| Year |
Citation |
Score |
| 2023 |
Tucci FJ, Jodts RJ, Hoffman BM, Rosenzweig AC. Product analog binding identifies the copper active site of particulate methane monooxygenase. Nature Catalysis. 6: 1194-1204. PMID 38187819 DOI: 10.1038/s41929-023-01051-x |
0.83 |
|
| 2023 |
Manesis AC, Slater JW, Cantave K, Martin Bollinger J, Krebs C, Rosenzweig AC. Capturing a -Fe(IV) State in OB3b MbnH. Biochemistry. 62: 1082-1092. PMID 36812111 DOI: 10.1021/acs.biochem.3c00021 |
0.507 |
|
| 2022 |
Schachner LF, Soye BD, Ro S, Kenney GE, Ives AN, Su T, Goo YA, Jewett MC, Rosenzweig AC, Kelleher NL. Revving an Engine of Human Metabolism: Activity Enhancement of Triosephosphate Isomerase via Hemi-Phosphorylation. Acs Chemical Biology. PMID 35951581 DOI: 10.1021/acschembio.2c00324 |
0.736 |
|
| 2022 |
Park YJ, Jodts RJ, Slater JW, Reyes RM, Winton VJ, Montaser RA, Thomas PM, Dowdle WB, Ruiz A, Kelleher NL, Bollinger JM, Krebs C, Hoffman BM, Rosenzweig AC. A mixed-valent Fe(II)Fe(III) species converts cysteine to an oxazolone/thioamide pair in methanobactin biosynthesis. Proceedings of the National Academy of Sciences of the United States of America. 119: e2123566119. PMID 35320042 DOI: 10.1073/pnas.2123566119 |
0.809 |
|
| 2021 |
Hadley RC, Zhitnitsky D, Livnat-Levanon N, Masrati G, Vigonsky E, Rose J, Ben-Tal N, Rosenzweig AC, Lewinson O. The copper-linked E. coli AZY operon: Structure, metal binding, and a possible physiological role in copper delivery. The Journal of Biological Chemistry. 101445. PMID 34822841 DOI: 10.1016/j.jbc.2021.101445 |
0.418 |
|
| 2021 |
Park YJ, Roberts GM, Montaser R, Kenney GE, Thomas PM, Kelleher NL, Rosenzweig AC. Characterization of a Copper-Chelating Natural Product from the Methanotroph sp. LW3. Biochemistry. PMID 34510894 DOI: 10.1021/acs.biochem.1c00443 |
0.762 |
|
| 2021 |
Jodts RJ, Ross MO, Koo CW, Doan PE, Rosenzweig AC, Hoffman BM. Coordination of the Copper Centers in Particulate Methane Monooxygenase: Comparison between Methanotrophs and Characterization of the Cu Site by EPR and ENDOR Spectroscopies. Journal of the American Chemical Society. PMID 34498465 DOI: 10.1021/jacs.1c07018 |
0.827 |
|
| 2021 |
Manesis AC, Jodts RJ, Hoffman BM, Rosenzweig AC. Copper binding by a unique family of metalloproteins is dependent on kynurenine formation. Proceedings of the National Academy of Sciences of the United States of America. 118. PMID 34074779 DOI: 10.1073/pnas.2100680118 |
0.852 |
|
| 2021 |
Cutsail GE, Ross MO, Rosenzweig AC, DeBeer S. Towards a unified understanding of the copper sites in particulate methane monooxygenase: an X-ray absorption spectroscopic investigation. Chemical Science. 12: 6194-6209. PMID 33996018 DOI: 10.1039/d1sc00676b |
0.754 |
|
| 2021 |
Koo CW, Rosenzweig AC. Biochemistry of aerobic biological methane oxidation. Chemical Society Reviews. PMID 33491685 DOI: 10.1039/d0cs01291b |
0.321 |
|
| 2019 |
Fisher OS, Sendzik MR, Ross MO, Lawton TJ, Hoffman BM, Rosenzweig AC. PCuC domains from methane-oxidizing bacteria use a histidine brace to bind copper. The Journal of Biological Chemistry. PMID 31527086 DOI: 10.1074/Jbc.Ra119.010093 |
0.811 |
|
| 2019 |
Kenney GE, Dassama LMK, Manesis AC, Ross MO, Chen S, Hoffman BM, Rosenzweig AC. MbnH is a diheme MauG-like protein associated with microbial copper homeostasis. The Journal of Biological Chemistry. PMID 31511324 DOI: 10.1074/Jbc.Ra119.010202 |
0.819 |
|
| 2019 |
Ro SY, Schachner LF, Koo CW, Purohit R, Remis JP, Kenney GE, Liauw BW, Thomas PM, Patrie SM, Kelleher NL, Rosenzweig AC. Native top-down mass spectrometry provides insights into the copper centers of membrane-bound methane monooxygenase. Nature Communications. 10: 2675. PMID 31209220 DOI: 10.1038/S41467-019-10590-6 |
0.803 |
|
| 2019 |
Ross MO, MacMillan F, Wang J, Nisthal A, Lawton TJ, Olafson BD, Mayo SL, Rosenzweig AC, Hoffman BM. Particulate methane monooxygenase contains only mononuclear copper centers. Science (New York, N.Y.). 364: 566-570. PMID 31073062 DOI: 10.1126/Science.Aav2572 |
0.798 |
|
| 2019 |
Ross MO, Fisher OS, Morgada MN, Krzyaniak MD, Wasielewski MR, Vila AJ, Hoffman BM, Rosenzweig AC. Formation and electronic structure of an atypical Cu site. Journal of the American Chemical Society. PMID 30807125 DOI: 10.1021/Jacs.8B13610 |
0.785 |
|
| 2018 |
Fisher OS, Kenney GE, Ross MO, Ro SY, Lemma BE, Batelu S, Thomas PM, Sosnowski VC, DeHart CJ, Kelleher NL, Stemmler TL, Hoffman BM, Rosenzweig AC. Characterization of a long overlooked copper protein from methane- and ammonia-oxidizing bacteria. Nature Communications. 9: 4276. PMID 30323281 DOI: 10.1038/s41467-018-06681-5 |
0.828 |
|
| 2018 |
