D. Perlstein

发表

Methods to Unravel the Roles of ATPases in Fe-S Cluster Biosynthesis.

Christa N Molé, K. Dave, D. Perlstein, 2021, Methods in molecular biology.

Why multiple small subunits (Y2 and Y4) for yeast ribonucleotide reductase? Toward understanding the role of Y4

R. Griffin, J. Stubbe, H. Nguyen, 2001, Proceedings of the National Academy of Sciences of the United States of America.

Purification of ribonucleotide reductase subunits Y1, Y2, Y3, and Y4 from yeast: Y4 plays a key role in diiron cluster assembly.

J. Stubbe, H. Nguyen, D. Perlstein, 1999, Proceedings of the National Academy of Sciences of the United States of America.

Approaches to Interrogate the Role of Nucleotide Hydrolysis by Metal Trafficking NTPases: The Nbp35-Cfd1 Iron-Sulfur Cluster Scaffold as a Case Study.

D. Perlstein, Deborah L. Perlstein, John D Grossman, 2018, Methods in enzymology.

Structures of the yeast ribonucleotide reductase Rnr2 and Rnr4 homodimers.

A. Rosenzweig, J. Stubbe, D. Perlstein, 2004, Biochemistry.

Coupling Nucleotide Binding and Hydrolysis to Iron-Sulfur Cluster Acquisition and Transfer Revealed through Genetic Dissection of the Nbp35 ATPase Site.

W. Walden, D. Perlstein, Deborah L. Perlstein, 2019, Biochemistry.

Determination of the in vivo stoichiometry of tyrosyl radical per ββ' in Saccharomyces cerevisiae ribonucleotide reductase

J. Stubbe, D. Perlstein, Deborah L. Perlstein, 2006 .

Studying a cell division amidase using defined peptidoglycan substrates.

S. Walker, D. Kahne, D. Perlstein, 2009, Journal of the American Chemical Society.

The Cfd1 Subunit of the Nbp35-Cfd1 Iron Sulfur Cluster Scaffolding Complex Controls Nucleotide Binding.

D. Perlstein, Deborah L. Perlstein, C. Neil, 2019, Biochemistry.

The active form of the Saccharomyces cerevisiae ribonucleotide reductase small subunit is a heterodimer in vitro and in vivo.

J. Stubbe, D. Perlstein, Deborah L. Perlstein, 2005, Biochemistry.

The role of the substrate lipid in processive glycan polymerization by the peptidoglycan glycosyltransferases.

S. Walker, D. Kahne, D. Perlstein, 2010, Journal of the American Chemical Society.

The direction of glycan chain elongation by peptidoglycan glycosyltransferases.

S. Walker, D. Kahne, D. Perlstein, 2007, Journal of the American Chemical Society.

Detection of low levels of Brønsted acidity in Na+Y and Na+X zeolites

C. Grey, H. Kao, D. Perlstein, 1998 .

Subcellular localization of yeast ribonucleotide reductase regulated by the DNA replication and damage checkpoint pathways

Zhen Zhang, JoAnne Stubbe, J. Stubbe, 2003, Proceedings of the National Academy of Sciences of the United States of America.

Complete characterization of the seventeen step moenomycin biosynthetic pathway.

S. Walker, D. Kahne, B. Ostash, 2009, Biochemistry.

Nuclear localization of the Saccharomyces cerevisiae ribonucleotide reductase small subunit requires a karyopherin and a WD40 repeat protein

N. Kelleher, J. Stubbe, L. Hicks, 2006, Proceedings of the National Academy of Sciences of the United States of America.

Defining the domains of Cia2 required for its essential function in vivo and in vitro.

D. Perlstein, Nicholas M Fleischman, K. Gay, 2017, Metallomics : integrated biometal science.

Identifying the Protein Interactions of the Cytosolic Iron-Sulfur Cluster Targeting Complex Essential for Its Assembly and Recognition of Apo-Targets.

D. Perlstein, Deborah L. Perlstein, Nicholas M Fleischman, 2017, Biochemistry.

Defining the active form of ribonucleotide reductase from Saccharomyces cerevisiae in vitro and in vivo

D. Perlstein, Deborah L. Perlstein, 2005 .

Structure of the yeast ribonucleotide reductase Y2Y4 heterodimer

A. Rosenzweig, J. Stubbe, D. Perlstein, 2001, Proceedings of the National Academy of Sciences of the United States of America.

Pulsed ELDOR spectroscopy measures the distance between the two tyrosyl dadicals in the R2 subunit of the E. coli ribonucleotide reductase.

J. Stubbe, M. Bennati, J. Antonic, 2003, Journal of the American Chemical Society.

Two distinct mechanisms for TIM barrel prenyltransferases in bacteria.

D. Cane, S. Walker, D. Perlstein, 2011, Journal of the American Chemical Society.

Cytosolic iron-sulfur protein assembly system identifies clients by a C-terminal tripeptide

Yaxi Liu, D. Perlstein, Deborah L. Perlstein, 2023, bioRxiv.