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FRISC: The Faculty Research Interests Science Comparator |
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Assistant Professor of Biochemistry
Biological
Chemistry
Phone: 214-648-3386
Fax: 214-648-9099
Building L; Room 4.247A
Email: grishin@chop.swmed.edu
We are interested in understanding proteins by means of theoretical methods.
The research areas cover (but are not limited to):
o Sequence and structure classification;
o Protein structure prediction;
o Molecular evolution;
o Construction and analysis of multiple sequence and structural alignments;
o Analysis of genomic data;
o Sequence-structure-function relationship in protein families.
The ultimate objective of computational biology is to classify available
sequence-structure data into a biologically relevant, hierarchical system
analogous to the one currently used in zoology and botany. Since sequence and
structural similarities usually imply functional similarity, such classification
is of indispensable value for biologists to aid in experimental design.
Our group combines sequence and structure analysis with evolutionary
considerations to facilitate discoveries of biological significance. Two major
directions are pursued: (i) development of new mathematical approaches for
analysis of protein sequence-structure data; and (ii) implementation of
available tools for solving biological problems by computer analysis. The
following publication list gives more specific ideas about what we do.
Selected Publications
J.J. Abbott, J. Pei, J.L. Ford, Y. Qi, V.N. Grishin, L.A. Pitcher, M.A.
Phillips, N.V. Grishin (2001) Structure prediction and active site
analysis of the metal binding determinants in {gamma}-glutamylcysteine
synthetase J. Biol. Chem. 2001 Aug 29
J. Pei and N.V. Grishin (2001) AL2CO: calculation of positional
conservation in a protein sequence alignment Bioinformatics 17(8):700-712
J. Pei and N.V. Grishin (2001) Type II CAAX prenyl endopeptidases belong
to a novel superfamily of putative membrane-bound metalloproteases Trends
Biochem Sci. 26(5):275-277
N.V. Grishin (2001) Treble clef finger--a functionally diverse
zinc-binding structural motif Nucleic Acids Res. 29(8):1703-1714
N.V. Grishin (2001) MH1 domain of Smad is a degraded homing endonuclease
J. Mol. Biol. 307(1):31-37
N.V. Grishin (2001) KH domain: one motif, two folds Nucleic Acid
Research. 29(3):638-643
M.M. Horvath and N.V. Grishin (2001) The C-terminal domain of E. coli HPII
catalase is a member of the type I glutamine amidotransferase superfamily
Proteins: Struct. Func. and Genetics, 42(2):230-236
J. Pei and N.V. Grishin (2001) GGDEF domain is homologous to adenylate
cyclase Proteins: Struct. Func. and Genetics, 42(2):210-216
M.Y. Galperin and N.V. Grishin (2000) N-terminal domains of
phosphotransacetylase and cobalamin biosynthesis enzymes CobB and CobQ belong to
a new family of ATP-dependent amidoligases, related to dethiobiotin synthase
Proteins: Struct. Func. and Genetics, 41(2):238-247
N.V. Grishin, Y.I. Wolf, and E.V. Koonin (2000) Phylogenetic analysis on
complete-genome scale using distributions of evolutionary rates among
proteins . Genome Res. 10(7):991-1000
X. Shao and N.V. Grishin (2000) Common fold in helix-hairpin-helix
proteins Nucleic Acid Reserach, 28(14):2643-2650
N.V. Grishin (2000) C-terminal domains of Escherichia coli topoisomerase I
belong to the zinc ribbon superfamily. J. Mol. Biol. 299(5):1165-1177.
Y.I. Wolf, N.V. Grishin, and E.V. Koonin (2000) Estimating the Number of
Protein Folds and Families from Complete Genome Data . J. Mol. Biol.
299(4):897-905.
N.V. Grishin (2000) Two tricks in one bundle: helix-turn-helix gains
enzymatic activity. Nucleic Acid Research, 28(11):2229-2233.
K.S. Makarova and N.V. Grishin (1999) Thermolysin and Mitochondrial Processing
Peptidase: How Far Structure-Functional Convergence Goes. Protein Science.
8(11):2537-2540
K.S. Makarova and N.V. Grishin (1999) The Zn-peptidase Superfamily: Functional
Convergence After Evolutionary Divergence. J. Mol. Biol., 292:11-17.
H. Zhang and N.V. Grishin (1999) The alpha subunit of protein prenyltransferases
is a member of the tetratricopeptide repat family. Protein Science, 8:1658-1667.
Y.I. Wolf, L. Aravind, N.V. Grishin, and E.V. Koonin (1999) Evolution of
aminoacyl-tRNA synthetases - analysis of synapomorphies and phylogenetic trees
reveals a complex history of horizontal gene transfer events. Genome Research,
9:689-710.
N.V. Grishin (1999) Phosphatidylinositol phosphate kinase - a link between
protein kinase and glutathione synthase folds. J. Mol. Biol. 291:239-2047.
N.V. Grishin (1999) A novel approach to phylogeny reconstruction from protein
sequences. J. Mol. Evol. 48:264-273.
N.V. Grishin (1998) R3H: a putative single-stranded nucleic acid-binding domain.
TIBS,. 23:329-330.
N.V. Grishin (1997) Estimation of evolutionary distances from protein spatial
structures. J. Mol. Evol. 45:359-369.
N.V. Grishin, M.A. Phillips, and E.J. Goldsmith (1995) Modeling of spatial
structure of eukaryotic ornithine decarboxylases. Protein Science, 4:1291-1304.
N.V. Grishin (1995) Estimation of the number of amino acid substitutions per
site when the substitution rate varies among sites. J. Mol. Evol. 41:675-679.
Extraction Method: Expand using Medical Synonyms-
Eliminated words list: MedlinePlus List
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Similarity Method: Weighted keyword count
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Database: Medline abstracts (1967 - Present)
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Publication Type: All
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Score Calculation Method: Cosine Similarity Method
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Sort by: Score
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Show: Top 100 hits
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Results computed on: 6/9/2006