Edward C. Abresch
About
Edward C. Abresch is a scholar working on Molecular Biology, Atomic and Molecular Physics, and Optics and Renewable Energy, Sustainability and the Environment.
According to data from OpenAlex, Edward C. Abresch has authored 38 papers receiving a total of 2.3k indexed citations (citations by other indexed papers that have themselves been cited), including 36 papers in Molecular Biology, 15 papers in Atomic and Molecular Physics, and Optics and 11 papers in Renewable Energy, Sustainability and the Environment. Recurrent topics in Edward C. Abresch's work include Photosynthetic Processes and Mechanisms (28 papers), Spectroscopy and Quantum Chemical Studies (15 papers) and Metalloenzymes and iron-sulfur proteins (9 papers). Edward C. Abresch is often cited by papers focused on Photosynthetic Processes and Mechanisms (28 papers), Spectroscopy and Quantum Chemical Studies (15 papers) and Metalloenzymes and iron-sulfur proteins (9 papers). Edward C. Abresch collaborates with scholars based in United States, Israel and Germany. Edward C. Abresch's co-authors include G. Fehér, M. Y. Okamura, Douglas C. Rees, Timothy McPhillips, Michael H. B. Stowell, S. Michael Soltis, Mark L. Paddock, Herbert L. Axelrod, R. A. Isaacson and Wolfgang Lubitz 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
Edward C. Abresch
38 papers receiving 2.3k citations
Hit Papers
Peers
Edward C. Abresch
Curtis W. Hoganson United States
Warren F. Beck United States
R. A. Isaacson United States
Tony A. Mattioli France
Jeffrey M. Peloquin United States
Örjan Hansson Sweden
G. McDermott United Kingdom
Fraser MacMillan Germany
H. Komiya United States
Cecilia Tommos United States
Citations per year, relative to Edward C. Abresch Edward C. Abresch (= 1×)
peers
Curtis W. Hoganson
Countries citing papers authored by Edward C. Abresch
Since
Specialization
Citations
This map shows the geographic impact of Edward C. Abresch'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 Edward C. Abresch with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Edward C. Abresch more than expected).
Fields of papers citing papers by Edward C. Abresch
Since
Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences
This network shows the impact of papers produced by Edward C. Abresch. 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 Edward C. Abresch. The network helps show where Edward C. Abresch may publish in the future.
Co-authorship network of co-authors of Edward C. Abresch
This figure shows the co-authorship network connecting the top 25 collaborators of Edward C. Abresch. A scholar is included among the top collaborators of Edward C. Abresch 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 Edward C. Abresch. Edward C. Abresch is excluded from the visualization to improve readability, since they are connected to all nodes in the network.
All Works
1.
Conlan, Andrea R., Mark L. Paddock, Christina M. Homer, et al.. (2011). Mutation of the His ligand in mitoNEET stabilizes the 2Fe–2S cluster despite conformational heterogeneity in the ligand environment. Acta Crystallographica Section D Biological Crystallography. 67(6). 516–523.
2.
Homer, Christina M., Herbert L. Axelrod, Aina E. Cohen, et al.. (2009). Structural Basis for Phosphate Stabilization of the Uniquely Coordinated 2Fe-2S Cluster of the Outer Mitochondrial Membrane Protein MitoNEET.∗. Biophysical Journal. 96(3). 442a–443a.
3.
Zuris, John A., Mark L. Paddock, Edward C. Abresch, et al.. (2009). Redox Potential of the Outer-Mitochondrial Membrane 2Fe-2S Protein MitoNEET. Biophysical Journal. 96(3). 240a–240a.
4.
Conlan, Andrea R., Mark L. Paddock, Herbert L. Axelrod, et al.. (2009). The novel 2Fe–2S outer mitochondrial protein mitoNEET displays conformational flexibility in its N-terminal cytoplasmic tethering domain. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 65(7). 654–659.
5.
Conlan, Andrea R., Herbert L. Axelrod, Aina E. Cohen, et al.. (2009). Crystal Structure of Miner1: The Redox-active 2Fe-2S Protein Causative in Wolfram Syndrome 2. Journal of Molecular Biology. 392(1). 143–153.
6.
