Jose A. Mendoza

942 total citations
28 papers, 838 citations indexed

About

Jose A. Mendoza is a scholar working on Molecular Biology, Materials Chemistry and Cell Biology. According to data from OpenAlex, Jose A. Mendoza has authored 28 papers receiving a total of 838 indexed citations (citations by other indexed papers that have themselves been cited), including 21 papers in Molecular Biology, 15 papers in Materials Chemistry and 11 papers in Cell Biology. Recurrent topics in Jose A. Mendoza's work include Heat shock proteins research (15 papers), Enzyme Structure and Function (15 papers) and Aldose Reductase and Taurine (9 papers). Jose A. Mendoza is often cited by papers focused on Heat shock proteins research (15 papers), Enzyme Structure and Function (15 papers) and Aldose Reductase and Taurine (9 papers). Jose A. Mendoza collaborates with scholars based in United States. Jose A. Mendoza's co-authors include Peleg Horowitz, George H. Lorimer, Edwin W. Rogers, Gustavo Zardeneta, Girish C. Melkani, Borries Demeler, Terri Warren, Paul M. Horowitz, Michael B. Jarstfer and David P. Goldenberg and has published in prestigious journals such as Journal of Biological Chemistry, Biochemistry and Biochemical and Biophysical Research Communications.

In The Last Decade

Jose A. Mendoza

28 papers receiving 825 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Jose A. Mendoza United States 14 715 421 161 93 49 28 838
Johan Zeelen Germany 17 921 1.3× 548 1.3× 88 0.5× 42 0.5× 53 1.1× 28 1.2k
Oscar P. Chilson United States 15 431 0.6× 95 0.2× 159 1.0× 120 1.3× 49 1.0× 32 777
Winfried Meining Germany 15 664 0.9× 361 0.9× 31 0.2× 23 0.2× 54 1.1× 24 826
Lynda Dieckman United States 10 691 1.0× 166 0.4× 80 0.5× 53 0.6× 18 0.4× 15 915
Ulrich Grau United States 8 608 0.9× 324 0.8× 77 0.5× 12 0.1× 80 1.6× 17 831
Thomas G. Warner United States 16 542 0.8× 60 0.1× 63 0.4× 105 1.1× 29 0.6× 29 749
Hiroko Ikushiro Japan 14 402 0.6× 114 0.3× 80 0.5× 28 0.3× 89 1.8× 21 513
Ganapathy N. Sarma United States 9 458 0.6× 76 0.2× 65 0.4× 39 0.4× 73 1.5× 21 638
Paul G. Blommel United States 12 584 0.8× 137 0.3× 48 0.3× 16 0.2× 31 0.6× 13 732
H. Groendijk Netherlands 11 399 0.6× 162 0.4× 34 0.2× 25 0.3× 84 1.7× 15 544

Countries citing papers authored by Jose A. Mendoza

Since Specialization
Citations

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

Fields of papers citing papers by Jose A. Mendoza

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Jose A. Mendoza. 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 Jose A. Mendoza. The network helps show where Jose A. Mendoza may publish in the future.

Co-authorship network of co-authors of Jose A. Mendoza

This figure shows the co-authorship network connecting the top 25 collaborators of Jose A. Mendoza. A scholar is included among the top collaborators of Jose A. Mendoza 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 Jose A. Mendoza. Jose A. Mendoza 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.
Mendoza, Jose A., et al.. (2021). The Hsp60 Protein of Helicobacter Pylori Exhibits Chaperone and ATPase Activities at Elevated Temperatures. MDPI (MDPI AG). 1(1). 19–25. 2 indexed citations
2.
Mendoza, Jose A., et al.. (2016). The Hsp60 protein of helicobacter pylori displays chaperone activity under acidic conditions. Biochemistry and Biophysics Reports. 9. 95–99. 9 indexed citations
3.
Mendoza, Jose A., et al.. (2012). GTP binds to α-crystallin and causes a significant conformational change. International Journal of Biological Macromolecules. 50(4). 895–898. 1 indexed citations
4.
Melkani, Girish C., et al.. (2008). Divalent cations stabilize GroEL under conditions of oxidative stress. Biochemical and Biophysical Research Communications. 368(3). 625–630. 4 indexed citations
5.
Melkani, Girish C., et al.. (2006). Protection of GroEL by its methionine residues against oxidation by hydrogen peroxide. Biochemical and Biophysical Research Communications. 347(2). 534–539. 8 indexed citations
6.
Melkani, Girish C., Gustavo Zardeneta, & Jose A. Mendoza. (2005). On the chaperonin activity of GroEL at heat-shock temperature. The International Journal of Biochemistry & Cell Biology. 37(7). 1375–1385. 11 indexed citations
7.
Melkani, Girish C., Gustavo Zardeneta, & Jose A. Mendoza. (2003). The ATPase activity of GroEL is supported at high temperatures by divalent cations that stabilize its structure. BioMetals. 16(3). 479–484. 21 indexed citations
8.
Melkani, Girish C., Gustavo Zardeneta, & Jose A. Mendoza. (2002). GroEL interacts transiently with oxidatively inactivated rhodanese facilitating its reactivation. Biochemical and Biophysical Research Communications. 294(4). 893–899. 8 indexed citations
9.
Zardeneta, Gustavo, et al.. (2000). α-Crystallin Facilitates the Reactivation of Hydrogen Peroxide-Inactivated Rhodanese. Biochemical and Biophysical Research Communications. 274(2). 461–466. 6 indexed citations
10.
11.
Mendoza, Jose A., et al.. (1996). Thermostabilization of enzymes by the chaperonin GroEL. Biotechnology Techniques. 10(7). 8 indexed citations
12.
Mendoza, Jose A., et al.. (1996). The ATPase Activity of Chaperonin GroEL Is Highly Stimulated at Elevated Temperatures. Biochemical and Biophysical Research Communications. 229(1). 271–274. 27 indexed citations
13.
Mendoza, Jose A., et al.. (1996). Ligand-induced Conformational Changes of GroEL Are Dependent on the Bound Substrate Polypeptide. Journal of Biological Chemistry. 271(27). 16344–16349. 18 indexed citations
14.
Mendoza, Jose A., et al.. (1995). Tetradecameric chaperonin 60 can be assembled in vitro from monomers in a process that is ATP independent. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1247(2). 209–214. 12 indexed citations
15.
Mendoza, Jose A., et al.. (1994). The chaperonin assisted and unassisted refolding of rhodanese can be modulated by its N-terminal peptide. Journal of Protein Chemistry. 13(1). 15–22. 6 indexed citations
16.
Mendoza, Jose A., Michael B. Jarstfer, & David P. Goldenberg. (1994). Effects of Amino Acid Replacements on the Reductive Unfolding Kinetics of Pancreatic Trypsin Inhibitor. Biochemistry. 33(5). 1143–1148. 43 indexed citations
17.
Mendoza, Jose A., et al.. (1993). Partially folded rhodanese or its N-terminal sequence can disrupt phospholipid vesicles. Journal of Protein Chemistry. 12(1). 65–69. 6 indexed citations
18.
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
19.
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
20.
Mendoza, Jose A., Edwin W. Rogers, George H. Lorimer, & Peleg Horowitz. (1991). Chaperonins facilitate the in vitro folding of monomeric mitochondrial rhodanese. Journal of Biological Chemistry. 266(20). 13044–13049. 268 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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