Paul M. Horowitz

2.6k total citations
114 papers, 2.3k citations indexed

About

Paul M. Horowitz is a scholar working on Molecular Biology, Biochemistry and Cell Biology. According to data from OpenAlex, Paul M. Horowitz has authored 114 papers receiving a total of 2.3k indexed citations (citations by other indexed papers that have themselves been cited), including 63 papers in Molecular Biology, 31 papers in Biochemistry and 26 papers in Cell Biology. Recurrent topics in Paul M. Horowitz's work include Protein Structure and Dynamics (25 papers), Heat shock proteins research (25 papers) and Enzyme Structure and Function (24 papers). Paul M. Horowitz is often cited by papers focused on Protein Structure and Dynamics (25 papers), Heat shock proteins research (25 papers) and Enzyme Structure and Function (24 papers). Paul M. Horowitz collaborates with scholars based in United States, United Kingdom and Netherlands. Paul M. Horowitz's co-authors include Boris Gorovits, John Westley, Richard F. Ludueña, Don L. Gibbons, Nick L. Criscimagna, Markandeswar Panda, Jeffrey W. Seale, Dhirendra L. Nandi, Arkka Bhattacharyya and Gary P. Kurzban and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and Biochemistry.

In The Last Decade

Paul M. Horowitz

112 papers receiving 2.2k citations

Peers

Paul M. Horowitz

BIOCH

Domenico Bordo Italy

Irving Listowsky United States

Vladimir N. Kasho United States

Mary Ellen Jones United States

И. Н. Смирнова United States

Stephen A. Kuby United States

Eberhard Hofmann Germany

Gerhard Pfleiderer Germany

Marvin L. Hackert United States

C.L. Borders United States

Domenico Bordo Italy

Paul M. Horowitz

1.5k ×1.0

253 ×0.5

264 ×0.6

235 ×0.6

BIOCH

221 ×1.1

Citations per year, relative to Paul M. Horowitz Paul M. Horowitz (= 1×) peers Domenico Bordo

Countries citing papers authored by Paul M. Horowitz

Since Specialization

Citations

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

Fields of papers citing papers by Paul M. Horowitz

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Paul M. Horowitz. 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 Paul M. Horowitz. The network helps show where Paul M. Horowitz may publish in the future.

Co-authorship network of co-authors of Paul M. Horowitz

This figure shows the co-authorship network connecting the top 25 collaborators of Paul M. Horowitz. A scholar is included among the top collaborators of Paul M. Horowitz 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 Paul M. Horowitz. Paul M. Horowitz 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

Maîre, Jérôme, S. Wright, F. D. Drake, et al.. (2018). Panoramic optical and near-infrared SETI instrument: prototype design and testing. Ground-based and Airborne Instrumentation for Astronomy VII. 9147. 200–200. 6 indexed citations

Horowitz, Paul M., et al.. (2004). Active Rhodanese Lacking Nonessential Sulfhydryl Groups Has Increased Hydrophobic Exposure Not Observed in Wild-Type Enzyme. The Protein Journal. 23(4). 255–261. 2 indexed citations

Panda, Markandeswar & Paul M. Horowitz. (2004). Activation Parameters for the Spontaneous and Pressure-Induced Phases of the Dissociation of Single-Ring GroEL (SR1) Chaperonin. The Protein Journal. 23(1). 85–94. 2 indexed citations

Horowitz, Paul M.. (2003). Chaperonin-Assisted Protein Folding of the Enzyme Rhodanese by GroEL/GroES. Humana Press eBooks. 40. 361–368. 7 indexed citations

Bhattacharyya, Arkka, et al.. (2003). Active Rhodanese Lacking Nonessential Sulfhydryl Groups Contains an Unstable C-terminal Domain and Can Be Bound, Inactivated, and Reactivated by GroEL*. Journal of Biological Chemistry. 278(3). 1693–1699. 4 indexed citations

