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Professor Emeritus of Biochemistry and Biophysics
Ph.D. University of California at Berkeley 1958

 
  Yeast molecular biology and genetics; gene expression; cytochrome c biosynthesis and degradation.

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About Fred Sherman:

Dr. Sherman has been investigating various broad aspects of gene expression in yeast, as means to determine processes operating in eukaryotic cells. By using iso-1-cytochrome c as a model system, general principles have been uncovered, including those involved in transcription, translation, co-translational and post-translational modification, mitochondrial import, heme attachment, enzymatic functions and protein degradation. Currently, efforts have been directed toward understanding the relationships between protein structure, protein modifications and degradation in vivo, and in uncovering new degradation systems in mitochondria.

 

 
 
         
 

Recent Publications

 
 

Polevoda B, Hoskins J, Sherman F (2009) Properties of Nat4, an N{alpha}-Acetyltransferase of Saccharomyces cerevisae that Modifies N termini of Histones H2A and H4. Mol Cell Biol,

Polevoda B, Brown S, Cardillo TS, Rigby S, Sherman F (2008) Yeast N(alpha)-terminal acetyltransferases are associated with ribosomes. J Cell Biochem, 103:492-508

Kabir MA, Sherman F (2008) Overexpressed ribosomal proteins suppress defective chaperonins in Saccharomyces cerevisiae. FEMS Yeast Res, 8:1236-44

Polevoda B, Sherman F (2007) Methylation of proteins involved in translation. Mol Microbiol, 65:590-606

Das B, Das S, Sherman F (2006) Mutant LYS2 mRNAs retained and degraded in the nucleus of Saccharomyces cerevisiae. Proc Natl Acad Sci U S A, 103:10871-6

Polevoda B, Panciera Y, Brown SP, Wei J, Sherman F (2006) Phenotypes of yeast mutants lacking the mitochondrial protein Pet20p. Yeast, 23:127-39

Polevoda B, Span L, Sherman F (2006) The yeast translation release factors Mrf1p and Sup45p (eRF1) are methylated, respectively, by the methyltransferases Mtq1p and Mtq2p. J Biol Chem, 281:2562-71

Kuai L, Das B, Sherman F (2005) A nuclear degradation pathway controls the abundance of normal mRNAs in Saccharomyces cerevisiae. Proc Natl Acad Sci U S A, 102:13962-7

Greenberg JR, Price NP, Oliver RP, Sherman F, Rustchenko E (2005) Candida albicans SOU1 encodes a sorbose reductase required for L-sorbose utilization. Yeast, 22:957-69

Gao Q, Das B, Sherman F, Maquat LE (2005) Cap-binding protein 1-mediated and eukaryotic translation initiation factor 4E-mediated pioneer rounds of translation in yeast. Proc Natl Acad Sci U S A, 102:4258-63

Sherman F (2005) The importance of mutation, then and now: studies with yeast cytochrome c. Mutat Res, 589:1-16

Kabir MA, Kaminska J, Segel GB, Bethlendy G, Lin P, Della Seta F, Blegen C, Swiderek KM, Zoladek T, Arndt KT, Sherman F (2005) Physiological effects of unassembled chaperonin Cct subunits in the yeast Saccharomyces cerevisiae. Yeast, 22:219-39

Chen X, Moerschell RP, Pearce DA, Ramanan DD, Sherman F (2005) Enhanced mitochondrial degradation of yeast cytochrome c with amphipathic structures. Curr Genet, 47:67-83

Kabir MA, Kaminska J, Segel GB, Bethlendy G, Lin P, Della Seta F, Blegen C, Swiderek KM, Zoladek T, Arndt KT, Sherman F (2005) Physiological effects of unassembled chaperonin Cct subunits in the yeast Saccharomyces cerevisiae. Yeast, 22:219-39

Polevoda B, Span L, Sherman F (2005) The yeast translation release factors Mrf1p and Sup45p (eRF1) are methylated, respectively, by the methyltransferases Mtq1p and Mtq2p. J Biol Chem,

 
     
 

Graduate Degree Programs

 
 

Graduate students in my laboratory work toward a Ph.D. degree in the following program[s]:

 
 


Ph.D. in Biochemistry
Ph.D. in Biophysics
Ph.D. in Genetics
Ph.D. in Microbiology and Immunology

 
 

Ph.D. candidates in my laboratory may also be affiliated with these programs:

 
 
click here to learn more and to apply to graduate school
 
     
 

Contact Information

E-Mail: Fred_Sherman@urmc.rochester.edu

Fred Sherman
Department of Biochemistry and Biophysics
University of Rochester School of Medicine and Dentistry
601 Elmwood Ave, Box 712
Rochester, New York 14642

Office: Medical Center 1-6806
Telephone: (585) 275-6647; Fax: (585) 275-6007

 
     



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