John J. Osterhout

1.1k total citations
21 papers, 916 citations indexed

About

John J. Osterhout is a scholar working on Molecular Biology, Materials Chemistry and Physiology. According to data from OpenAlex, John J. Osterhout has authored 21 papers receiving a total of 916 indexed citations (citations by other indexed papers that have themselves been cited), including 19 papers in Molecular Biology, 8 papers in Materials Chemistry and 3 papers in Physiology. Recurrent topics in John J. Osterhout's work include Protein Structure and Dynamics (12 papers), Enzyme Structure and Function (8 papers) and Chemical Synthesis and Analysis (6 papers). John J. Osterhout is often cited by papers focused on Protein Structure and Dynamics (12 papers), Enzyme Structure and Function (8 papers) and Chemical Synthesis and Analysis (6 papers). John J. Osterhout collaborates with scholars based in United States. John J. Osterhout's co-authors include Alexander M. Klibanov, Tatyana Knubovets, Youcef Fezoui, Peter J. Connolly, D. L. Weaver, Peter E. Wright, H. Jane Dyson, Eunice J. York, Robert L. Baldwin and John M. Stewart 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

John J. Osterhout

21 papers receiving 885 citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
John J. Osterhout United States	15	758	298	97	93	81	21	916
G.G. Dodson United Kingdom	14	849 1.1×	268 0.9×	130 1.3×	116 1.2×	34 0.4×	23	1.3k
Luciana Esposito Italy	23	1.1k 1.5×	437 1.5×	97 1.0×	191 2.1×	89 1.1×	74	1.4k
Arimatti Jutila Finland	19	758 1.0×	95 0.3×	107 1.1×	122 1.3×	67 0.8×	28	984
Eric Hébert France	13	729 1.0×	221 0.7×	67 0.7×	32 0.3×	45 0.6×	25	1.1k
Peizhi Luo United States	8	785 1.0×	228 0.8×	124 1.3×	30 0.3×	46 0.6×	8	942
Weixin Xu Singapore	19	973 1.3×	190 0.6×	56 0.6×	299 3.2×	111 1.4×	27	1.2k
Paweł Krupa Poland	19	678 0.9×	403 1.4×	138 1.4×	87 0.9×	42 0.5×	47	865
Joseph A. Schauerte United States	15	514 0.7×	177 0.6×	59 0.6×	269 2.9×	91 1.1×	21	825
Radhakrishnan Mahalakshmi India	20	1.1k 1.5×	116 0.4×	133 1.4×	71 0.8×	114 1.4×	73	1.3k
A. J. Geddes United Kingdom	12	473 0.6×	145 0.5×	97 1.0×	135 1.5×	135 1.7×	22	740

Countries citing papers authored by John J. Osterhout

Since Specialization

Citations

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

Fields of papers citing papers by John J. Osterhout

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of John J. Osterhout

This figure shows the co-authorship network connecting the top 25 collaborators of John J. Osterhout. A scholar is included among the top collaborators of John J. Osterhout 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 J. Osterhout. John J. Osterhout is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

Sort: Min cites: Since: Top N: Style:

20 of 20 papers shown

Boyer, Leslie, et al.. (2006). Resistance of antivenom proteins to foaming-induced denaturation. Toxicon. 47(4). 445–452. 5 indexed citations

Xian, Wujing, et al.. (2006). Fundamental processes of protein folding: Measuring the energetic balance between helix formation and hydrophobic interactions. Protein Science. 15(9). 2062–2070. 12 indexed citations

Osterhout, John J.. (2005). Understanding Protein Folding Through Peptide Models. Protein and Peptide Letters. 12(2). 159–164. 11 indexed citations

Fezoui, Youcef, David B. Teplow, Dean M. Hartley, et al.. (2000). A de novo designed helix-turn-helix peptide forms nontoxic amyloid fibrils.. Nature Structural Biology. 7(12). 1095–1099. 112 indexed citations

Knubovets, Tatyana, John J. Osterhout, & Alexander M. Klibanov. (1999). Structure of lysozyme dissolved in neat organic solvents as assessed by NMR and CD spectroscopies. Biotechnology and Bioengineering. 63(2). 242–248. 83 indexed citations

