{"id":16,"date":"2019-05-23T08:43:18","date_gmt":"2019-05-23T12:43:18","guid":{"rendered":"https:\/\/sites.bu.edu\/perlstein\/?page_id=16"},"modified":"2023-12-18T15:51:52","modified_gmt":"2023-12-18T20:51:52","slug":"publications","status":"publish","type":"page","link":"https:\/\/sites.bu.edu\/perlstein\/publications\/","title":{"rendered":"Publications"},"content":{"rendered":"

Perlstein lab publications on:<\/h3>\n

google scholar<\/a><\/p>\n

pubmed<\/a><\/p>\n

Publications from Boston University<\/h3>\n

24. Vasquez, S; Marquez, MD; Brignole, EJ; Vo, A; Kong, S; Park, C; Perlstein, DL<\/strong>; Drennan CL. Structural and biochemical investigation of a HEAT-repeat protein involved in the cytosolic iron-sulfur assembly pathway<\/a>. Nature<\/em> Communications Biology<\/em>. 2023<\/strong>, 6<\/em>, 1-12.<\/p>\n

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23. Marquez, MD; Greth, C; Buzuk, A; Liu, Y; Blinn, CM; Beller, S; Leiskau, L; Hushka, A; Wu, K; Nur, K; Netz, DJA; Perlstein, DL<\/strong>; Pierik, AJ. Cytosolic iron-sulfur protein assembly system identifies clients by a C-terminal tripeptide<\/a>. PNAS<\/em>.\u00a0 2023<\/strong>, 120<\/em>, 1-7.<\/p>\n

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22. Mol\u00e9, CN; Dave K; Perlstein, DL<\/strong>. Methods to Unravel the Roles of ATPases in Fe-S Cluster Biosynthesis<\/a>. Methods in Molecular Biology<\/em>, 2021<\/strong>, 2353<\/em>, 155-171.<\/p>\n

21. Grossman, JD; Gay, KA; Camire, EJ; Walden, WE; and\u00a0Perlstein, DL<\/strong>. Coupling of Nucleotide Binding and Hydrolysis to Iron-Sulfur Cluster Acquisition and Transfer Revealed through Genetic Dissection of the Nbp35 ATPase Site<\/a>.\u00a0Biochemistry,\u00a0<\/em>2019<\/strong>, 58, 2017-2027.<\/em><\/p>\n

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20.\u00a0Grossman, JD; Camire, EJ; Glynn, CA; Neil, CM; Seguinot, BO;\u00a0 and\u00a0Perlstein, DL.\u00a0<\/strong>The Cfd1 Subunit of the Nbp35-Cfd1 Iron Sulfur Cluster Scaffolding Complex Controls Nucleotide Binding.<\/a>\u00a0\u00a0Biochemistry,\u00a0<\/em>2019<\/strong>, 58, 1587-1595.<\/em><\/p>\n

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19. Grossman, JD; Camire, EJ; and\u00a0Perlstein, DL.<\/strong> Approaches to Interrogate the Role of Nucleotide Hydrolysis by Metal Trafficking NTPases: The Nbp35-Cfd1 Iron-Sulfur Cluster Scaffold as a Case Study<\/a>.\u00a0Methods Enzymol.\u00a0<\/em>2018<\/strong>,\u00a0599<\/em>, 293-325.<\/p>\n

18. Vo, AT; Fleischman, NM; Camire, EJ; Esonwune, SU; Grossman, JD; Gay, KA; Cosman, JA; and Perlstein, DL.\u00a0<\/strong>Defining the domains of Cia2 required for its essential function in vivo and in vitro<\/a>.\u00a0Metallomics<\/em>\u00a02017<\/strong>,\u00a09,\u00a0<\/em>1645-1654.<\/p>\n

\"Graphical<\/p>\n

17. Vo, AT; Fleischman, NM; Froehlich, MJ; Lee, CY; Cosman, JA; Glynn, CA; Hassan, ZO, and\u00a0Perlstein, DL.<\/strong> Identifying the Protein Interactions of the Cytosolic Iron-Sulfur Cluster Targeting complex Essential for Its Assembly and Recognition of Apo-Targets<\/a>.\u00a0Biochemistry,\u00a0<\/em>2018<\/strong>,\u00a057, 2349-2358.<\/p>\n