Deng YW, Ro SY, Rosenzweig AC. Structure and function of the lanthanide-dependent methanol dehydrogenase XoxF from the methanotroph Methylomicrobium buryatense 5GB1C. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. PMID 30132076 DOI: 10.1007/S00775-018-1604-2 |
0.371 |
|
| 2018 |
Ro SY, Ross MO, Deng YW, Batelu S, Lawton TJ, Hurley JD, Stemmler TL, Hoffman BM, Rosenzweig AC. From micelles to bicelles: Effect of the membrane on particulate methane monooxygenase activity. The Journal of Biological Chemistry. PMID 29739854 DOI: 10.1074/Jbc.Ra118.003348 |
0.774 |
|
| 2018 |
Park YJ, Kenney GE, Schachner LF, Kelleher NL, Rosenzweig AC. Repurposed HisC Aminotransferases Complete the Biosynthesis of Some Methanobactins. Biochemistry. PMID 29694778 DOI: 10.1021/Acs.Biochem.8B00296 |
0.767 |
|
| 2018 |
Kenney GE, Rosenzweig AC. Chalkophores. Annual Review of Biochemistry. PMID 29668305 DOI: 10.1146/annurev-biochem-062917-012300 |
0.779 |
|
| 2018 |
Kenney GE, Dassama LMK, Pandelia ME, Gizzi AS, Martinie RJ, Gao P, DeHart CJ, Schachner LF, Skinner OS, Ro SY, Zhu X, Sadek M, Thomas PM, Almo SC, Bollinger JM, ... ... Rosenzweig AC, et al. The biosynthesis of methanobactin. Science (New York, N.Y.). 359: 1411-1416. PMID 29567715 DOI: 10.1126/Science.Aap9437 |
0.821 |
|
| 2018 |
Purohit R, Ross MO, Batelu S, Kusowski A, Stemmler TL, Hoffman BM, Rosenzweig AC. Cu-specific CopB transporter: Revising P-type ATPase classification. Proceedings of the National Academy of Sciences of the United States of America. PMID 29440418 DOI: 10.1073/Pnas.1721783115 |
0.797 |
|
| 2018 |
Kenney GE, Rosenzweig AC. Methanobactins: maintaining copper homeostasis in methanotrophs and beyond. The Journal of Biological Chemistry. PMID 29348173 DOI: 10.1074/Jbc.Tm117.000185 |
0.795 |
|
| 2017 |
Cao L, Caldararu O, Rosenzweig AC, Ryde U. Quantum refinement does not support dinuclear copper sites in crystal structures of particulate methane monooxygenase. Angewandte Chemie (International Ed. in English). PMID 29164769 DOI: 10.1002/Anie.201708977 |
0.451 |
|
| 2017 |
Rosenzweig AC. A biochemical sulfur delivery service. Science (New York, N.Y.). 358: 307-308. PMID 29051366 DOI: 10.1126/Science.Aap9299 |
0.317 |
|
| 2016 |
Smith AT, Ross MO, Hoffman BM, Rosenzweig AC. Metal Selectivity of a Cd-, Co-, and Zn-Transporting P1B-type ATPase. Biochemistry. PMID 28001366 DOI: 10.1021/Acs.Biochem.6B01022 |
0.806 |
|
| 2016 |
Dassama LM, Kenney GE, Rosenzweig AC. Methanobactins: from genome to function. Metallomics : Integrated Biometal Science. PMID 27905614 DOI: 10.1039/C6Mt00208K |
0.822 |
|
| 2016 |
Ross MO, Rosenzweig AC. A tale of two methane monooxygenases. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. PMID 27878395 DOI: 10.1007/S00775-016-1419-Y |
0.743 |
|
| 2016 |
Dassama LM, Kenney GE, Ro SY, Zielazinski EL, Rosenzweig AC. Methanobactin transport machinery. Proceedings of the National Academy of Sciences of the United States of America. PMID 27807137 DOI: 10.1073/Pnas.1603578113 |
0.805 |
|
| 2016 |
Lawton TJ, Rosenzweig AC. Biocatalysts for methane conversion: big progress on breaking a small substrate. Current Opinion in Chemical Biology. 35: 142-149. PMID 27768948 DOI: 10.1016/J.Cbpa.2016.10.001 |
0.306 |
|
| 2016 |
Trana EN, Nocek JM, Woude JV, Span I, Smith SM, Rosenzweig AC, Hoffman BM. Charge-Disproportionation Symmetry Breaking Creates a Heterodimeric Myoglobin Complex with Enhanced Affinity and Rapid Intracomplex Electron Transfer. Journal of the American Chemical Society. PMID 27646786 DOI: 10.1021/Jacs.6B07672 |
0.452 |
|
| 2016 |
Kenney GE, Goering AW, Ross MO, DeHart CJ, Thomas PM, Hoffman BM, Kelleher NL, Rosenzweig AC. Characterization of methanobactin from Methylosinus sp. LW4. Journal of the American Chemical Society. PMID 27527063 DOI: 10.1021/Jacs.6B06821 |
0.781 |
|
| 2016 |
Lawton TJ, Rosenzweig AC. Methane-oxidizing enzymes: An upstream problem in biological gas-to-liquids conversion. Journal of the American Chemical Society. PMID 27366961 DOI: 10.1021/Jacs.6B04568 |
0.329 |
|
| 2016 |
Kenney GE, Sadek M, Rosenzweig AC. Copper-responsive gene expression in the methanotroph Methylosinus trichosporium OB3b. Metallomics : Integrated Biometal Science. PMID 27087171 DOI: 10.1039/C5Mt00289C |
0.788 |
|
| 2016 |
Lawton TJ, Kenney GE, Hurley JD, Rosenzweig AC. The CopC Family: Structural and Bioinformatic Insights into a Diverse Group of Periplasmic Copper Binding Proteins. Biochemistry. PMID 27010565 DOI: 10.1021/Acs.Biochem.6B00175 |
0.813 |
|
| 2015 |
Kathman SG, Span I, Smith AT, Xu Z, Zhan J, Rosenzweig AC, Statsyuk AV. A Small Molecule That Switches a Ubiquitin Ligase From a Processive to a Distributive Enzymatic Mechanism. Journal of the American Chemical Society. 137: 12442-5. PMID 26371805 DOI: 10.1021/Jacs.5B06839 |
0.562 |
|
| 2015 |