Conlan, Andrea R., Herbert L. Axelrod, Aina E. Cohen, et al.. (2009). Structural Comparison Of A Diabetes Drug Target, Mitoneet, A 2Fe-2S Cluster Protein To Its More Stable Mutant, H87C. Biophysical Journal. 96(3). 67a–67a.
7.
Paddock, M. L., R. A. Isaacson, Edward C. Abresch, & M. Y. Okamura. (2007). Light-induced EPR spectra of reaction centers fromRhodobacter sphaeroides at 80 K: Evidence for reduction of QB by B branch electron transfer in native reaction centers. Applied Magnetic Resonance. 31(1-2). 29–43.
8.
Paddock, Mark L., Sandra E. Wiley, Herbert L. Axelrod, et al.. (2007). MitoNEET is a uniquely folded 2Fe–2S outer mitochondrial membrane protein stabilized by pioglitazone. Proceedings of the National Academy of Sciences. 104(36). 14342–14347.
9.
Wiley, Sandra E., Mark L. Paddock, Edward C. Abresch, et al.. (2007). The Outer Mitochondrial Membrane Protein mitoNEET Contains a Novel Redox-active 2Fe-2S Cluster. Journal of Biological Chemistry. 282(33). 23745–23749.
10.
Flores, Marco, R. A. Isaacson, Edward C. Abresch, et al.. (2006). Protein-Cofactor Interactions in Bacterial Reaction Centers from Rhodobacter sphaeroides R-26: I. Identification of the ENDOR Lines Associated with the Hydrogen Bonds to the Primary Quinone Q A ⋅ −
11.
Flores, Marco, R. A. Isaacson, Edward C. Abresch, et al.. (2006). Protein-Cofactor Interactions in Bacterial Reaction Centers from Rhodobacter sphaeroides R-26: II. Geometry of the Hydrogen Bonds to the Primary Quinone Q A ⋅ −
12.
Paddock, M. L., Qiang Xu, Edward C. Abresch, et al.. (2005). Quinone (QB) Reduction by B-Branch Electron Transfer in Mutant Bacterial Reaction Centers fromRhodobacter sphaeroides: Quantum Efficiency and X-ray Structure,. Biochemistry. 44(18). 6920–6928.
13.
Xu, Qiang, Herbert L. Axelrod, Edward C. Abresch, et al.. (2004). X-Ray Structure Determination of Three Mutants of the Bacterial Photosynthetic Reaction Centers from Rb. sphaeroides. Structure. 12(4). 703–715.
15.
Axelrod, Herbert L., Edward C. Abresch, M. Y. Okamura, et al.. (2002). X-ray Structure Determination of the Cytochrome c2: Reaction Center Electron Transfer Complex from Rhodobacter sphaeroides. Journal of Molecular Biology. 319(2). 501–515.
16.
Abresch, Edward C., M. L. Paddock, Michael H. B. Stowell, et al.. (1998). Identification of proton transfer pathways in the X-ray crystal structure of the bacterial reaction center from Rhodobacter sphaeroides. Photosynthesis Research. 55(2-3). 119–125.
17.
Stowell, Michael H. B., Timothy McPhillips, Douglas C. Rees, et al.. (1997). Light-Induced Structural Changes in Photosynthetic Reaction Center: Implications for Mechanism of Electron-Proton Transfer. Science. 276(5313). 812–816.
18.
Huber, Martina, R. A. Isaacson, Edward C. Abresch, et al.. (1996). Electronic structure of the oxidized primary electron donor of the HL (M202) and HL (L173) heterodimer mutants of the photosynthetic bacterium Rhodobacter sphaeroides: ENDOR on single crystals of reaction centers. Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1273(2). 108–128.
19.
Isaacson, R. A., Friedhelm Lendzian, Edward C. Abresch, Wolfgang Lubitz, & G. Fehér. (1995). Electronic structure of Q-A in reaction centers from Rhodobacter sphaeroides. I. Electron paramagnetic resonance in single crystals. Biophysical Journal. 69(2). 311–322.
20.
Paddock, Mark L., S. H. Rongey, Edward C. Abresch, G. Fehér, & M. Y. Okamura. (1988). Reaction centers from three herbicide-resistant mutants of Rhodobacter sphaeroides 2.4.1: sequence analysis and preliminary characterization. Photosynthesis Research. 17(1-2). 75–96.
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