John W. Shriver

2.2k total citations
54 papers, 1.8k citations indexed

About

John W. Shriver is a scholar working on Molecular Biology, Materials Chemistry and Cardiology and Cardiovascular Medicine. According to data from OpenAlex, John W. Shriver has authored 54 papers receiving a total of 1.8k indexed citations (citations by other indexed papers that have themselves been cited), including 44 papers in Molecular Biology, 26 papers in Materials Chemistry and 10 papers in Cardiology and Cardiovascular Medicine. Recurrent topics in John W. Shriver's work include Enzyme Structure and Function (25 papers), Protein Structure and Dynamics (20 papers) and DNA and Nucleic Acid Chemistry (13 papers). John W. Shriver is often cited by papers focused on Enzyme Structure and Function (25 papers), Protein Structure and Dynamics (20 papers) and DNA and Nucleic Acid Chemistry (13 papers). John W. Shriver collaborates with scholars based in United States, Canada and Taiwan. John W. Shriver's co-authors include Stephen P. Edmondson, Bradford S. McCrary, Brian D. Sykes, Andrew H.‐J. Wang, Yi‐Gui Gao, Howard Robinson, Tessa Gordon, R. B. Stein, James G. McAfee and Andrew Clark and has published in prestigious journals such as Nature, Journal of the American Chemical Society and Journal of Biological Chemistry.

In The Last Decade

John W. Shriver

54 papers receiving 1.8k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
John W. Shriver United States 26 1.4k 468 263 228 194 54 1.8k
Vincent Forge France 31 1.8k 1.3× 626 1.3× 208 0.8× 61 0.3× 367 1.9× 46 2.5k
S. Trakhanov United States 22 1.8k 1.3× 300 0.6× 412 1.6× 113 0.5× 54 0.3× 31 2.1k
William E. Meador United States 14 1.9k 1.3× 821 1.8× 132 0.5× 192 0.8× 332 1.7× 29 2.6k
Kazuya Hasegawa Japan 25 1.3k 0.9× 495 1.1× 147 0.6× 91 0.4× 91 0.5× 84 2.1k
Ulrich Zachariae United Kingdom 27 2.0k 1.4× 209 0.4× 199 0.8× 224 1.0× 274 1.4× 70 2.6k
Ray Yu‐Ruei Wang United States 10 1.9k 1.3× 464 1.0× 209 0.8× 68 0.3× 78 0.4× 10 2.5k
Thorsten Dieckmann United States 27 1.7k 1.2× 149 0.3× 164 0.6× 70 0.3× 213 1.1× 58 2.1k
Johnny Habchi United Kingdom 32 1.9k 1.3× 410 0.9× 137 0.5× 46 0.2× 204 1.1× 57 3.1k
N. Nevskaya Russia 21 1.5k 1.1× 324 0.7× 240 0.9× 51 0.2× 192 1.0× 46 1.9k
Dmitri N. Ermolenko United States 25 2.5k 1.7× 297 0.6× 394 1.5× 201 0.9× 67 0.3× 49 2.7k

Countries citing papers authored by John W. Shriver

Since Specialization
Citations

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

Fields of papers citing papers by John W. Shriver

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by John W. Shriver. 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 John W. Shriver. The network helps show where John W. Shriver may publish in the future.