Li J, Lawton TJ, Kostecki JS, Nisthal A, Fang J, Mayo SL, Rosenzweig AC, Jewett MC. Cell-free protein synthesis enables high yielding synthesis of an active multicopper oxidase. Biotechnology Journal. PMID 26356243 DOI: 10.1002/Biot.201500030 |
0.379 |
|
| 2015 |
Boal AK, Rosenzweig AC. Response from Boal and Rosenzweig to Crystallography and chemistry should always go together: a cautionary tale of protein complexes with cisplatin and carboplatin. Acta Crystallographica. Section D, Biological Crystallography. 71: 1984-6. PMID 26327389 DOI: 10.1107/S1399004715014352 |
0.589 |
|
| 2015 |
Smith AT, Barupala D, Stemmler TL, Rosenzweig AC. A new metal binding domain involved in cadmium, cobalt and zinc transport. Nature Chemical Biology. PMID 26192600 DOI: 10.1038/Nchembio.1863 |
0.647 |
|
| 2015 |
Sirajuddin S, Rosenzweig AC. Enzymatic oxidation of methane. Biochemistry. 54: 2283-94. PMID 25806595 DOI: 10.1021/Acs.Biochem.5B00198 |
0.412 |
|
| 2015 |
Kathman S, Span I, Smith AT, Xu Z, Zhan J, Rosenzweig AC, Statsyuk AV. Discovery and Structural Characterization of Covalent Inhibitors of Nedd4-1 Ubiquitin Ligase Processivity Journal of the American Chemical Society. DOI: 10.2210/Pdb5C91/Pdb |
0.562 |
|
| 2015 |
Smith AT, Barupala D, Stemmler TL, Rosenzweig AC. A new metal binding domain involved in cadmium, cobalt and zinc transport Nature Chemical Biology. DOI: 10.1038/nchembio.1863 |
0.578 |
|
| 2014 |
Culpepper MA, Rosenzweig AC. Structure and protein-protein interactions of methanol dehydrogenase from Methylococcus capsulatus (Bath). Biochemistry. 53: 6211-9. PMID 25185034 DOI: 10.1021/Bi500850J |
0.376 |
|
| 2014 |
Culpepper MA, Cutsail GE, Gunderson WA, Hoffman BM, Rosenzweig AC. Identification of the valence and coordination environment of the particulate methane monooxygenase copper centers by advanced EPR characterization. Journal of the American Chemical Society. 136: 11767-75. PMID 25059917 DOI: 10.1021/Ja5053126 |
0.614 |
|
| 2014 |
Sirajuddin S, Barupala D, Helling S, Marcus K, Stemmler TL, Rosenzweig AC. Effects of zinc on particulate methane monooxygenase activity and structure. The Journal of Biological Chemistry. 289: 21782-94. PMID 24942740 DOI: 10.1074/Jbc.M114.581363 |
0.453 |
|
| 2014 |
Silakov A, Grove TL, Radle MI, Bauerle MR, Green MT, Rosenzweig AC, Boal AK, Booker SJ. Characterization of a cross-linked protein-nucleic acid substrate radical in the reaction catalyzed by RlmN. Journal of the American Chemical Society. 136: 8221-8. PMID 24806349 DOI: 10.1021/Ja410560P |
0.614 |
|
| 2014 |
Smith AT, Smith KP, Rosenzweig AC. Diversity of the metal-transporting P1B-type ATPases. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 19: 947-60. PMID 24729073 DOI: 10.1007/S00775-014-1129-2 |
0.642 |
|
| 2014 |
Austin RN, Kenney GE, Rosenzweig AC. Perspective: what is known, and not known, about the connections between alkane oxidation and metal uptake in alkanotrophs in the marine environment. Metallomics : Integrated Biometal Science. 6: 1121-5. PMID 24710692 DOI: 10.1039/C4Mt00041B |
0.771 |
|
| 2014 |
Chang WC, Guo Y, Wang C, Butch SE, Rosenzweig AC, Boal AK, Krebs C, Bollinger JM. Mechanism of the C5 stereoinversion reaction in the biosynthesis of carbapenem antibiotics. Science (New York, N.Y.). 343: 1140-4. PMID 24604200 DOI: 10.1126/Science.1248000 |
0.761 |
|
| 2014 |
Lawton TJ, Ham J, Sun T, Rosenzweig AC. Structural conservation of the B subunit in the ammonia monooxygenase/particulate methane monooxygenase superfamily. Proteins. 82: 2263-7. PMID 24523098 DOI: 10.1002/Prot.24535 |
0.432 |
|
| 2014 |
Makhlynets O, Boal AK, Rhodes DV, Kitten T, Rosenzweig AC, Stubbe J. Streptococcus sanguinis class Ib ribonucleotide reductase: high activity with both iron and manganese cofactors and structural insights. The Journal of Biological Chemistry. 289: 6259-72. PMID 24381172 DOI: 10.1074/Jbc.M113.533554 |
0.665 |
|
| 2013 |
Zielazinski EL, González-Guerrero M, Subramanian P, Stemmler TL, Argüello JM, Rosenzweig AC. Sinorhizobium meliloti Nia is a P(1B-5)-ATPase expressed in the nodule during plant symbiosis and is involved in Ni and Fe transport. Metallomics : Integrated Biometal Science. 5: 1614-23. PMID 24056637 DOI: 10.1039/C3Mt00195D |
0.796 |
|
| 2013 |
Dassama LM, Krebs C, Bollinger JM, Rosenzweig AC, Boal AK. Structural basis for assembly of the Mn(IV)/Fe(III) cofactor in the class Ic ribonucleotide reductase from Chlamydia trachomatis. Biochemistry. 52: 6424-36. PMID 23924396 DOI: 10.1021/Bi400819X |
0.788 |
|
| 2013 |
Lawton TJ, Bowen KE, Sayavedra-Soto LA, Arp DJ, Rosenzweig AC. Characterization of a nitrite reductase involved in nitrifier denitrification. The Journal of Biological Chemistry. 288: 25575-83. PMID 23857587 DOI: 10.1074/Jbc.M113.484543 |
0.386 |
|
| 2013 |
