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Michael Smith, Ph.D.

Affiliations: 
University of British Columbia University of British Columbia, Vancouver, Vancouver, BC, Canada 
Area:
Nucleic acid chemistry
Website:
http://www.nobelprize.org/nobel_prizes/chemistry/laureates/1993/smith-bio.html
Google:
"chemistry nucleic acid site directed mutagenesis"
Bio:

(1932 - 2000)
http://www.nasonline.org/member-directory/deceased-members/3001741.html
http://www.science.ca/scientists/scientistprofile.php?pID=18
http://www.msl.ubc.ca/about/michaelsmith
http://en.wikipedia.org/wiki/Michael_Smith_%28chemist%29
The Nobel Prize in Chemistry 1993 was awarded "for contributions to the developments of methods within DNA-based chemistry" jointly with one half to Kary B. Mullis "for his invention of the polymerase chain reaction (PCR) method" and with one half to Michael Smith "for his fundamental contributions to the establishment of oligonucleotide-based, site-directed mutagenesis and its development for protein studies".

Mean distance: 7.85
 
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Publications

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Zhao EE, Liu YF, Oyer SL, et al. (2019) Chondrosarcoma Arising in the Mastoid Involving the Intratemporal Facial Nerve. Jama Otolaryngology-- Head & Neck Surgery
Smith M. (1994) Synthetic DNA and Biology Bioscience Reports. 14: 51-66
Thurgood AG, Pielak GJ, Cutler RL, et al. (1991) Change in charge of an unvaried heme contact residue does not cause a major change of conformation in cytochrome c. Febs Letters. 284: 173-7
Ner SS, Goodin DB, Pielak GJ, et al. (1988) A rapid droplet method for Sanger dideoxy sequencing. Biotechniques. 6: 408, 410, 412
Louie GV, Pielak GJ, Smith M, et al. (1988) Role of phenylalanine-82 in yeast iso-1-cytochrome c and remote conformational changes induced by a serine residue at this position. Biochemistry. 27: 7870-6
Liang N, Mauk AG, Pielak GJ, et al. (1988) Regulation of interprotein electron transfer by residue 82 of yeast cytochrome c. Science (New York, N.Y.). 240: 311-3
Liang N, Pielak GJ, Mauk AG, et al. (1987) Yeast cytochrome c with phenylalanine or tyrosine at position 87 transfers electrons to (zinc cytochrome c peroxidase)+ at a rate ten thousand times that of the serine-87 or glycine-87 variants. Proceedings of the National Academy of Sciences of the United States of America. 84: 1249-52
Cutler RL, Pielak GJ, Mauk AG, et al. (1987) Replacement of cysteine-107 of Saccharomyces cerevisiae iso-1-cytochrome c with threonine: improved stability of the mutant protein. Protein Engineering. 1: 95-9
Russell DW, Jensen R, Zoller MJ, et al. (1986) Structure of the Saccharomyces cerevisiae HO gene and analysis of its upstream regulatory region. Molecular and Cellular Biology. 6: 4281-94
Pielak GJ, Mauk AG, Smith M. (1985) Site-directed mutagenesis of cytochrome c shows that an invariant Phe is not essential for function. Nature. 313: 152-4
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