Catherine Schein

Dr. Catherine Schein

orcid

Research Focus & Metrics

Academic Career Length

47Years (1980-Present)

(Calculated once Scilit publication data is synced: current year − year of first publication + 1)

Representative Publications

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1 March 1988 in Nature Biotechnology
Verified
Journal Article
Closed access
CSCatherine Schein
Catherine Schein
MNMathieu H. M. Noteborn
Mathieu H. M. Noteborn

1 January 2003 in Nucleic Acids Research
Verified
Journal Article
Closed access
OIOvidiu Ivanciuc
Ovidiu Ivanciuc
CSCatherine Schein
Catherine Schein
WBWerner Braun
Werner Braun
SDAP (Structural Database of Allergenic Proteins) is a web server that provides rapid, cross-referenced access to the sequences, structures and IgE epitopes of allergenic proteins. The SDAP core is a series of CGI scripts that process the user queries, interrogate the database, perform various computations related to protein allergenic determinants and prepare the output HTML pages. The database component of SDAP contains information about the allergen name, source, sequence, structure, IgE epitopes and literature references and easy links to the major protein (PDB, SWISS-PROT/TrEMBL, PIR-ALN, NCBI Taxonomy Browser) and literature (PubMed, MEDLINE) on-line servers. The computational component in SDAP uses an original algorithm based on conserved properties of amino acid side chains to identify regions of known allergens similar to user-supplied peptides or selected from the SDAP database of IgE epitopes. This and other bioinformatics tools can be used to rapidly determine potential cross-reactivities between allergens and to screen novel proteins for the presence of IgE epitopes they may share with known allergens. SDAP is available via the World Wide Web at http://fermi.utmb.edu/SDAP/.

1 April 1990 in Nature Biotechnology
Verified
Journal Article
Closed access
CSCatherine Schein
Catherine Schein

12 October 2007 in Bioinformatics
Verified
Journal Article
Closed access
SNSurendra S. Negi
Surendra S. Negi
CSCatherine Schein
Catherine Schein
NONuman Oezguen
Numan Oezguen
TPTrevor D. Power
Trevor D. Power
WBWerner Braun
Werner Braun
Summary: A new web server, InterProSurf, predicts interacting amino acid residues in proteins that are most likely to interact with other proteins, given the 3D structures of subunits of a protein complex. The prediction method is based on solvent accessible surface area of residues in the isolated subunits, a propensity scale for interface residues and a clustering algorithm to identify surface regions with residues of high interface propensities. Here we illustrate the application of InterProSurf to determine which areas of Bacillus anthracis toxins and measles virus hemagglutinin protein interact with their respective cell surface receptors. The computationally predicted regions overlap with those regions previously identified as interface regions by sequence analysis and mutagenesis experiments.Availability: The InterProSurf web server is available at http://curie.utmb.edu/Contact: webraun@utmb.eduSupplementary information: Other test examples are available as Supplementary Material at Bioinformatics online.

1 November 1989 in Nature Biotechnology
Verified
Journal Article
Closed access
PDF file
CSCatherine Schein
Catherine Schein

1 May 1983 in Gene
Verified
Journal Article
Closed access
IPIlkka Palva
Ilkka Palva
PLPäivi Lehtovaara
Päivi Lehtovaara
LKLeevi Kääriäinen
Leevi Kääriäinen
MSMervi Sibakov
Mervi Sibakov
KCKari Cantell
Kari Cantell
CWCharles Weissmann
Charles Weissmann