Knubovets, Tatyana, John J. Osterhout, Peter J. Connolly, & Alexander M. Klibanov. (1999). Structure, thermostability, and conformational flexibility of hen egg-white lysozyme dissolved in glycerol. Proceedings of the National Academy of Sciences. 96(4). 1262–1267. 166 indexed citations

Fezoui, Youcef, Emory H. Braswell, Wujing Xian, & John J. Osterhout. (1999). Dissection of the de Novo Designed Peptide αtα: Stability and Properties of the Intact Molecule and Its Constituent Helices. Biochemistry. 38(9). 2796–2804. 19 indexed citations

Dyson, H. Jane, Lizann Bolinger, Victoria A. Feher, et al.. (1998). Sequence requirements for stabilization of a peptide reverse turn in water solution. European Journal of Biochemistry. 255(2). 462–471. 26 indexed citations

Choe, Sung, Paul Matsudaira, John J. Osterhout, Gerhard Wagner, & Eugene I. Shakhnovich. (1998). Folding Kinetics of Villin 14T, a Protein Domain with a Central β-Sheet and Two Hydrophobic Cores. Biochemistry. 37(41). 14508–14518. 23 indexed citations

10.

Fezoui, Youcef, Peter J. Connolly, & John J. Osterhout. (1997). Solution structure of αtα, a helical hairpin peptide of de novo design. Protein Science. 6(9). 1869–1877. 42 indexed citations

11.

Fezoui, Youcef, D. L. Weaver, & John J. Osterhout. (1995). Strategies and rationales for the de novo design of a helical hairpin peptide. Protein Science. 4(2). 286–295. 24 indexed citations

12.

Desai, Umesh R., John J. Osterhout, & Alexander M. Klibanov. (1994). Protein Structure in the Lyophilized State: A Hydrogen Isotope Exchange/NMR Study with Bovine Pancreatic Trypsin Inhibitor. Journal of the American Chemical Society. 116(21). 9420–9422. 52 indexed citations

13.

Fezoui, Youcef, D. L. Weaver, & John J. Osterhout. (1994). De novo design and structural characterization of an alpha-helical hairpin peptide: a model system for the study of protein folding intermediates.. Proceedings of the National Academy of Sciences. 91(9). 3675–3679. 64 indexed citations

14.

Osterhout, John J., Tracy M. Handel, Nebu Abraham George, et al.. (1992). Characterization of the structural properties of .alpha.1B, a peptide designed to form a four-helix bundle. Journal of the American Chemical Society. 114(1). 331–337. 47 indexed citations

15.

Osterhout, John J., Robert L. Baldwin, Eunice J. York, et al.. (1989). Proton NMR studies of the solution conformations of an analog of the C-peptide of ribonuclease A. Biochemistry. 28(17). 7059–7064. 131 indexed citations

16.

Nall, Barry T., John J. Osterhout, & Latha Ramdas. (1988). pH Dependence of folding of iso-2-cytochrome c. Biochemistry. 27(19). 7310–7314. 14 indexed citations

17.

Osterhout, John J., et al.. (1985). pH-Induced conformation changes and equilibrium unfolding in yeast iso-2 cytochrome c. Biochemistry. 24(23). 6680–6684. 13 indexed citations

18.

Osterhout, John J. & Barry T. Nall. (1985). Slow refolding kinetics in yeast iso-2 cytochrome c. Biochemistry. 24(27). 7999–8005. 20 indexed citations

19.

Osterhout, John J., S R Lax, & Joanne M. Ravel. (1983). Factors from wheat germ that enhance the activity of eukaryotic initiation factor eIF-2. Isolation and characterization of Co-eIF-2 alpha.. Journal of Biological Chemistry. 258(13). 8285–8289. 23 indexed citations

20.

Lax, S R, John J. Osterhout, & Joanne M. Ravel. (1982). Factors from wheat germ that enhance the activity of eukaryotic initiation factor eIF-2. Isolation and characterization of Co-eIF-2 beta.. Journal of Biological Chemistry. 257(14). 8233–8237. 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.

Explore authors with similar magnitude of impact