Charles T. Rauch

16.7k total citations · 8 hit papers
33 papers, 14.1k citations indexed

About

Charles T. Rauch is a scholar working on Molecular Biology, Cell Biology and Immunology. According to data from OpenAlex, Charles T. Rauch has authored 33 papers receiving a total of 14.1k indexed citations (citations by other indexed papers that have themselves been cited), including 21 papers in Molecular Biology, 12 papers in Cell Biology and 8 papers in Immunology. Recurrent topics in Charles T. Rauch's work include Microtubule and mitosis dynamics (12 papers), Cell death mechanisms and regulation (5 papers) and Genetic Neurodegenerative Diseases (4 papers). Charles T. Rauch is often cited by papers focused on Microtubule and mitosis dynamics (12 papers), Cell death mechanisms and regulation (5 papers) and Genetic Neurodegenerative Diseases (4 papers). Charles T. Rauch collaborates with scholars based in United States, Canada and France. Charles T. Rauch's co-authors include Raymond G. Goodwin, Craig A. Smith, Carl J. March, Henning Walczak, Martin F. Wolfson, Roy A. Black, Jillian Nicholl, Wenie S. Din, Pamela J. Smolak and Terri Smith and has published in prestigious journals such as Nature, Science and Cell.

In The Last Decade

Charles T. Rauch

33 papers receiving 13.8k citations

Hit Papers

A metalloproteinase disin... 1990 2026 2002 2014 1997 1995 1999 1998 1994 500 1000 1.5k 2.0k 2.5k

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Charles T. Rauch United States 24 8.2k 5.3k 3.2k 2.6k 1.4k 33 14.1k
Carl J. March United States 38 6.5k 0.8× 6.6k 1.2× 3.2k 1.0× 1.7k 0.7× 1.9k 1.3× 60 15.2k
Roy A. Black United States 50 7.3k 0.9× 3.9k 0.7× 3.8k 1.2× 2.6k 1.0× 2.7k 1.9× 95 14.8k
Mathew A. Vadas Australia 69 9.2k 1.1× 4.4k 0.8× 2.2k 0.7× 3.7k 1.4× 1.9k 1.3× 207 17.4k
Shin Yonehara Japan 66 10.3k 1.3× 9.0k 1.7× 3.3k 1.0× 1.7k 0.6× 722 0.5× 172 18.7k
Martin Turner United Kingdom 67 7.8k 0.9× 8.6k 1.6× 2.7k 0.9× 3.7k 1.4× 1.6k 1.1× 208 17.6k
Chikao Morimoto United States 74 5.1k 0.6× 8.4k 1.6× 5.6k 1.7× 1.7k 0.6× 2.7k 1.9× 339 18.5k
Reiner Gentz United States 48 10.2k 1.2× 5.5k 1.0× 2.4k 0.8× 2.6k 1.0× 656 0.5× 88 15.3k
Tak W. Mak Canada 57 6.7k 0.8× 9.9k 1.9× 3.0k 0.9× 1.6k 0.6× 802 0.6× 115 16.9k
Joseph B. Bolen United States 71 6.8k 0.8× 7.8k 1.5× 4.1k 1.3× 935 0.4× 2.0k 1.4× 171 16.0k
Karen O’Rourke United States 39 15.5k 1.9× 7.8k 1.5× 3.5k 1.1× 4.3k 1.7× 517 0.4× 44 20.2k

Countries citing papers authored by Charles T. Rauch

Since Specialization
Citations

This map shows the geographic impact of Charles T. Rauch'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 Charles T. Rauch with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Charles T. Rauch more than expected).

Fields of papers citing papers by Charles T. Rauch

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Charles T. Rauch. 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 Charles T. Rauch. The network helps show where Charles T. Rauch may publish in the future.