<\/p>\n

16. Camire, EJ; Grossman, JD; Thole, GJ; Fleischman, NM; and\u00a0Perlstein, DL.<\/strong> The Yeast Nbp35-Cfd1 Cytosolic Iron-Sulfur Cluster Scaffold Is an ATPase<\/a>.\u00a0J. Biol. Chem.\u00a0<\/em>2015<\/strong>,\u00a0290<\/em>, 23793-23802.<\/p>\n

Prior to Boston University:<\/h3>\n

15.\u00a0Doud EH;\u00a0<\/span>Perlstein DL;<\/b>\u00a0Wolpert M; Cane DE; and Walker S. Two distinct mechanisms for TIM barrel prenyltransferases in bacteria.\u00a0J. Am. Chem. Soc.\u00a0<\/em>2011<\/strong>,\u00a0113<\/em>, 1270-1273.<\/span><\/p>\n

14.\u00a0Perlstein D;<\/b>\u00a0Wang TS; Doud EH; Kahne D; Walker S. The Role of the substrate lipid in processive glycan polymerization by the peptidglycan glycosyltransferases.\u00a0J. Am. Chem. Soc.\u00a0<\/em>2010<\/strong>,\u00a0132,\u00a0<\/em>48-49.<\/span><\/p>\n

13.\u00a0Lupoli TJ; Taniguchi T; Wang TS;\u00a0<\/span>Perlstein DL;<\/b>\u00a0Walker S; and Kahne DE. Studying a cell division amidase using defined peptidoglycan substrates.\u00a0J. Am. Chem. Soc.\u00a0<\/em>2009<\/strong>,\u00a0131,\u00a0<\/em>18230-18231.<\/span><\/p>\n

12.Ostash B, Doud EH, Lin C, Ostash I,\u00a0<\/span>Perlstein DL<\/b>, Fuse S, Wolpert M, Kahne D, Walker S. Complete characterization of the seventeen step moenomycin biosynthetic pathway.\u00a0Biochemistry,\u00a0<\/em>2009<\/strong>, 48<\/em>, 8830-41.<\/span><\/p>\n

11.\u00a0Perlstein DL<\/b>, Zhang Y, Wang TS, Kahne DE, Walker S. The direction of glycan chain elongation by peptidoglycan glycosyltransferaes.\u00a0J. Am. Chem. Soc.,\u00a02007<\/strong>,\u00a0129,<\/em> 12674-12675.<\/span><\/p>\n

10.\u00a0Ortigosa AD*, Hristova D,*\u00a0<\/span>Perlstein DL<\/b>,* Zhang Z, Huang M, Stubbe J. Determination of the in vivo stoichiometry of tyrosyl radical per beta-beta’ in Saccharomyces cerevisiae ribonucleotide reductase.\u00a0Biochemistry,\u00a0<\/em>2006<\/strong>, 45<\/em>, 12282-12294.<\/span><\/p>\n

9.\u00a0Zhang Z, An X, Yang K,\u00a0<\/span>Perlstein DL<\/b>, 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.\u00a0Proc. Natl. Acad. Sci. U.S.A.<\/em>,\u00a02006<\/strong>, 103<\/em>, 1422-1427.<\/span><\/p>\n

8.\u00a0Perlstein DL<\/b>, 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.\u00a0<\/span>Biochemistry,\u00a0<\/em>2005<\/strong>, 44<\/em>, 15366-77.<\/span><\/p>\n

7.\u00a0Sommerhalter M, Voegtli WC,\u00a0<\/span>Perlstein DL<\/b>, Ge J, Stubbe J, Rosenzweig AC. Structures of the yeast ribonucleotide reductase Rnr2 and Rnr4 homodimers.\u00a0Biochemistry,\u00a0<\/em>2004<\/strong>, 43<\/em>, 7736-42.<\/span><\/p>\n

6.\u00a0Bennati M, Weber A, Antonic J,\u00a0<\/span>Perlstein DL<\/b>, 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.\u00a0\u00a0J. Am. Chem. Soc.,\u00a02003<\/strong>,\u00a0125,<\/em> 14988-14989.<\/span><\/p>\n