Rosenzweig AC. Metalloenzymes: Put a ring on it. Nature Chemical Biology. 9: 220-1. PMID 23508187 DOI: 10.1038/Nchembio.1208 |
0.394 |
|
| 2013 |
Kenney GE, Rosenzweig AC. Genome mining for methanobactins. Bmc Biology. 11: 17. PMID 23442874 DOI: 10.1186/1741-7007-11-17 |
0.777 |
|
| 2012 |
Rosenzweig AC, Argüello JM. Toward a molecular understanding of metal transport by P(1B)-type ATPases. Current Topics in Membranes. 69: 113-36. PMID 23046649 DOI: 10.1016/B978-0-12-394390-3.00005-7 |
0.436 |
|
| 2012 |
Boal AK, Rosenzweig AC. Biochemistry. A radical route for nitrogenase carbide insertion. Science (New York, N.Y.). 337: 1617-8. PMID 23019640 DOI: 10.1126/Science.1229088 |
0.632 |
|
| 2012 |
Zielazinski EL, Cutsail GE, Hoffman BM, Stemmler TL, Rosenzweig AC. Characterization of a cobalt-specific P(1B)-ATPase. Biochemistry. 51: 7891-900. PMID 22971227 DOI: 10.1021/Bi3006708 |
0.798 |
|
| 2012 |
Culpepper MA, Rosenzweig AC. Architecture and active site of particulate methane monooxygenase. Critical Reviews in Biochemistry and Molecular Biology. 47: 483-92. PMID 22725967 DOI: 10.3109/10409238.2012.697865 |
0.443 |
|
| 2012 |
Culpepper MA, Cutsail GE, Hoffman BM, Rosenzweig AC. Evidence for oxygen binding at the active site of particulate methane monooxygenase. Journal of the American Chemical Society. 134: 7640-3. PMID 22540911 DOI: 10.1021/Ja302195P |
0.52 |
|
| 2012 |
Boal AK, Cotruvo JA, Stubbe J, Rosenzweig AC. The dimanganese(II) site of Bacillus subtilis class Ib ribonucleotide reductase. Biochemistry. 51: 3861-71. PMID 22443445 DOI: 10.1021/Bi201925T |
0.675 |
|
| 2012 |
Dassama LM, Boal AK, Krebs C, Rosenzweig AC, Bollinger JM. Evidence that the β subunit of Chlamydia trachomatis ribonucleotide reductase is active with the manganese ion of its manganese(IV)/iron(III) cofactor in site 1. Journal of the American Chemical Society. 134: 2520-3. PMID 22242660 DOI: 10.1021/Ja211314P |
0.795 |
|
| 2012 |
Kenney GE, Rosenzweig AC. Chemistry and biology of the copper chelator methanobactin. Acs Chemical Biology. 7: 260-8. PMID 22126187 DOI: 10.1021/Cb2003913 |
0.787 |
|
| 2011 |
Smith SM, Rawat S, Telser J, Hoffman BM, Stemmler TL, Rosenzweig AC. Crystal structure and characterization of particulate methane monooxygenase from Methylocystis species strain M. Biochemistry. 50: 10231-40. PMID 22013879 DOI: 10.1021/Bi200801Z |
0.58 |
|
| 2011 |
Balasubramanian R, Kenney GE, Rosenzweig AC. Dual pathways for copper uptake by methanotrophic bacteria. The Journal of Biological Chemistry. 286: 37313-9. PMID 21900235 DOI: 10.1074/Jbc.M111.284984 |
0.781 |
|
| 2011 |
Boal AK, Grove TL, McLaughlin MI, Yennawar NH, Booker SJ, Rosenzweig AC. Structural basis for methyl transfer by a radical SAM enzyme. Science (New York, N.Y.). 332: 1089-92. PMID 21527678 DOI: 10.1126/Science.1205358 |
0.616 |
|
| 2011 |
Lawton TJ, Rosenzweig AC. Detection and characterization of a multicopper oxidase from Nitrosomonas europaea. Methods in Enzymology. 496: 423-33. PMID 21514474 DOI: 10.1016/B978-0-12-386489-5.00017-8 |
0.316 |
|
| 2011 |
Smith SM, Balasubramanian R, Rosenzweig AC. Metal reconstitution of particulate methane monooxygenase and heterologous expression of the pmoB subunit. Methods in Enzymology. 495: 195-210. PMID 21419923 DOI: 10.1016/B978-0-12-386905-0.00013-9 |
0.351 |
|
| 2011 |
Benítez JJ, Keller AM, Huffman DL, Yatsunyk LA, Rosenzweig AC, Chen P. Relating dynamic protein interactions of metallochaperones with metal transfer at the single-molecule level. Faraday Discussions. 148: 71-82; discussion 97. PMID 21322478 DOI: 10.1039/C004913A |
0.409 |
|
| 2010 |
Boal AK, Cotruvo JA, Stubbe J, Rosenzweig AC. Structural basis for activation of class Ib ribonucleotide reductase. Science (New York, N.Y.). 329: 1526-30. PMID 20688982 DOI: 10.1126/Science.1190187 |
0.653 |
|
| 2010 |
Traverso ME, Subramanian P, Davydov R, Hoffman BM, Stemmler TL, Rosenzweig AC. Identification of a hemerythrin-like domain in a P1B-type transport ATPase. Biochemistry. 49: 7060-8. PMID 20672819 DOI: 10.1021/Bi100866B |
0.694 |
|
| 2010 |
Agarwal S, Hong D, Desai NK, Sazinsky MH, Argüello JM, Rosenzweig AC. Structure and interactions of the C-terminal metal binding domain of Archaeoglobus fulgidus CopA. Proteins. 78: 2450-8. PMID 20602459 DOI: 10.1002/Prot.22753 |
0.576 |
|
| 2010 |
Walker CB, de la Torre JR, Klotz MG, Urakawa H, Pinel N, Arp DJ, Brochier-Armanet C, Chain PS, Chan PP, Gollabgir A, Hemp J, Hügler M, Karr EA, Könneke M, Shin M, ... ... Rosenzweig AC, et al. Nitrosopumilus maritimus genome reveals unique mechanisms for nitrification and autotrophy in globally distributed marine crenarchaea. Proceedings of the National Academy of Sciences of the United States of America. 107: 8818-23. PMID 20421470 DOI: 10.1073/Pnas.0913533107 |
0.34 |
|
| 2010 |
