Michelle A. Pressler

1.1k total citations
14 papers, 910 citations indexed

About

Michelle A. Pressler is a scholar working on Molecular Biology, Cellular and Molecular Neuroscience and Atomic and Molecular Physics, and Optics. According to data from OpenAlex, Michelle A. Pressler has authored 14 papers receiving a total of 910 indexed citations (citations by other indexed papers that have themselves been cited), including 10 papers in Molecular Biology, 7 papers in Cellular and Molecular Neuroscience and 3 papers in Atomic and Molecular Physics, and Optics. Recurrent topics in Michelle A. Pressler's work include Photosynthetic Processes and Mechanisms (10 papers), Photoreceptor and optogenetics research (7 papers) and Mitochondrial Function and Pathology (4 papers). Michelle A. Pressler is often cited by papers focused on Photosynthetic Processes and Mechanisms (10 papers), Photoreceptor and optogenetics research (7 papers) and Mitochondrial Function and Pathology (4 papers). Michelle A. Pressler collaborates with scholars based in United States, Sweden and Greece. Michelle A. Pressler's co-authors include Ǵerald Babcock, Denis A. Proshlyakov, David L. DeWitt, Joseph F. Leykam, Jonathan P. Hosler, Michael J. Maroney, Roberta O. Day, Shaukat A. Mirza, Melyssa R. Bratton and Manoj Kumar and has published in prestigious journals such as Science, Proceedings of the National Academy of Sciences and Journal of the American Chemical Society.

In The Last Decade

Michelle A. Pressler

14 papers receiving 893 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Michelle A. Pressler United States 12 641 282 262 151 142 14 910
Julia Behr Germany 8 739 1.2× 329 1.2× 170 0.6× 72 0.5× 100 0.7× 10 922
Bo G. Malmstroem Sweden 8 428 0.7× 213 0.8× 129 0.5× 32 0.2× 113 0.8× 8 612
Alain Desbois France 21 605 0.9× 101 0.4× 199 0.8× 86 0.6× 253 1.8× 46 1.1k
W. Anthony Oertling United States 17 551 0.9× 93 0.3× 223 0.9× 59 0.4× 316 2.2× 31 881
Vaithianathan Palaniappan United States 14 482 0.8× 153 0.5× 205 0.8× 56 0.4× 676 4.8× 20 1.2k
Dragan M. Popović United States 16 640 1.0× 346 1.2× 112 0.4× 30 0.2× 124 0.9× 25 884
Malin Abrahamsson Sweden 9 548 0.9× 193 0.7× 242 0.9× 236 1.6× 345 2.4× 12 1.1k
Jean‐Luc Zimmermann France 18 947 1.5× 377 1.3× 309 1.2× 145 1.0× 136 1.0× 29 1.2k
Giovanni Giacometti Italy 17 651 1.0× 180 0.6× 76 0.3× 79 0.5× 255 1.8× 59 1.1k

Countries citing papers authored by Michelle A. Pressler

Since Specialization
Citations

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

Fields of papers citing papers by Michelle A. Pressler

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Michelle A. Pressler

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

All Works

14 of 14 papers shown
1.
Oertling, W. Anthony, Charisa D. Cornellison, Nathan R. Treff, et al.. (2006). Photoacoustic characterization of protein dynamics following CO photodetachment from fully reduced bovine cytochrome c oxidase. Journal of Inorganic Biochemistry. 101(4). 635–643. 1 indexed citations
2.
Proshlyakov, Denis A., et al.. (2000). Oxygen Activation and Reduction in Respiration: Involvement of Redox-Active Tyrosine 244. Science. 290(5496). 1588–1591. 249 indexed citations
3.
Bratton, Melyssa R., Michelle A. Pressler, & Jonathan P. Hosler. (1999). Suicide Inactivation of Cytochrome c Oxidase:  Catalytic Turnover in the Absence of Subunit III Alters the Active Site. Biochemistry. 38(49). 16236–16245. 57 indexed citations
4.
Hoganson, Curtis W., Michelle A. Pressler, Denis A. Proshlyakov, & Ǵerald Babcock. (1998). From water to oxygen and back again: mechanistic similarities in the enzymatic redox conversion between water and dioxygen. Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1365(1-2). 170–174. 23 indexed citations
5.
Colpas, Gerard J., Timothy G. Brayman, John McCracken, et al.. (1998). Spectroscopic characterization of metal binding by Klebsiella aerogenes UreE urease accessory protein. JBIC Journal of Biological Inorganic Chemistry. 3(2). 150–160. 32 indexed citations
6.
Proshlyakov, Denis A., Michelle A. Pressler, & Ǵerald Babcock. (1998). Dioxygen activation and bond cleavage by mixed-valence cytochrome c oxidase. Proceedings of the National Academy of Sciences. 95(14). 8020–8025. 259 indexed citations
7.
Qian, Jie, Wenjun Shi, Michelle A. Pressler, et al.. (1997). Aspartate-407 in Rhodobacter sphaeroides Cytochrome c Oxidase Is Not Required for Proton Pumping or Manganese Binding. Biochemistry. 36(9). 2539–2543. 29 indexed citations
8.
Mitchell, David M., Pia Ädelroth, Jonathan P. Hosler, et al.. (1996). A Ligand-Exchange Mechanism of Proton Pumping Involving Tyrosine-422 of Subunit I of Cytochrome Oxidase Is Ruled Out. Biochemistry. 35(3). 824–828. 7 indexed citations
9.
Hosler, Jonathan P., James P. Shapleigh, David M. Mitchell, et al.. (1996). Polar Residues in Helix VIII of Subunit I of Cytochrome c Oxidase Influence the Activity and the Structure of the Active Site. Biochemistry. 35(33). 10776–10783. 73 indexed citations
10.
Babcock, Ǵerald, René Floris, T. Nilsson, et al.. (1996). Dioxygen activation in enzymatic systems and in inorganic models. Inorganica Chimica Acta. 243(1-2). 345–353. 21 indexed citations
11.
Mitchell, David M., John Fetter, Denise A. Mills, et al.. (1996). Site-Directed Mutagenesis of Residues Lining a Putative Proton Transfer Pathway in Cytochrome c Oxidase from Rhodobacter sphaeroides. Biochemistry. 35(40). 13089–13093. 31 indexed citations
12.
Choudhury, Suranjan Bhanja, Michelle A. Pressler, Shaukat A. Mirza, Roberta O. Day, & Michael J. Maroney. (1994). Structure and Redox Chemistry of Analogous Nickel Thiolato and Selenolato Complexes: Implications for the Nickel Sites in Hydrogenases. Inorganic Chemistry. 33(22). 4831–4839. 47 indexed citations
13.
Mirza, Shaukat A., Michelle A. Pressler, Manoj Kumar, Roberta O. Day, & Michael J. Maroney. (1993). Oxidation of nickel thiolate ligands by dioxygen. Inorganic Chemistry. 32(6). 977–987. 69 indexed citations
14.
Wilker, Jonathan J., Andrew Gelasco, Michelle A. Pressler, Roberta O. Day, & Michael J. Maroney. (1991). Coupled carbon-hydrogen bond heterolysis and tautomerism in a nickel macrocyclic complex with a thiolate ligand. Journal of the American Chemical Society. 113(16). 6342–6343. 12 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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