John F. Carpenter

3.5k total citations · 2 hit papers
15 papers, 2.9k citations indexed

About

John F. Carpenter is a scholar working on Molecular Biology, Food Science and Cell Biology. According to data from OpenAlex, John F. Carpenter has authored 15 papers receiving a total of 2.9k indexed citations (citations by other indexed papers that have themselves been cited), including 13 papers in Molecular Biology, 6 papers in Food Science and 3 papers in Cell Biology. Recurrent topics in John F. Carpenter's work include Protein purification and stability (11 papers), Proteins in Food Systems (5 papers) and Viral Infectious Diseases and Gene Expression in Insects (4 papers). John F. Carpenter is often cited by papers focused on Protein purification and stability (11 papers), Proteins in Food Systems (5 papers) and Viral Infectious Diseases and Gene Expression in Insects (4 papers). John F. Carpenter collaborates with scholars based in United States, United Kingdom and Denmark. John F. Carpenter's co-authors include John H. Crowe, Theodore W. Randolph, Tsutomu Arakawa, Byeong S. Chang, Michael J. Pikal, Steven J. Prestrelski, William C. Kenney, Thomas J. Anchordoquy, Mark C. Manning and Yoshiko Kita and has published in prestigious journals such as Biochemistry, Advanced Drug Delivery Reviews and Biochimica et Biophysica Acta (BBA) - Biomembranes.

In The Last Decade

John F. Carpenter

15 papers receiving 2.7k citations

Hit Papers

An infrared spectroscopic... 1989 2026 2001 2013 1989 1997 200 400 600

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
John F. Carpenter United States 15 2.0k 691 453 445 327 15 2.9k
Byeong S. Chang United States 22 2.5k 1.2× 627 0.9× 434 1.0× 736 1.7× 439 1.3× 26 3.2k
Steven J. Prestrelski United States 30 2.6k 1.3× 1.0k 1.5× 499 1.1× 379 0.9× 490 1.5× 54 4.2k
Brent S. Kendrick United States 29 2.3k 1.1× 330 0.5× 230 0.5× 796 1.8× 336 1.0× 60 3.0k
Xiaolin Tang United States 14 1.3k 0.6× 553 0.8× 601 1.3× 239 0.5× 569 1.7× 22 2.2k
Satoshi Ohtake United States 22 1.1k 0.6× 408 0.6× 319 0.7× 292 0.7× 171 0.5× 34 1.9k
Liuquan Chang United States 10 829 0.4× 379 0.5× 333 0.7× 252 0.6× 372 1.1× 12 1.4k
Thomas W. Patapoff United States 31 2.0k 1.0× 190 0.3× 258 0.6× 1.2k 2.7× 170 0.5× 65 2.9k
Sandeep Nema United States 14 1.7k 0.8× 192 0.3× 382 0.8× 837 1.9× 150 0.5× 23 2.2k
Robert J. Falconer Australia 29 1.1k 0.6× 555 0.8× 186 0.4× 176 0.4× 223 0.7× 75 2.6k
Daisuke Ejima Japan 34 3.3k 1.6× 379 0.5× 109 0.2× 1.3k 2.8× 455 1.4× 72 4.3k

Countries citing papers authored by John F. Carpenter

Since Specialization
Citations

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

Fields of papers citing papers by John F. Carpenter

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of John F. Carpenter

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

All Works

15 of 15 papers shown
1.
Arakawa, Tsutomu, Steven J. Prestrelski, William C. Kenney, & John F. Carpenter. (2001). Factors affecting short-term and long-term stabilities of proteins. Advanced Drug Delivery Reviews. 46(1-3). 307–326. 482 indexed citations
2.
Anchordoquy, Thomas J., Ken‐ichi Izutsu, Theodore W. Randolph, & John F. Carpenter. (2001). Maintenance of Quaternary Structure in the Frozen State Stabilizes Lactate Dehydrogenase during Freeze–Drying. Archives of Biochemistry and Biophysics. 390(1). 35–41. 93 indexed citations
3.
Meyer, Jeffrey D., et al.. (2000). Stability of Human Serum Albumin During Bioprocessing: Denaturation and Aggregation During Processing of Albumin Paste. Pharmaceutical Research. 17(4). 391–396. 35 indexed citations
4.
Heller, Martin, John F. Carpenter, & Theodore W. Randolph. (1999). Conformational Stability of Lyophilized PEGylated Proteins in a Phase-Separating System. Journal of Pharmaceutical Sciences. 88(1). 58–64. 28 indexed citations
5.
Yang, Tzung‐Horng, et al.. (1999). Use of infrared spectroscopy to assess secondary structure of human growth hormone within biodegradable microspheres. Journal of Pharmaceutical Sciences. 88(2). 161–165. 54 indexed citations
6.
Jones, LaToya S., Theodore W. Randolph, Sven Frøkjær, et al.. (1998). Effect of tween 20 on freeze-thawing- and agitation-induced aggregation of recombinant human factor XIII. Journal of Pharmaceutical Sciences. 87(12). 1597–1603. 194 indexed citations
7.
Allison, Steven, Theodore W. Randolph, Mark C. Manning, et al.. (1998). Effects of Drying Methods and Additives on Structure and Function of Actin: Mechanisms of Dehydration-Induced Damage and Its Inhibition. Archives of Biochemistry and Biophysics. 358(1). 171–181. 99 indexed citations
8.
Anchordoquy, Thomas J., et al.. (1998). Stability of lipid/DNA complexes during agitation and freeze–thawing. Journal of Pharmaceutical Sciences. 87(9). 1046–1051. 47 indexed citations
9.
Bam, Narendra B., Jeffrey L. Cleland, Mark C. Manning, et al.. (1998). Tween protects recombinant human growth hormone against agitation-induced damage via hydrophobic interactions. Journal of Pharmaceutical Sciences. 87(12). 1554–1559. 230 indexed citations
10.
Carpenter, John F., Michael J. Pikal, Byeong S. Chang, & Theodore W. Randolph. (1997). Rational Design of Stable Lyophilized Protein Formulations: Some Practical Advice. Pharmaceutical Research. 14(8). 969–975. 547 indexed citations breakdown →
11.
Anchordoquy, Thomas J. & John F. Carpenter. (1996). Polymers Protect Lactate Dehydrogenase during Freeze-Drying by Inhibiting Dissociation in the Frozen State. Archives of Biochemistry and Biophysics. 332(2). 231–238. 142 indexed citations
12.
Powers, Michael E., et al.. (1994). Thermal Stability of Low Molecular Weight Urokinase During Heat Treatment. II. Effect of Polymeric Additives. Pharmaceutical Research. 11(7). 1004–1008. 41 indexed citations
13.
Arakawa, Tsutomu, Yoshiko Kita, & John F. Carpenter. (1991). Protein–Solvent Interactions in Pharmaceutical Formulations. Pharmaceutical Research. 8(3). 285–291. 167 indexed citations
14.
Carpenter, John F. & John H. Crowe. (1989). An infrared spectroscopic study of the interactions of carbohydrates with dried proteins. Biochemistry. 28(9). 3916–3922. 633 indexed citations breakdown →
15.
Anchordoguy, Thomas J., John F. Carpenter, Stephen H. Loomis, & John H. Crowe. (1988). Mechanisms of interaction of amino acids with phospholipid bilayers during freezing. Biochimica et Biophysica Acta (BBA) - Biomembranes. 946(2). 299–306. 71 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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