Co-authorship network of co-authors of John W. Shriver

This figure shows the co-authorship network connecting the top 25 collaborators of John W. Shriver. A scholar is included among the top collaborators of John W. Shriver 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 John W. Shriver. John W. Shriver 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.
Edmondson, Stephen P., et al.. (2016). Insights into the Structure of Sulfolobus Nucleoid Using Engineered Sac7d Dimers with a Defined Orientation. Biochemistry. 55(45). 6230–6237. 2 indexed citations
2.
Shriver, John W. & Stephen P. Edmondson. (2008). Defining the Stability of Multimeric Proteins. Methods in molecular biology. 490. 57–82. 13 indexed citations
3.
Shriver, John W. & Stephen P. Edmondson. (2008). Ligand-Binding Interactions and Stability. Methods in molecular biology. 490. 135–164. 9 indexed citations
4.
Clark, Andrew, et al.. (2007). Carboxyl pKa Values, Ion Pairs, Hydrogen Bonding, and the pH-dependence of Folding the Hyperthermophile Proteins Sac7d and Sso7d. Journal of Molecular Biology. 372(4). 992–1008. 29 indexed citations
5.
Chen, Liqing, Yujun Wang, Andrew Clark, et al.. (2004). The Hyperthermophile Protein Sso10a is a Dimer of Winged Helix DNA-binding Domains Linked by an Antiparallel Coiled Coil Rod. Journal of Molecular Biology. 341(1). 73–91. 30 indexed citations
6.
Edmondson, Stephen P., et al.. (2004). Thermodynamics of DNA Binding and Distortion by the Hyperthermophile Chromatin Protein Sac7d. Journal of Molecular Biology. 343(2). 339–360. 41 indexed citations
7.
Edmondson, Stephen P., et al.. (2003). Cloning, expression, crystallization and preliminary X-ray analysis of the DNA-binding protein Sso10a fromSulfolobus solfataricus. Acta Crystallographica Section D Biological Crystallography. 59(7). 1320–1322. 3 indexed citations
8.
Shriver, John W., et al.. (2001). [31] Calorimetric analyses of hyperthermophile proteins. Methods in enzymology on CD-ROM/Methods in enzymology. 334. 389–422. 10 indexed citations
9.
Gao, Yi‐Gui, Howard Robinson, Yen‐Chywan Liaw, et al.. (2000). Crystal structures of the chromosomal proteins Sso7d/Sac7d bound to DNA containing T-G mismatched base-pairs. Journal of Molecular Biology. 303(3). 395–403. 32 indexed citations
10.
McCrary, Bradford S., et al.. (2000). The acid‐induced folded state of Sac7d is the native state. Protein Science. 9(10). 1878–1888. 14 indexed citations
11.
Robinson, Howard, Yi‐Gui Gao, Bradford S. McCrary, et al.. (1998). The hyperthermophile chromosomal protein Sac7d sharply kinks DNA. Nature. 392(6672). 202–205. 173 indexed citations
12.
Gao, Yi‐Gui, Howard Robinson, Louis W. Lim, et al.. (1998). The crystal structure of the hyperthermophile chromosomal protein Sso7d bound to DNA. Nature Structural Biology. 5(9). 782–786. 125 indexed citations
13.
McCrary, Bradford S., et al.. (1998). Linkage of protonation and anion binding to the folding of Sac7d. Journal of Molecular Biology. 276(1). 203–224. 46 indexed citations
14.
McCrary, Bradford S., Stephen P. Edmondson, & John W. Shriver. (1996). Hyperthermophile Protein Folding Thermodynamics: Differential Scanning Calorimetry and Chemical Denaturation of Sac7d. Journal of Molecular Biology. 264(4). 784–805. 137 indexed citations
15.
McAfee, James G., Stephen P. Edmondson, Prasun K. Datta, John W. Shriver, & Ramesh C. Gupta. (1995). Gene Cloning, Expression, and Characterization of the Sac7 Proteins from the Hyperthermophile Sulfolobus acidocaldarius. Biochemistry. 34(31). 10063–10077. 66 indexed citations
16.
Edmondson, Stephen P., et al.. (1995). Solution Structure of the DNA-Binding Protein Sac7d from the Hyperthermophile Sulfolobus acidocaldarius. Biochemistry. 34(41). 13289–13304. 59 indexed citations
17.
Shriver, John W. & Stephen P. Edmondson. (1993). Defining the precision with which a protein structure is determined by NMR. Application to motilin. Biochemistry. 32(6). 1610–1617. 13 indexed citations
18.
Ehrenberg, Anders, et al.. (1990). Sequence-specific proton NMR assignments and secondary structure of porcine motilin. Biochemistry. 29(24). 5743–5751. 30 indexed citations
19.
Shriver, John W., et al.. (1990). Differential scanning calorimetry of the unfolding of myosin subfragment 1, subfragment 2, and heavy meromyosin. Biochemistry. 29(10). 2556–2564. 36 indexed citations
20.
Shriver, John W., E. W. Abrahamson, & Gheorghe D. Mateescu. (1976). The structure of visual pigments. I. Carbon-13 nuclear magnetic resonance spectroscopy of N-all-trans-retinylidenepropylimine and its protonated species. Journal of the American Chemical Society. 98(9). 2407–2409. 27 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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