Balasubramanian R, Smith SM, Rawat S, Yatsunyk LA, Stemmler TL, Rosenzweig AC. Oxidation of methane by a biological dicopper centre. Nature. 465: 115-9. PMID 20410881 DOI: 10.1038/Nature08992 |
0.453 |
|
| 2010 |
Ukaegbu UE, Kantz A, Beaton M, Gassner GT, Rosenzweig AC. Structure and ligand binding properties of the epoxidase component of styrene monooxygenase . Biochemistry. 49: 1678-88. PMID 20055497 DOI: 10.1021/Bi901693U |
0.808 |
|
| 2009 |
Rosenzweig AC. Bioinorganic chemistry: Zeroing in on a new copper site. Nature Chemistry. 1: 684-5. PMID 21124349 DOI: 10.1038/Nchem.456 |
0.447 |
|
| 2009 |
Boal AK, Rosenzweig AC. Structural biology of copper trafficking. Chemical Reviews. 109: 4760-79. PMID 19824702 DOI: 10.1021/Cr900104Z |
0.727 |
|
| 2009 |
Boal AK, Rosenzweig AC. Crystal structures of cisplatin bound to a human copper chaperone. Journal of the American Chemical Society. 131: 14196-7. PMID 19807176 DOI: 10.1021/Ja906363T |
0.689 |
|
| 2009 |
Barker KD, Eckermann AL, Sazinsky MH, Hartings MR, Abajian C, Georganopoulou D, Ratner MA, Rosenzweig AC, Meade TJ. Protein binding and the electronic properties of iron(II) complexes: an electrochemical and optical investigation of outer sphere effects. Bioconjugate Chemistry. 20: 1930-9. PMID 19788194 DOI: 10.1021/Bc900270A |
0.808 |
|
| 2009 |
Ukaegbu UE, Rosenzweig AC. Structure of the redox sensor domain of Methylococcus capsulatus (Bath) MmoS. Biochemistry. 48: 2207-15. PMID 19271777 DOI: 10.1021/Bi8019614 |
0.782 |
|
| 2009 |
Lawton TJ, Sayavedra-Soto LA, Arp DJ, Rosenzweig AC. Crystal structure of a two-domain multicopper oxidase: implications for the evolution of multicopper blue proteins. The Journal of Biological Chemistry. 284: 10174-80. PMID 19224923 DOI: 10.1074/Jbc.M900179200 |
0.42 |
|
| 2008 |
Rosenzweig AC. The metal centres of particulate methane mono-oxygenase. Biochemical Society Transactions. 36: 1134-7. PMID 19021511 DOI: 10.1042/Bst0361134 |
0.371 |
|
| 2008 |
Banci L, Bertini I, Cantini F, Rosenzweig AC, Yatsunyk LA. Metal binding domains 3 and 4 of the Wilson disease protein: solution structure and interaction with the copper(I) chaperone HAH1. Biochemistry. 47: 7423-9. PMID 18558714 DOI: 10.1021/Bi8004736 |
0.434 |
|
| 2008 |
Hakemian AS, Kondapalli KC, Telser J, Hoffman BM, Stemmler TL, Rosenzweig AC. The metal centers of particulate methane monooxygenase from Methylosinus trichosporium OB3b. Biochemistry. 47: 6793-801. PMID 18540635 DOI: 10.1021/Bi800598H |
0.823 |
|
| 2008 |
Balasubramanian R, Rosenzweig AC. Copper methanobactin: a molecule whose time has come. Current Opinion in Chemical Biology. 12: 245-9. PMID 18313412 DOI: 10.1016/J.Cbpa.2008.01.043 |
0.475 |
|
| 2008 |
Yatsunyk LA, Easton JA, Kim LR, Sugarbaker SA, Bennett B, Breece RM, Vorontsov II, Tierney DL, Crowder MW, Rosenzweig AC. Structure and metal binding properties of ZnuA, a periplasmic zinc transporter from Escherichia coli. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 13: 271-88. PMID 18027003 DOI: 10.1007/S00775-007-0320-0 |
0.453 |
|
| 2007 |
Sazinsky MH, LeMoine B, Orofino M, Davydov R, Bencze KZ, Stemmler TL, Hoffman BM, Argüello JM, Rosenzweig AC. Characterization and structure of a Zn2+ and [2Fe-2S]-containing copper chaperone from Archaeoglobus fulgidus. The Journal of Biological Chemistry. 282: 25950-9. PMID 17609202 DOI: 10.1074/Jbc.M703311200 |
0.62 |
|
| 2007 |
Balasubramanian R, Rosenzweig AC. Structural and mechanistic insights into methane oxidation by particulate methane monooxygenase. Accounts of Chemical Research. 40: 573-80. PMID 17444606 DOI: 10.1021/Ar700004S |
0.423 |
|
| 2007 |
Wheeler KE, Nocek JM, Cull DA, Yatsunyk LA, Rosenzweig AC, Hoffman BM. Dynamic docking of cytochrome b5 with myoglobin and alpha-hemoglobin: heme-neutralization "squares" and the binding of electron-transfer-reactive configurations. Journal of the American Chemical Society. 129: 3906-17. PMID 17343378 DOI: 10.1021/Ja067598G |
0.446 |
|
| 2007 |
Hakemian AS, Rosenzweig AC. The biochemistry of methane oxidation. Annual Review of Biochemistry. 76: 223-41. PMID 17328677 DOI: 10.1146/Annurev.Biochem.76.061505.175355 |
0.839 |
|
| 2007 |
Yatsunyk LA, Rosenzweig AC. Cu(I) binding and transfer by the N terminus of the Wilson disease protein. The Journal of Biological Chemistry. 282: 8622-31. PMID 17229731 DOI: 10.1074/Jbc.M609533200 |
0.46 |
|
| 2007 |
Sommerhalter M, Zhang Y, Rosenzweig AC. Solution structure of the COMMD1 N-terminal domain. Journal of Molecular Biology. 365: 715-21. PMID 17097678 DOI: 10.1016/J.Jmb.2006.10.030 |
0.342 |
|
| 2006 |
Rosenzweig AC, Sazinsky MH. Structural insights into dioxygen-activating copper enzymes. Current Opinion in Structural Biology. 16: 729-35. PMID 17011183 DOI: 10.1016/J.Sbi.2006.09.005 |
0.457 |
|
| 2006 |
