×	42	1.6k
Yeon Gyu Yu South Korea	20	790 0.5×	203 0.3×	95 0.4×	61 0.3×	88 0.4×	73	1.2k
Ray Yu‐Ruei Wang United States	10	1.9k 1.3×	464 0.6×	33 0.1×	59 0.2×	198 0.9×	10	2.5k
Stéfano Ricagno Italy	28	1.4k 1.0×	274 0.4×	74 0.3×	34 0.1×	220 0.9×	83	2.0k

Countries citing papers authored by C. Craig Hyde

Since Specialization

Citations

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

Fields of papers citing papers by C. Craig Hyde

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of C. Craig Hyde

This figure shows the co-authorship network connecting the top 25 collaborators of C. Craig Hyde. A scholar is included among the top collaborators of C. Craig Hyde 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 C. Craig Hyde. C. Craig Hyde 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

Nemes, Zoltán, et al.. (2001). Crystallization and Preliminary X-Ray Analysis of Human Transglutaminase 3 from Zymogen to Active Form. Journal of Structural Biology. 135(1). 73–77. 16 indexed citations

Mueser, Timothy C., Charles E. Jones, Nancy G. Nossal, & C. Craig Hyde. (2000). Bacteriophage T4 gene 59 helicase assembly protein binds replication fork DNA. The 1.45 Å resolution crystal structure reveals a novel α-helical two-domain fold 1 1Edited by P. E. Wright. Journal of Molecular Biology. 296(2). 597–612. 40 indexed citations

Yang, Zhongning, Timothy C. Mueser, Frederic D. Bushman, & C. Craig Hyde. (2000). Crystal structure of an active two-domain derivative of rous sarcoma virus integrase 1 1Edited by I. A. Wilson. Journal of Molecular Biology. 296(2). 535–548. 105 indexed citations

Yang, Zhongning, Timothy C. Mueser, Joshua D. Kaufman, et al.. (1999). The Crystal Structure of the SIV gp41 Ectodomain at 1.47 Å Resolution. Journal of Structural Biology. 126(2). 131–144. 109 indexed citations

Miroshnikov, Konstantin A., Elena Marusich, Mario E Cerritelli, et al.. (1998). Engineering trimeric fibrous proteins based on bacteriophage T4 adhesins. Protein Engineering Design and Selection. 11(4). 329–332. 45 indexed citations

Stahl, Stephen J., et al.. (1998). Purification of Recombinant Rous Sarcoma Virus Integrase Possessing Physical and Catalytic Properties Similar to Virion-Derived Integrase. Protein Expression and Purification. 14(2). 167–177. 19 indexed citations

Alberdi, Elena, C. Craig Hyde, & S. Patricia Becerra. (1998). Pigment Epithelium-Derived Factor (PEDF) Binds to Glycosaminoglycans: Analysis of the Binding Site. Biochemistry. 37(30). 10643–10652. 88 indexed citations

Vora, Ajaykumar C., Goodarz Goodarzi, Stephen J. Stahl, et al.. (1997). Avian Retrovirus U3 and U5 DNA Inverted Repeats. Journal of Biological Chemistry. 272(38). 23938–23945. 34 indexed citations

Wingfield, Paul T., Stephen J. Stahl, Joshua D. Kaufman, et al.. (1997). The extracellular domain of immunodeficiency virus gp41 protein: Expression inEscherichia coli, purification, and crystallization. Protein Science. 6(8). 1653–1660. 46 indexed citations

10.

Rhee, Sangkee, Kevin Parris, C. Craig Hyde, et al.. (1997). Crystal Structures of a Mutant (βK87T) Tryptophan Synthase α₂β₂ Complex with Ligands Bound to the Active Sites of the α- and β-Subunits Reveal Ligand-Induced Conformational Changes. Biochemistry. 36(25). 7664–7680. 111 indexed citations

11.

Rhee, Sangkee, C. Craig Hyde, P.H. Rogers, et al.. (1997). Refinement and Comparisons of the Crystal Structures of Pig Cytosolic Aspartate Aminotransferase and Its Complex with 2-Methylaspartate. Journal of Biological Chemistry. 272(28). 17293–17302. 91 indexed citations

12.

Mueser, Timothy C., Nancy G. Nossal, & C. Craig Hyde. (1996). Structure of Bacteriophage T4 RNase H, a 5′ to 3′ RNA–DNA and DNA–DNA Exonuclease with Sequence Similarity to the RAD2 Family of Eukaryotic Proteins. Cell. 85(7). 1101–1112. 157 indexed citations

13.

Brzović, Peter S., C. Craig Hyde, Edith Wilson Miles, & Michael F. Dunn. (1993). Characterization of the functional role of a flexible loop in the .alpha.-subunit of tryptophan synthase from Salmonella typhimurium by rapid-scanning, stopped-flow spectroscopy and site-directed mutagenesis. Biochemistry. 32(39). 10404–10413. 49 indexed citations

14.

Brzović, Peter S., Yoshihiro Sawa, C. Craig Hyde, Edith Wilson Miles, & Michael F. Dunn. (1992). Evidence that mutations in a loop region of the alpha-subunit inhibit the transition from an open to a closed conformation in the tryptophan synthase bienzyme complex.. Journal of Biological Chemistry. 267(18). 13028–13038. 69 indexed citations

15.

Wilmanns, Matthias, C. Craig Hyde, David R. Davies, Kasper Kirschner, & Johan N. Jansonius. (1991). Structural conservation in parallel .beta./.alpha.-barrel enzymes that catalyze three sequential reactions in the pathway of tryptophan biosynthesis. Biochemistry. 30(38). 9161–9169. 130 indexed citations

16.

Hyde, C. Craig & Edith Wilson Miles. (1990). The Tryptophan Synthase Multienzyme Complex: Exploring Structure-Function Relationships with X-Ray Crystallography and Mutagenesis. Nature Biotechnology. 8(1). 27–32. 38 indexed citations

17.

Nagata, Shigekazu, C. Craig Hyde, & Edith Wilson Miles. (1989). The α Subunit of Tryptophan Synthase. Journal of Biological Chemistry. 264(11). 6288–6296. 68 indexed citations

18.

Metzler, Carol M., David E. Metzler, Marvin W. Makinen, et al.. (1988). Correlation of polarized absorption spectroscopic and X-ray diffraction studies of crystalline cytosolic aspartate aminotransferase of pig hearts. Journal of Molecular Biology. 203(1). 197–220. 29 indexed citations

19.

Hyde, C. Craig, Salman Ahmed, Eduardo A. Padlan, Edith Wilson Miles, & David R. Davies. (1988). Three-dimensional structure of the tryptophan synthase alpha 2 beta 2 multienzyme complex from Salmonella typhimurium.. Journal of Biological Chemistry. 263(33). 17857–17871. 603 indexed citations breakdown →

20.

Hyde, C. Craig, et al.. (1987). Microcrystals of tryptophan synthase .alpha.2.beta.2 complex from Salmonella typhimurium are catalytically active. Biochemistry. 26(17). 5492–5498. 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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