J.P. Rose

876 total citations
27 papers, 726 citations indexed

About

J.P. Rose is a scholar working on Molecular Biology, Materials Chemistry and Cellular and Molecular Neuroscience. According to data from OpenAlex, J.P. Rose has authored 27 papers receiving a total of 726 indexed citations (citations by other indexed papers that have themselves been cited), including 25 papers in Molecular Biology, 12 papers in Materials Chemistry and 4 papers in Cellular and Molecular Neuroscience. Recurrent topics in J.P. Rose's work include Enzyme Structure and Function (8 papers), Protein Structure and Dynamics (7 papers) and bioluminescence and chemiluminescence research (4 papers). J.P. Rose is often cited by papers focused on Enzyme Structure and Function (8 papers), Protein Structure and Dynamics (7 papers) and bioluminescence and chemiluminescence research (4 papers). J.P. Rose collaborates with scholars based in United States, Russia and China. J.P. Rose's co-authors include Bi‐Cheng Wang, Lu Deng, B. G. Vekhter, R. Stephen Berry, Eugene S. Vysotski, Zhi‐Jie Liu, John Lee, Svetlana V. Markova, Dezhi Yang and Esther Breslow and has published in prestigious journals such as Proceedings of the National Academy of Sciences, The Journal of Chemical Physics and Journal of Molecular Biology.

In The Last Decade

J.P. Rose

26 papers receiving 705 citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
J.P. Rose United States	13	547	189	141	94	67	27	726
Jim E. Pitts United Kingdom	15	785 1.4×	267 1.4×	166 1.2×	11 0.1×	68 1.0×	37	1.0k
Georg Holtermann Germany	13	400 0.7×	39 0.2×	167 1.2×	46 0.5×	34 0.5×	21	671
Javier Farinas United States	14	1.1k 1.9×	181 1.0×	46 0.3×	213 2.3×	32 0.5×	20	1.6k
Kenta Yamada Japan	17	452 0.8×	114 0.6×	43 0.3×	36 0.4×	6 0.1×	52	1.2k
D. C. Harris United Kingdom	9	618 1.1×	58 0.3×	82 0.6×	29 0.3×	24 0.4×	16	1.2k
Norzehan Abdul-Manan United States	17	1.2k 2.1×	234 1.2×	114 0.8×	63 0.7×	13 0.2×	19	1.7k
Jakob T. Nielsen Denmark	21	999 1.8×	34 0.2×	239 1.7×	46 0.5×	9 0.1×	46	1.4k
Cristina Paulino Netherlands	18	1.1k 2.1×	302 1.6×	95 0.7×	56 0.6×	6 0.1×	30	1.4k
Siegfried Engelbrecht Germany	23	2.5k 4.6×	340 1.8×	104 0.7×	38 0.4×	9 0.1×	47	2.8k
Mrinal Shekhar United States	17	639 1.2×	150 0.8×	105 0.7×	27 0.3×	12 0.2×	30	938

Countries citing papers authored by J.P. Rose

Since Specialization

Citations

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

Fields of papers citing papers by J.P. Rose

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by J.P. Rose. 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 J.P. Rose. The network helps show where J.P. Rose may publish in the future.

Co-authorship network of co-authors of J.P. Rose

This figure shows the co-authorship network connecting the top 25 collaborators of J.P. Rose. A scholar is included among the top collaborators of J.P. Rose 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 J.P. Rose. J.P. Rose 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

Rose, J.P.. (2012). Effective Absorption Modeling in Relative Bioavailability Study Risk Assessment. The AAPS Journal. 14(4). 895–903. 3 indexed citations

Rose, J.P., et al.. (2008). Pushing the envelop of sulfur SAS structure determination at UGA/SER-CAT. Acta Crystallographica Section A Foundations of Crystallography. 64(a1). C179–C179.