Lieberman RL, Kondapalli KC, Shrestha DB, Hakemian AS, Smith SM, Telser J, Kuzelka J, Gupta R, Borovik AS, Lippard SJ, Hoffman BM, Rosenzweig AC, Stemmler TL. Characterization of the particulate methane monooxygenase metal centers in multiple redox states by X-ray absorption spectroscopy. Inorganic Chemistry. 45: 8372-81. PMID 16999437 DOI: 10.1021/Ic060739V |
0.828 |
|
| 2006 |
Ukaegbu UE, Henery S, Rosenzweig AC. Biochemical characterization of MmoS, a sensor protein involved in copper-dependent regulation of soluble methane monooxygenase. Biochemistry. 45: 10191-8. PMID 16922494 DOI: 10.1021/Bi060693H |
0.827 |
|
| 2006 |
Sazinsky MH, Agarwal S, Argüello JM, Rosenzweig AC. Structure of the actuator domain from the Archaeoglobus fulgidus Cu(+)-ATPase. Biochemistry. 45: 9949-55. PMID 16906753 DOI: 10.1021/Bi0610045 |
0.56 |
|
| 2006 |
Abajian C, Rosenzweig AC. Crystal structure of yeast Sco1. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 11: 459-66. PMID 16570183 DOI: 10.1007/S00775-006-0096-7 |
0.841 |
|
| 2006 |
Sazinsky MH, Mandal AK, Argüello JM, Rosenzweig AC. Structure of the ATP binding domain from the Archaeoglobus fulgidus Cu+-ATPase. The Journal of Biological Chemistry. 281: 11161-6. PMID 16495228 DOI: 10.1074/Jbc.M510708200 |
0.43 |
|
| 2006 |
Lieberman RL, Rosenzweig AC. Biophysical and structural characterization of particulate methane monooxygenase Acs National Meeting Book of Abstracts. 231. |
0.57 |
|
| 2005 |
Hakemian AS, Tinberg CE, Kondapalli KC, Telser J, Hoffman BM, Stemmler TL, Rosenzweig AC. The copper chelator methanobactin from Methylosinus trichosporium OB3b binds copper(I). Journal of the American Chemical Society. 127: 17142-3. PMID 16332035 DOI: 10.1021/Ja0558140 |
0.82 |
|
| 2005 |
Sommerhalter M, Saleh L, Bollinger JM, Rosenzweig AC. Structure of Escherichia coli ribonucleotide reductase R2 in space group P6122. Acta Crystallographica. Section D, Biological Crystallography. 61: 1649-54. PMID 16301799 DOI: 10.1107/S0907444905034062 |
0.579 |
|
| 2005 |
Lieberman RL, Rosenzweig AC. The quest for the particulate methane monooxygenase active site. Dalton Transactions (Cambridge, England : 2003). 3390-6. PMID 16234916 DOI: 10.1039/B506651D |
0.667 |
|
| 2005 |
Sommerhalter M, Lieberman RL, Rosenzweig AC. X-ray crystallography and biological metal centers: is seeing believing? Inorganic Chemistry. 44: 770-8. PMID 15859245 DOI: 10.1021/Ic0485256 |
0.654 |
|
| 2005 |
Lieberman RL, Rosenzweig AC. Crystal structure of a membrane-bound metalloenzyme that catalyses the biological oxidation of methane. Nature. 434: 177-82. PMID 15674245 DOI: 10.1038/Nature03311 |
0.685 |
|
| 2004 |
Lieberman RL, Rosenzweig AC. Biological methane oxidation: regulation, biochemistry, and active site structure of particulate methane monooxygenase. Critical Reviews in Biochemistry and Molecular Biology. 39: 147-64. PMID 15596549 DOI: 10.1080/10409230490475507 |
0.686 |
|
| 2004 |
Abajian C, Yatsunyk LA, Ramirez BE, Rosenzweig AC. Yeast cox17 solution structure and Copper(I) binding. The Journal of Biological Chemistry. 279: 53584-92. PMID 15465825 DOI: 10.1074/Jbc.M408099200 |
0.834 |
|
| 2004 |
Sommerhalter M, Voegtli WC, Perlstein DL, Ge J, Stubbe J, Rosenzweig AC. Structures of the yeast ribonucleotide reductase Rnr2 and Rnr4 homodimers. Biochemistry. 43: 7736-42. PMID 15196016 DOI: 10.1021/Bi049510M |
0.767 |
|
| 2004 |
Wernimont AK, Yatsunyk LA, Rosenzweig AC. Binding of copper(I) by the Wilson disease protein and its copper chaperone. The Journal of Biological Chemistry. 279: 12269-76. PMID 14709553 DOI: 10.1074/Jbc.M311213200 |
0.458 |
|
| 2004 |
Lieberman RL, Rosenzweig AC. Metal Ion Homeostasis Comprehensive Coordination Chemistry Ii. 8: 195-211. DOI: 10.1016/B0-08-043748-6/08136-6 |
0.697 |
|
| 2004 |
Lieberman RL, Rosenzweig AC. Crystallographic trapping of a precatalytic enzyme complex provides new insight into dioxygen activation at a mononuclear copper center Chemtracts. 17: 562-568. |
0.626 |
|
| 2003 |
Voegtli WC, Sommerhalter M, Saleh L, Baldwin J, Bollinger JM, Rosenzweig AC. Variable coordination geometries at the diiron(II) active site of ribonucleotide reductase R2. Journal of the American Chemical Society. 125: 15822-30. PMID 14677973 DOI: 10.1021/Ja0370387 |
0.792 |
|
| 2003 |
Miller MT, Gerratana B, Stapon A, Townsend CA, Rosenzweig AC. Crystal structure of carbapenam synthetase (CarA). The Journal of Biological Chemistry. 278: 40996-1002. PMID 12890666 DOI: 10.1074/Jbc.M307901200 |
0.326 |
|
| 2003 |
Lieberman RL, Shrestha DB, Doan PE, Hoffman BM, Stemmler TL, Rosenzweig AC. Purified particulate methane monooxygenase from Methylococcus capsulatus (Bath) is a dimer with both mononuclear copper and a copper-containing cluster. Proceedings of the National Academy of Sciences of the United States of America. 100: 3820-5. PMID 12634423 DOI: 10.1073/Pnas.0536703100 |
