| Year |
Citation |
Score |
| 2019 |
Grossman JD, Gay KA, Camire EJ, Walden WE, Perlstein DL. Coupling nucleotide binding and hydrolysis to iron-sulfur cluster acquisition and transfer revealed through genetic dissection of the Nbp35 ATPase site. Biochemistry. PMID 30865432 DOI: 10.1021/Acs.Biochem.8B00737 |
0.365 |
|
| 2019 |
Grossman JD, Camire EJ, Glynn CA, Neil CM, Seguinot BO, Perlstein DL. The Cfd1 subunit of the Nbp35-Cfd1 iron sulfur cluster scaffolding complex controls nucleotide binding. Biochemistry. PMID 30785732 DOI: 10.1021/Acs.Biochem.8B00798 |
0.395 |
|
| 2018 |
Grossman JD, Camire EJ, Perlstein DL. Approaches to Interrogate the Role of Nucleotide Hydrolysis by Metal Trafficking NTPases: The Nbp35-Cfd1 Iron-Sulfur Cluster Scaffold as a Case Study. Methods in Enzymology. 599: 293-325. PMID 29746244 DOI: 10.1016/Bs.Mie.2017.11.005 |
0.362 |
|
| 2017 |
Vo AT, Fleischman NM, Marquez MD, Camire EJ, Esonwune SU, Grossman JD, Gay KA, Cosman JA, Perlstein DL. Defining the domains of Cia2 required for its essential function in vivo and in vitro. Metallomics : Integrated Biometal Science. PMID 29057997 DOI: 10.1039/C7Mt00181A |
0.352 |
|
| 2017 |
Vo ATV, Fleischman NM, Froehlich MJ, Lee CY, Cosman JA, Glynn CA, Hassan ZO, Perlstein DL. Identifying the protein interactions of the cytosolic iron sulfur cluster targeting complex essential for its assembly and recognition of apo-targets. Biochemistry. PMID 28539047 DOI: 10.1021/Acs.Biochem.7B00072 |
0.343 |
|
| 2015 |
Camire EJ, Grossman JD, Thole GJ, Fleischman NM, Perlstein DL. The yeast Nbp35-Cfd1 cytosolic iron-sulfur cluster scaffold is an ATPase Journal of Biological Chemistry. 290: 23793-23802. PMID 26195633 DOI: 10.1074/Jbc.M115.667022 |
0.385 |
|
| 2011 |
Doud EH, Perlstein DL, Wolpert M, Cane DE, Walker S. Two distinct mechanisms for TIM barrel prenyltransferases in bacteria. Journal of the American Chemical Society. 133: 1270-3. PMID 21214173 DOI: 10.1021/Ja109578B |
0.46 |
|
| 2010 |
Perlstein DL, Wang TS, Doud EH, Kahne D, Walker S. The role of the substrate lipid in processive glycan polymerization by the peptidoglycan glycosyltransferases. Journal of the American Chemical Society. 132: 48-9. PMID 20017480 DOI: 10.1021/Ja909325M |
0.466 |
|
| 2009 |
Lupoli TJ, Taniguchi T, Wang TS, Perlstein DL, Walker S, Kahne DE. Studying a cell division amidase using defined peptidoglycan substrates. Journal of the American Chemical Society. 131: 18230-1. PMID 19957935 DOI: 10.1021/Ja908916Z |
0.488 |
|
| 2009 |
Ostash B, Doud EH, Lin C, Ostash I, Perlstein DL, Fuse S, Wolpert M, Kahne D, Walker S. Complete characterization of the seventeen step moenomycin biosynthetic pathway. Biochemistry. 48: 8830-41. PMID 19640006 DOI: 10.1021/Bi901018Q |
0.48 |
|
| 2007 |
Perlstein DL, Zhang Y, Wang TS, Kahne DE, Walker S. The direction of glycan chain elongation by peptidoglycan glycosyltransferases. Journal of the American Chemical Society. 129: 12674-5. PMID 17914829 DOI: 10.1021/Ja075965Y |
0.493 |
|
| 2006 |
Ortigosa AD, Hristova D, Perlstein DL, Zhang Z, Huang M, Stubbe J. Determination of the in vivo stoichiometry of tyrosyl radical per betabeta' in Saccharomyces cerevisiae ribonucleotide reductase. Biochemistry. 45: 12282-94. PMID 17014081 DOI: 10.1021/Bi0610404 |
0.585 |
|
| 2006 |
Zhang Z, An X, Yang K, Perlstein DL, Hicks L, Kelleher N, Stubbe J, Huang M. Nuclear localization of the Saccharomyces cerevisiae ribonucleotide reductase small subunit requires a karyopherin and a WD40 repeat protein. Proceedings of the National Academy of Sciences of the United States of America. 103: 1422-7. PMID 16432237 DOI: 10.1073/Pnas.0510516103 |
0.578 |
|
| 2005 |
Perlstein DL, Ge J, Ortigosa AD, Robblee JH, Zhang Z, Huang M, Stubbe J. The active form of the Saccharomyces cerevisiae ribonucleotide reductase small subunit is a heterodimer in vitro and in vivo. Biochemistry. 44: 15366-77. PMID 16285741 DOI: 10.1021/Bi051616+ |
0.516 |
|
| 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 |
0.579 |
|
| 2003 |
Bennati M, Weber A, Antonic J, Perlstein DL, Robblee J, Stubbe J. Pulsed ELDOR Spectroscopy Measures the Distance between the Two Tyrosyl Radicals in the R2 Subunit of the E. coli Ribonucleotide Reductase Journal of the American Chemical Society. 125: 14988-14989. PMID 14653724 DOI: 10.1021/Ja0362095 |
0.552 |
|
| 2003 |
Yao R, Zhang Z, An X, Bucci B, Perlstein DL, Stubbe J, Huang M. Subcellular localization of yeast ribonucleotide reductase regulated by the DNA replication and damage checkpoint pathways Proceedings of the National Academy of Sciences of the United States of America. 100: 6628-6633. PMID 12732713 DOI: 10.1073/Pnas.1131932100 |
0.496 |
|
| 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 |
0.594 |
|
| 2001 |
Ge J, Perlstein DL, Nguyen HH, Bar G, Griffin RG, Stubbe J. Why multiple small subunits (Y2 and Y4) for yeast ribonucleotide reductase? Toward understanding the role of Y4 Proceedings of the National Academy of Sciences of the United States of America. 98: 10067-10072. PMID 11526232 DOI: 10.1073/Pnas.181336498 |
0.565 |
|
| 1999 |
Nguyen HHT, Ge J, Perlstein DL, Stubbe J. Purification of ribonucleotide reductase subunits Y1, Y2, Y3, and Y4 from yeast: Y4 plays a key role in diiron cluster assembly Proceedings of the National Academy of Sciences of the United States of America. 96: 12339-12344. PMID 10535923 DOI: 10.1073/Pnas.96.22.12339 |
0.531 |
|
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