5.\u00a0Yao R, Zhang Z, An X, Bucci B,\u00a0<\/span>Perlstein DL<\/b>, Stubbe J, Huang M. Subcellular localization of yeast ribonucleotide reductase regulated by the DNA replication and damage checkpoint pathways.\u00a0Proc. Natl. Acad. Sci. U.S.A.<\/em>,\u00a02003<\/strong>, 100<\/em>, 6628-6633.<\/span><\/p>\n

4.\u00a0Voegtli WC, Ge J,\u00a0<\/span>Perlstein DL<\/b>, Stubbe J, Rosenzweig AC. Structure of the yeast ribonucleotide reductase Y2Y4 heterodimer.\u00a0Proc. Natl. Acad. Sci. U.S.A.<\/em>,\u00a02001<\/strong>,\u00a098<\/em>, 10073-10078.<\/span><\/p>\n

3.\u00a0Ge J,\u00a0<\/span>Perlstein DL<\/b>, 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.\u00a0<\/span>Proc. Natl. Acad. Sci. U.S.A.<\/em>,\u00a02001<\/strong>,\u00a098<\/em>, 10067-10072.<\/span><\/p>\n

2.\u00a0Nguyen HH, Ge J,\u00a0<\/span>Perlstein DL<\/b>, Stubbe J. Purification of ribonucleotide reductase subunits Y1, Y2, Y3, and Y4 from yeast: Y4 plays a key role in diiron cluster assembly.\u00a0Proc. Natl. Acad. Sci. U.S.A.<\/em>,\u00a01999<\/strong>,\u00a096<\/em>, 12339-12344.<\/span><\/p>\n

1. Rao, VJ; Perlstein, DL<\/strong>; Robbins, RJ; Lakshminarasimhan, PH; Kao, HM; Grey, CP; and Ramamurthy, V. Detection of low levels of Bronsted acidity in Na+<\/sup>Y and\u00a0Na+<\/sup>X\u00a0zeolites.\u00a0Chem. Comm.<\/em>,\u00a01998<\/strong>,\u00a02<\/em>, 268-270.<\/p>\n

 <\/p>\n","protected":false},"excerpt":{"rendered":"

Perlstein lab publications on: google scholar pubmed Publications from Boston University 24. Vasquez, S; Marquez, MD; Brignole, EJ; Vo, A; Kong, S; Park, C; Perlstein, DL; Drennan CL. Structural and biochemical investigation of a HEAT-repeat protein involved in the cytosolic iron-sulfur assembly pathway. Nature Communications Biology. 2023, 6, 1-12. 23. Marquez, MD; Greth, C; Buzuk, […]<\/p>\n","protected":false},"author":10222,"featured_media":0,"parent":0,"menu_order":3,"comment_status":"closed","ping_status":"closed","template":"","meta":[],"_links":{"self":[{"href":"https:\/\/sites.bu.edu\/perlstein\/wp-json\/wp\/v2\/pages\/16"}],"collection":[{"href":"https:\/\/sites.bu.edu\/perlstein\/wp-json\/wp\/v2\/pages"}],"about":[{"href":"https:\/\/sites.bu.edu\/perlstein\/wp-json\/wp\/v2\/types\/page"}],"author":[{"embeddable":true,"href":"https:\/\/sites.bu.edu\/perlstein\/wp-json\/wp\/v2\/users\/10222"}],"replies":[{"embeddable":true,"href":"https:\/\/sites.bu.edu\/perlstein\/wp-json\/wp\/v2\/comments?post=16"}],"version-history":[{"count":11,"href":"https:\/\/sites.bu.edu\/perlstein\/wp-json\/wp\/v2\/pages\/16\/revisions"}],"predecessor-version":[{"id":627,"href":"https:\/\/sites.bu.edu\/perlstein\/wp-json\/wp\/v2\/pages\/16\/revisions\/627"}],"wp:attachment":[{"href":"https:\/\/sites.bu.edu\/perlstein\/wp-json\/wp\/v2\/media?parent=16"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}