0.76 |
|
| 2003 |
Wernimont AK, Huffman DL, Finney LA, Demeler B, O'Halloran TV, Rosenzweig AC. Crystal structure and dimerization equilibria of PcoC, a methionine-rich copper resistance protein from Escherichia coli. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 8: 185-94. PMID 12459914 DOI: 10.1007/S00775-002-0404-9 |
0.668 |
|
| 2002 |
Miller MT, Bachmann BO, Townsend CA, Rosenzweig AC. The catalytic cycle of beta -lactam synthetase observed by x-ray crystallographic snapshots. Proceedings of the National Academy of Sciences of the United States of America. 99: 14752-7. PMID 12409610 DOI: 10.1073/Pnas.232361199 |
0.316 |
|
| 2002 |
Rosenzweig AC. Metallochaperones: bind and deliver. Chemistry & Biology. 9: 673-7. PMID 12079778 DOI: 10.1016/S1074-5521(02)00156-4 |
0.348 |
|
| 2001 |
Voegtli WC, Ge J, Perlstein DL, Stubbe J, Rosenzweig AC. Structure of the yeast ribonucleotide reductase Y2Y4 heterodimer. Proceedings of the National Academy of Sciences of the United States of America. 98: 10073-8. PMID 11526233 DOI: 10.1073/Pnas.181336398 |
0.765 |
|
| 2001 |
Lamb AL, Torres AS, O'Halloran TV, Rosenzweig AC. Heterodimeric structure of superoxide dismutase in complex with its metallochaperone. Nature Structural Biology. 8: 751-5. PMID 11524675 DOI: 10.1038/Nsb0901-751 |
0.64 |
|
| 2001 |
Baldwin J, Voegtli WC, Khidekel N, Moënne-Loccoz P, Krebs C, Pereira AS, Ley BA, Huynh BH, Loehr TM, Riggs-Gelasco PJ, Rosenzweig AC, Bollinger JM. Rational reprogramming of the R2 subunit of Escherichia coli ribonucleotide reductase into a self-hydroxylating monooxygenase. Journal of the American Chemical Society. 123: 7017-30. PMID 11459480 DOI: 10.1021/Ja002114G |
0.791 |
|
| 2001 |
Lieberman RL, Arciero DM, Hooper AB, Rosenzweig AC. Crystal structure of a novel red copper protein from Nitrosomonas europaea. Biochemistry. 40: 5674-81. PMID 11341832 DOI: 10.1021/Bi0102611 |
0.718 |
|
| 2001 |
Whittington DA, Rosenzweig AC, Frederick CA, Lippard SJ. Xenon and halogenated alkanes track putative substrate binding cavities in the soluble methane monooxygenase hydroxylase. Biochemistry. 40: 3476-82. PMID 11297413 DOI: 10.1021/Bi0022487 |
0.514 |
|
| 2001 |
Rosenzweig AC. Copper delivery by metallochaperone proteins. Accounts of Chemical Research. 34: 119-28. PMID 11263870 DOI: 10.1021/Ar000012P |
0.477 |
|
| 2000 |
Voegtli WC, White DJ, Reiter NJ, Rusnak F, Rosenzweig AC. Structure of the bacteriophage lambda Ser/Thr protein phosphatase with sulfate ion bound in two coordination modes. Biochemistry. 39: 15365-74. PMID 11112522 DOI: 10.1021/Bi0021030 |
0.776 |
|
| 2000 |
Lamb AL, Torres AS, O'Halloran TV, Rosenzweig AC. Heterodimer formation between superoxide dismutase and its copper chaperone. Biochemistry. 39: 14720-7. PMID 11101286 DOI: 10.1021/Bi002207A |
0.641 |
|
| 2000 |
Wernimont AK, Huffman DL, Lamb AL, O'Halloran TV, Rosenzweig AC. Structural basis for copper transfer by the metallochaperone for the Menkes/Wilson disease proteins. Nature Structural Biology. 7: 766-71. PMID 10966647 DOI: 10.1038/78999 |
0.659 |
|
| 2000 |
Coufal DE, Blazyk JL, Whittington DA, Wu WW, Rosenzweig AC, Lippard SJ. Sequencing and analysis of the Mmethylococcus capsulatus (Bath) solublemethane monooxygenase genes. European Journal of Biochemistry / Febs. 267: 2174-85. PMID 10759840 DOI: 10.1046/J.1432-1327.2000.01210.X |
0.518 |
|
| 2000 |
Rosenzweig AC, O'Halloran TV. Structure and chemistry of the copper chaperone proteins. Current Opinion in Chemical Biology. 4: 140-7. PMID 10742187 DOI: 10.1016/S1367-5931(99)00066-6 |
0.621 |
|
| 2000 |
Rosenzweig AC. Nitrous oxide reductase from CuA to CuZ. Nature Structural Biology. 7: 169-71. PMID 10700265 DOI: 10.1038/73244 |
0.379 |
|
| 2000 |
Lamb AL, Wernimont AK, Pufahl RA, O'Halloran TV, Rosenzweig AC. Crystal structure of the second domain of the human copper chaperone for superoxide dismutase. Biochemistry. 39: 1589-95. PMID 10677207 DOI: 10.1021/Bi992822I |
0.621 |
|
| 2000 |
Voegtli WC, Khidekel N, Baldwin J, Ley BA, Bollinger JM, Rosenzweig AC. Crystal structure of the ribonucleotide reductase R2 mutant that accumulates a μ-1,2-peroxodiiron(III) intermediate during oxygen activation Journal of the American Chemical Society. 122: 3255-3261. DOI: 10.1021/Ja991839L |
0.787 |
|
| 1999 |
Lamb AL, Wernimont AK, Pufahl RA, Culotta VC, O'Halloran TV, Rosenzweig AC. Crystal structure of the copper chaperone for superoxide dismutase. Nature Structural Biology. 6: 724-9. PMID 10426947 DOI: 10.1038/11489 |
0.627 |
|
| 1999 |
Rosenzweig AC, Huffman DL, Hou MY, Wernimont AK, Pufahl RA, O'Halloran TV. Crystal structure of the Atx1 metallochaperone protein at 1.02 A resolution. Structure (London, England : 1993). 7: 605-17. PMID 10404590 DOI: 10.1016/S0969-2126(99)80082-3 |
