2017 - Member of the National Academy of Sciences
2014 - Fellow of the American Academy of Arts and Sciences
2007 - Fellow of the American Association for the Advancement of Science (AAAS)
2003 - Fellow of the MacArthur Foundation
Her primary areas of investigation include Biochemistry, Metallochaperones, Methylococcus capsulatus, Methane monooxygenase and Active site. Amy C. Rosenzweig regularly ties together related areas like Copper in her Biochemistry studies. Her Metallochaperones research incorporates elements of Amino acid, Superoxide dismutase, Biophysics, Peptide sequence and Metal ions in aqueous solution.
She combines subjects such as Inorganic chemistry, Hydroxide, Methylococcaceae and Methanobactin with her study of Methylococcus capsulatus. Her research on Methane monooxygenase often connects related areas such as Anaerobic oxidation of methane. As a part of the same scientific study, Amy C. Rosenzweig usually deals with the Binding site, concentrating on Histidine and frequently concerns with Stereochemistry, Side chain and Docking.
Her primary areas of study are Biochemistry, Methane monooxygenase, Stereochemistry, Copper and Crystallography. Her Methane monooxygenase research is multidisciplinary, incorporating perspectives in Methanotroph, Anaerobic oxidation of methane and Active site. Her biological study spans a wide range of topics, including Oxidoreductase, Ribonucleotide reductase, Protein subunit, Cofactor and Binding site.
Her research integrates issues of Metalloprotein, Molecule and Chaperone in her study of Copper. Her Crystallography study which covers Dimer that intersects with Molecular mass. In her research on the topic of Methylococcus capsulatus, Protomer is strongly related with Inorganic chemistry.
Her main research concerns Biochemistry, Methane monooxygenase, Enzyme, Methane and Anaerobic oxidation of methane. Her work carried out in the field of Methane monooxygenase brings together such families of science as Methanotroph, Active site, Copper, Copper protein and Binding site. Her Active site study incorporates themes from Pyridoxal, Inorganic chemistry, Crystal structure, Catalytic cycle and Combinatorial chemistry.
The Methane study combines topics in areas such as Natural gas, Methanol and Biochemical engineering. As part of one scientific family, Amy C. Rosenzweig deals mainly with the area of Methanol, narrowing it down to issues related to the Stereochemistry, and often Electron transfer and Dimer. Her work deals with themes such as Environmental chemistry, Oxidizing agent and Archaea, which intersect with Anaerobic oxidation of methane.
The scientist’s investigation covers issues in Methane monooxygenase, Enzyme, Active site, Biochemistry and Methane. The various areas that Amy C. Rosenzweig examines in her Methane monooxygenase study include Inorganic chemistry, Anaerobic oxidation of methane and Binding site. Her work on Substrate and Metalloprotein as part of her general Enzyme study is frequently connected to Cell-free protein synthesis, thereby bridging the divide between different branches of science.
Her studies in Active site integrate themes in fields like Combinatorial chemistry, Crystallography, Methanotroph and Copper. Her Copper research incorporates themes from Protein ligand, Molecule, Metal and Crystal structure. Her Methane research is multidisciplinary, relying on both Methanol and Natural gas.
This overview was generated by a machine learning system which analysed the scientist’s body of work. If you have any feedback, you can contact us here.
Crystal structure of a bacterial non-haem iron hydroxylase that catalyses the biological oxidation of methane
Amy C. Rosenzweig;Christin A. Frederick;Stephen J. Lippard;Pär Nordlund.
Nature (1993)
Crystal structure of double-stranded DNA containing the major adduct of the anticancer drug cisplatin
Patricia M. Takahara;Amy C. Rosenzweig;Christin A. Frederick;Stephen J. Lippard.
Nature (1995)
Nitrosopumilus maritimus genome reveals unique mechanisms for nitrification and autotrophy in globally distributed marine crenarchaea
C.B. Walker;J.R. De la Torre;M.G. Klotz;H. Urakawa.
Proceedings of the National Academy of Sciences of the United States of America (2010)
Crystal structure of a membrane-bound metalloenzyme that catalyses the biological oxidation of methane.
Raquel L. Lieberman;Amy C. Rosenzweig.
Nature (2005)
Oxidation of methane by a biological dicopper centre
Ramakrishnan Balasubramanian;Stephen M. Smith;Swati Rawat;Liliya A. Yatsunyk.
Nature (2010)
Geometry of the soluble methane monooxygenase catalytic diiron center in two oxidation states
Amy C. Rosenzweig;Pär Nordlund;Patricia M. Takahara;Christin A. Frederick.
Chemistry & Biology (1995)
Structural biology of copper trafficking.
Amie K. Boal;Amy C. Rosenzweig.
Chemical Reviews (2009)
Structural basis for copper transfer by the metallochaperone for the Menkes/Wilson disease proteins.
Amy K. Wernimont;David L. Huffman;Audrey L. Lamb;Thomas V. O'Halloran.
Nature Structural & Molecular Biology (2000)
The biochemistry of methane oxidation.
Amanda S Hakemian;Amy C Rosenzweig.
Annual Review of Biochemistry (2007)
Copper Delivery by Metallochaperone Proteins
Amy C. Rosenzweig.
Accounts of Chemical Research (2001)
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