Shaw, Neil, W. Tempel, Jessie Chang, et al.. (2007). Crystal structure solution of a ParB‐like nuclease at atomic resolution. Proteins Structure Function and Bioinformatics. 70(1). 263–267. 7 indexed citations

Shaw, Neil, Chongyun Cheng, W. Tempel, et al.. (2007). (NZ)CH...O Contacts assist crystallization of a ParB-like nuclease. BMC Structural Biology. 7(1). 46–46. 11 indexed citations

Kataeva, Irina, Jessie Chang, Hao Xu, et al.. (2005). Improving Solubility ofShewanellaoneidensisMR-1 andClostridiumthermocellumJW-20 Proteins Expressed intoEsherichiacoli. Journal of Proteome Research. 4(6). 1942–1951. 44 indexed citations

Deng, Lu, Eugene S. Vysotski, Svetlana V. Markova, et al.. (2005). All three Ca²⁺‐binding loops of photoproteins bind calcium ions: The crystal structures of calcium‐loaded apo‐aequorin and apo‐obelin. Protein Science. 14(3). 663–675. 78 indexed citations

Tempel, W., Zhi‐Jie Liu, P.S. Horanyi, et al.. (2005). Three‐dimesional structure of GlcNAcα1‐4Gal releasing Endo‐β‐Galactosidase from Clostridium perfringens. Proteins Structure Function and Bioinformatics. 59(1). 141–144. 9 indexed citations

Zhou, Weihong, Amaresh Das, Jeff E. Habel, et al.. (2005). Isolation, crystallization and preliminary X-ray analysis of a methanol-induced corrinoid protein fromMoorella thermoacetica. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 61(5). 537–540. 8 indexed citations

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

10.

Kataeva, Irina, Vladimir N. Uversky, John M. Brewer, et al.. (2004). Interactions between immunoglobulin-like and catalytic modules in Clostridium thermocellum cellulosomal cellobiohydrolase CbhA. Protein Engineering Design and Selection. 17(11). 759–769. 44 indexed citations

11.

Liu, Zhi‐Jie, Eugene S. Vysotski, Lu Deng, et al.. (2003). Atomic resolution structure of obelin: soaking with calcium enhances electron density of the second oxygen atom substituted at the C2-position of coelenterazine. Biochemical and Biophysical Research Communications. 311(2). 433–439. 53 indexed citations

12.

Schubot, Florian D., Chun‐Jung Chen, J.P. Rose, & Bi‐Cheng Wang. (2000). Crystallization and preliminary X-ray diffraction analysis of the mitochondrial transcription factor sc-mtTFB fromSaccharomyces cerevisiae. Acta Crystallographica Section D Biological Crystallography. 56(7). 902–903. 1 indexed citations

13.

Burden, Amy E., Tamara A. Dailey, Ish K. Dhawan, et al.. (1999). Human ferrochelatase: crystallization, characterization of the [2Fe-2S] cluster and determination that the enzyme is a homodimer. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1435(1-2). 191–197. 54 indexed citations

14.

Berry, R. Stephen, et al.. (1997). Linking topography of its potential surface with the dynamics of folding of a protein model. Proceedings of the National Academy of Sciences. 94(18). 9520–9524. 67 indexed citations

15.

Hempel, J, Zhijie Liu, John Perozich, et al.. (1996). Conserved Residues in the Aldehyde Dehydrogenase Family. Advances in experimental medicine and biology. 414. 9–13. 10 indexed citations

16.

Liu, Zhijie, J Hempel, J.P. Rose, et al.. (1996). Crystal Structure of a Class 3 Aldehyde Dehydrogenase at 2.6Å Resolution. Advances in experimental medicine and biology. 414. 1–7. 13 indexed citations

17.

Rose, J.P., et al.. (1994). A surface mutant (G82R) of a human α‐glutathione S‐transferase shows decreased thermal stability and a new mode of molecular association in the crystal. Proteins Structure Function and Bioinformatics. 20(3). 259–263. 5 indexed citations

18.

Rose, J.P., et al.. (1991). Crystals of a bovine neurophysin II tripeptide complex. Journal of Molecular Biology. 222(1). 23–25. 3 indexed citations

19.

Chen, Long‐Qing, J.P. Rose, Esther Breslow, et al.. (1991). Crystal structure of a bovine neurophysin II dipeptide complex at 2.8 A determined from the single-wavelength anomalous scattering signal of an incorporated iodine atom.. Proceedings of the National Academy of Sciences. 88(10). 4240–4244. 116 indexed citations

20.

Rose, J.P., J Hempel, Ingrid Kuo, Ronald Lindahl, & Bi‐Cheng Wang. (1990). Preliminary crystallographic analysis of class 3 rat liver aldehyde dehydrogenase. Proteins Structure Function and Bioinformatics. 8(4). 305–308. 18 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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