0.648 |
|
| 1999 |
Portnoy ME, Rosenzweig AC, Rae T, Huffman DL, O'Halloran TV, Culotta VC. Structure-function analyses of the ATX1 metallochaperone. The Journal of Biological Chemistry. 274: 15041-5. PMID 10329707 DOI: 10.1074/Jbc.274.21.15041 |
0.681 |
|
| 1997 |
Rosenzweig AC, Brandstetter H, Whittington DA, Nordlund P, Lippard SJ, Frederick CA. Crystal structures of the methane monooxygenase hydroxylase from Methylococcus capsulatus (Bath): implications for substrate gating and component interactions. Proteins. 29: 141-52. PMID 9329079 DOI: 10.1002/(Sici)1097-0134(199710)29:2<141::Aid-Prot2>3.0.Co;2-G |
0.516 |
|
| 1996 |
Dooley DM, Alvarez ML, Rosenzweig AC, Hollis RS, Zumft WG. Exogenous ligand binding to Pseudomonas stutzeri nitrous oxide reductase Inorganica Chimica Acta. 242: 239-244. DOI: 10.1016/0020-1693(95)04873-1 |
0.419 |
|
| 1995 |
Rosenzweig AC, Nordlund P, Takahara PM, Frederick CA, Lippard SJ. Geometry of the soluble methane monooxygenase catalytic diiron center in two oxidation states. Chemistry & Biology. 2: 409-18. PMID 9432288 DOI: 10.1016/1074-5521(95)90222-8 |
0.817 |
|
| 1995 |
Rosenzweig AC, Nordlund P, Takahara PM, Frederick CA, Lippard SJ. Geometry of the soluble methane monooxygenase catalytic diiron center in two oxidation states. Chemistry & Biology. 2: 409-18. PMID 9383443 |
0.817 |
|
| 1995 |
Takahara PM, Rosenzweig AC, Frederick CA, Lippard SJ. Crystal structure of double-stranded DNA containing the major adduct of the anticancer drug cisplatin. Nature. 377: 649-52. PMID 7566180 DOI: 10.1038/377649A0 |
0.784 |
|
| 1995 |
DeWitt JG, Rosenzweig AC, Salifoglou A, Hedman B, Lippard SJ, Hodgson KO. X-ray Absorption Spectroscopic Studies of the Diiron Center in Methane Monooxygenase in the Presence of Substrate and the Coupling Protein of the Enzyme System Inorganic Chemistry. 34: 2505-2515. DOI: 10.1021/Ic00114A007 |
0.476 |
|
| 1995 |
Rosenzweig AC, Nordlund P, Lippard SJ, Frederick CA. High resolution crystal structures of the hydroxylase protein of methane monooxygenase Journal of Inorganic Biochemistry. 59: 381. DOI: 10.1016/0162-0134(95)97479-A |
0.447 |
|
| 1995 |
Takahara PM, Rosenzweig AC, Frederick CA, Lippard SJ. X-ray structure of a dodecamer duplex containing the major cisplatin d(GpG) intrastrand cross-link Journal of Inorganic Biochemistry. 59: 194. DOI: 10.1016/0162-0134(95)97300-F |
0.765 |
|
| 1994 |
Bender CJ, Rosenzweig AC, Lippard SJ, Peisach J. Nuclear hyperfine coupling of nitrogen in the coordination sphere of the diiron center of methane monooxygenase hydroxylase. The Journal of Biological Chemistry. 269: 15993-8. PMID 8206895 |
0.357 |
|
| 1994 |
Rosenzweig AC, Lippard SJ. Determining the Structure of a Hydroxylase Enzyme That Catalyzes the Conversion of Methane to Methanol in Methanotrophic Bacteria Accounts of Chemical Research. 27: 229-236. DOI: 10.1021/Ar00044A003 |
0.487 |
|
| 1994 |
Rosenzweig AC, Lippard SJ. Chemical nature of the hydroxylase enzyme of methane monooxygenase as revealed by the 2.2 Å crystal structure Chemistry and Biology. 1: xxii-xxiii. DOI: 10.1016/1074-5521(94)90028-0 |
0.457 |
|
| 1993 |
Rosenzweig AC, Frederick CA, Lippard SJ, Nordlund P. Crystal structure of a bacterial non-haem iron hydroxylase that catalyses the biological oxidation of methane. Nature. 366: 537-43. PMID 8255292 DOI: 10.1038/366537A0 |
0.507 |
|
| 1993 |
Rosenzweig A, Nordlund P, Frederick C, Lippard S. X-ray crystallographic studies of the hydroxylase component of methane monooxygenase from Methylococcus capsulatus (Bath) Journal of Inorganic Biochemistry. 51: 151. DOI: 10.1016/0162-0134(93)85187-D |
0.393 |
|
| 1992 |
Rosenzweig AC, Frederick CA, Lippard SJ. Crystallization and preliminary X-ray analysis of the methane monooxygenase hydroxylase protein from Methylococcus capsulatus (Bath). Journal of Molecular Biology. 227: 583-5. PMID 1404375 DOI: 10.1016/0022-2836(92)90913-5 |
0.465 |
|
| 1991 |
DeWitt JG, Bentsen JG, Rosenzweig AC, Hedman B, Green J, Pilkington S, Papaefthymiou GC, Dalton H, Hodgson KO, Lippard SJ. X-ray absorption, Moessbauer, and EPR studies of the dinuclear iron center in the hydroxylase component of methane monooxygenase Journal of the American Chemical Society. 113: 9219-9235. DOI: 10.1021/Ja00024A031 |
0.444 |
|
| 1991 |
Dooley DM, McGuirl MA, Rosenzweig AC, Landin JA, Scott RA, Zumft WG, Devlin F, Stephens PJ. Spectroscopic studies of the copper sites in wild-type Pseudomonas stutzeri N2O reductase and in an inactive protein isolated from a mutant deficient in copper-site biosynthesis Inorganic Chemistry. 30: 3006-3011. |
0.311 |
|
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