Co-authorship network of co-authors of Charles T. Rauch

This figure shows the co-authorship network connecting the top 25 collaborators of Charles T. Rauch. A scholar is included among the top collaborators of Charles T. Rauch 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 Charles T. Rauch. Charles T. Rauch 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.
Ho, Joseph D., Matthew R. Lee, Charles T. Rauch, et al.. (2020). Structure-based, multi-targeted drug discovery approach to eicosanoid inhibition: Dual inhibitors of mPGES-1 and 5-lipoxygenase activating protein (FLAP). Biochimica et Biophysica Acta (BBA) - General Subjects. 1865(2). 129800–129800. 17 indexed citations
2.
Antonysamy, Stephen, Zahid Bonday, Robert M. Campbell, et al.. (2012). Crystal structure of the human PRMT5:MEP50 complex. Proceedings of the National Academy of Sciences. 109(44). 17960–17965. 256 indexed citations
3.
Galibert, Laurent, Geoffrey S. Diemer, Zhi Liu, et al.. (2005). Nectin-like Protein 2 Defines a Subset of T-cell Zone Dendritic Cells and Is a Ligand for Class-I-restricted T-cell-associated Molecule. Journal of Biological Chemistry. 280(23). 21955–21964. 146 indexed citations
4.
Jin, Guixian, Roy A. Black, Martin F. Wolfson, et al.. (2002). A Continuous Fluorimetric Assay for Tumor Necrosis Factor-α Converting Enzyme. Analytical Biochemistry. 302(2). 269–275. 51 indexed citations
5.
Holland, Pamela M., Alison Milne, Kirsten E. Garka, et al.. (2002). Purification, Cloning, and Characterization of Nek8, a Novel NIMA-related Kinase, and Its Candidate Substrate Bicd2. Journal of Biological Chemistry. 277(18). 16229–16240. 50 indexed citations
6.
Sprick, Martin R., Markus Weigand, Eva Rieser, et al.. (2000). FADD/MORT1 and Caspase-8 Are Recruited to TRAIL Receptors 1 and 2 and Are Essential for Apoptosis Mediated by TRAIL Receptor 2. Immunity. 12(6). 599–609. 678 indexed citations breakdown →
7.
Walczak, Henning, Robert E. Miller, K. Ariail, et al.. (1999). Tumoricidal activity of tumor necrosis factor–related apoptosis–inducing ligand in vivo. Nature Medicine. 5(2). 157–163. 2158 indexed citations breakdown →
8.
Peschon, Jacques J., Jennifer L. Slack, P. Linga Reddy, et al.. (1998). An Essential Role for Ectodomain Shedding in Mammalian Development. Science. 282(5392). 1281–1284. 1355 indexed citations breakdown →
9.
Comeau, Michael R., Richard D. Johnson, Robert DuBose, et al.. (1998). A Poxvirus-Encoded Semaphorin Induces Cytokine Production from Monocytes and Binds to a Novel Cellular Semaphorin Receptor, VESPR. Immunity. 8(4). 473–482. 206 indexed citations
10.
Black, Roy A., Charles T. Rauch, Carl J. Kozlosky, et al.. (1997). A metalloproteinase disintegrin that releases tumour-necrosis factor-α from cells. Nature. 385(6618). 729–733. 2557 indexed citations breakdown →
11.
Müllberg, Jürgen, Charles T. Rauch, Martin F. Wolfson, et al.. (1997). Further evidence for a common mechanism for shedding of cell surface proteins. FEBS Letters. 401(2-3). 235–238. 49 indexed citations
12.
Wiley, Steven R., Ken Schooley, Pamela J. Smolak, et al.. (1995). Identification and characterization of a new member of the TNF family that induces apoptosis. Immunity. 3(6). 673–682. 2479 indexed citations breakdown →
13.
Anderson, Dirk, Stewart D. Lyman, Allison M. Baird, et al.. (1990). Molecular cloning of mast cell growth factor, a hematopoietin that is active in both membrane bound and soluble forms. Cell. 63(1). 235–243. 745 indexed citations breakdown →
14.
Pirollet, Fabienne, Charles T. Rauch, Didier Job, & Robert L. Margolis. (1989). Monoclonal antibody to microtubule-associated STOP protein: affinity purification of neuronal STOP activity and comparison of antigen with activity in neuronal and nonneuronal cell extracts. Biochemistry. 28(2). 835–842. 41 indexed citations
15.
Margolis, Robert L., et al.. (1988). Monoclonal antibody identification of stop protein a 145 kda protein which induces microtubule cold stability and is present in axons and in neuroblast mitotic spindles. 3. 459. 1 indexed citations
16.
Job, Didier, Charles T. Rauch, & Robert L. Margolis. (1987). High concentrations of STOP protein induce a microtubule super-stable state. Biochemical and Biophysical Research Communications. 148(1). 429–434. 16 indexed citations
17.
Margolis, Robert L., Charles T. Rauch, & Didier Job. (1986). [17] Purification and assay of cold-stable microtubules and STOP protein. Methods in enzymology on CD-ROM/Methods in enzymology. 134. 160–170. 9 indexed citations
18.
Margolis, Robert L., Charles T. Rauch, & Didier Job. (1986). Purification and assay of a 145-kDa protein (STOP145) with microtubule-stabilizing and motility behavior.. Proceedings of the National Academy of Sciences. 83(3). 639–643. 73 indexed citations
19.
Job, Didier, Charles T. Rauch, Edmond H. Fischer, & Robert L. Margolis. (1982). Recycling of cold-stable microtubules: evidence that cold stability is due to substoichiometric polymer blocks. Biochemistry. 21(3). 509–515. 105 indexed citations
20.
Margolis, Robert L., Charles T. Rauch, & Leslie Wilson. (1980). Mechanism of colchicine-dimer addition to microtubule ends: implications for the microtubule polymerization mechanism. Biochemistry. 19(24). 5550–5557. 74 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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