Kramer, Gisela, Vasanthi Ramachandiran, Paul M. Horowitz, & Britta Denise Hardesty. (2002). The molecular chaperone DnaK is not recruited to translating ribosomes that lack trigger factor. Archives of Biochemistry and Biophysics. 403(1). 63–70. 8 indexed citations

Kramer, Gisela, Vasanthi Ramachandiran, Paul M. Horowitz, & Britta Denise Hardesty. (2001). An Additional Serine Residue at the C Terminus of Rhodanese Destabilizes the Enzyme. Archives of Biochemistry and Biophysics. 385(2). 332–337. 6 indexed citations

Bhattacharyya, Arkka & Paul M. Horowitz. (2000). Alteration Around the Active Site of Rhodanese during Urea-induced Denaturation and Its Implications for Folding. Journal of Biological Chemistry. 275(20). 14860–14864. 16 indexed citations

Horowitz, Paul M., et al.. (1999). Nucleotide and Mg2+ Induced Conformational Changes in GroEL can be Detected by Sulfhydryl Labeling. Journal of Protein Chemistry. 18(3). 387–396. 7 indexed citations

10.

Cleland, Jeffrey L., et al.. (1997). Model Peptide Studies Demonstrate That Amphipathic Secondary Structures Can Be Recognized by the Chaperonin GroEL (cpn60). Journal of Biological Chemistry. 272(8). 5105–5111. 24 indexed citations

11.

Gorovits, Boris, et al.. (1997). Conditions for Nucleotide-dependent GroES-GroEL Interactions. Journal of Biological Chemistry. 272(43). 26999–27004. 10 indexed citations

12.

Gibbons, Don L., et al.. (1996). Intrinsic Fluorescence Studies of the Chaperonin GroEL Containing Single Tyr → Trp Replacements Reveal Ligand-induced Conformational Changes. Journal of Biological Chemistry. 271(50). 31989–31995. 9 indexed citations

13.

Horowitz, Paul M., et al.. (1995). Inactive GroEL Monomers Can Be Isolated and Reassembled to Functional Tetradecamers That Contain Few Bound Peptides. Journal of Biological Chemistry. 270(39). 22962–22967. 29 indexed citations

14.

Gibbons, Don L. & Paul M. Horowitz. (1995). Exposure of Hydrophobic Surfaces on the Chaperonin GroEL Oligomer by Protonation or Modification of His-401. Journal of Biological Chemistry. 270(13). 7335–7340. 19 indexed citations

15.

Seale, Jeffrey W., et al.. (1995). Photoincorporation of 4,4'-Bis(1-anilino-8-naphthalenesulfonic Acid) into the Apical Domain of GroEL: Specific Information from a Nonspecific Probe. Biochemistry. 34(22). 7443–7449. 33 indexed citations

16.

Gorovits, Boris, C.S. Raman, & Paul M. Horowitz. (1995). High Hydrostatic Pressure Induces the Dissociation of cpn60 Tetradecamers and Reveals a Plasticity of the Monomers. Journal of Biological Chemistry. 270(5). 2061–2066. 56 indexed citations

17.

Georgiou, George, Pascal Valax, Marc Ostermeier, & Paul M. Horowitz. (1994). Folding and aggregation of TEM β‐lactamase: Analogies with the formation of inclusion bodies in Escherichia coli. Protein Science. 3(11). 1953–1960. 56 indexed citations

18.

Miller, David M., Gary P. Kurzban, Jose A. Mendoza, et al.. (1992). Recombinant bovine rhodanese: purification and comparison with bovine liver rhodanese. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1121(3). 286–292. 39 indexed citations

19.

Mendoza, Jose A. & Paul M. Horowitz. (1992). Sulfhydryl modification ofE. coli cpn60 leads to loss of its ability to support refolding of rhodanese but not to form a binary complex. Journal of Protein Chemistry. 11(6). 589–594. 13 indexed citations

20.

Horowitz, Paul M., et al.. (1986). Ultranarrowband searches for extraterrestrial intelligence with dedicated signal-processing hardware. Icarus. 67(3). 525–539. 5 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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