[1]
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NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1038/273723a0; PubMed=661981 [NCBI, ExPASy, EBI, Israel, Japan]
McReynolds L.,
O'Malley B.W.,
Nisbet A.D.,
Fothergill J.E.,
Givol D.,
Fields S.,
Robertson M.,
Brownlee G.G.;
"Sequence of chicken ovalbumin mRNA.";
Nature 273:723-728(1978).
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[2]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1038/275510a0; PubMed=692731 [NCBI, ExPASy, EBI, Israel, Japan]
Catterall J.F.,
O'Malley B.W.,
Robertson M.A.,
Staden R.,
Tanaka Y.,
Brownlee G.G.;
"Nucleotide sequence homology at 12 intron-exon junctions in the chick ovalbumin gene.";
Nature 275:510-513(1978).
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[3]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1021/bi00525a024; PubMed=6272839 [NCBI, ExPASy, EBI, Israel, Japan]
Woo S.L.C.,
Beattie W.G.,
Catterall J.F.,
Dugaiczyk A.,
Staden R.,
Brownlee G.G.,
O'Malley B.W.;
"Complete nucleotide sequence of the chicken chromosomal ovalbumin gene and its biological significance.";
Biochemistry 20:6437-6446(1981).
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[4]
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NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT PHE-283.
STRAIN=Mangyondak;
Kim R.,
Rim D.,
Li Y.;
"Ovalbumin from the chicken called Mangyondak in North Korea.";
Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
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[5]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-155.
DOI=10.1038/278370a0; PubMed=423993 [NCBI, ExPASy, EBI, Israel, Japan]
Robertson M.A.,
Staden R.,
Tanaka Y.,
Catterall J.F.,
O'Malley B.W.,
Brownlee G.G.;
"Sequence of three introns in the chick ovalbumin gene.";
Nature 278:370-372(1979).
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[6]
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PROTEIN SEQUENCE OF 2-36, AND ACETYLATION AT GLY-2.
PubMed=272676 [NCBI, ExPASy, EBI, Israel, Japan]
Palmiter R.D.,
Gagnon J.,
Walsh K.A.;
"Ovalbumin: a secreted protein without a transient hydrophobic leader sequence.";
Proc. Natl. Acad. Sci. U.S.A. 75:94-98(1978).
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[7]
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PROTEIN SEQUENCE OF 2-17, AND ACETYLATION AT GLY-2.
PubMed=751625 [NCBI, ExPASy, EBI, Israel, Japan]
Thompson E.O.P.,
Fisher W.K.;
"A correction and extension of the acetylated amino terminal sequence of ovalbumin.";
Aust. J. Biol. Sci. 31:443-446(1978).
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[8]
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PROTEIN SEQUENCE OF 6-17; 30-36; 61-79; 116-124; 367-374 AND 380-386.
PubMed=751624 [NCBI, ExPASy, EBI, Israel, Japan]
Thompson E.O.P.,
Fisher W.K.;
"Amino acid sequences containing half-cystine residues in ovalbumin.";
Aust. J. Biol. Sci. 31:433-442(1978).
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[9]
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PROTEIN SEQUENCE OF 60-85 AND 338-360, AND PHOSPHORYLATION AT SER-69 AND SER-345.
PubMed=6783411 [NCBI, ExPASy, EBI, Israel, Japan]
Henderson J.Y.,
Moir A.J.G.,
Fothergill L.A.,
Fothergill J.E.;
"Sequences of sixteen phosphoserine peptides from ovalbumins of eight species.";
Eur. J. Biochem. 114:439-450(1981).
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[10]
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FUNCTION OF THE UNCLEAVED SIGNAL PEPTIDE.
PubMed=6749856 [NCBI, ExPASy, EBI, Israel, Japan]
Meek R.L.,
Walsh K.A.,
Palmiter R.D.;
"The signal sequence of ovalbumin is located near the NH2 terminus.";
J. Biol. Chem. 257:12245-12251(1982).
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[11]
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FUNCTION OF THE UNCLEAVED SIGNAL PEPTIDE.
DOI=10.1016/0014-5793(86)80751-7; PubMed=3732511 [NCBI, ExPASy, EBI, Israel, Japan]
Robinson A.,
Meredith C.,
Austen B.M.;
"Isolation and properties of the signal region from ovalbumin.";
FEBS Lett. 203:243-246(1986).
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[12]
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REVIEW.
PubMed=11419711 [NCBI, ExPASy, EBI, Israel, Japan]
Huntington J.A.,
Stein P.E.;
"Structure and properties of ovalbumin.";
J. Chromatogr. B 756:189-198(2001).
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[13]
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X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS).
DOI=10.1038/347099a0; PubMed=2395463 [NCBI, ExPASy, EBI, Israel, Japan]
Stein P.E.,
Leslie A.G.W.,
Finch J.T.,
Turnell W.G.,
McLaughlin P.J.,
Carrell R.W.;
"Crystal structure of ovalbumin as a model for the reactive centre of serpins.";
Nature 347:99-102(1990).
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[14]
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X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS).
DOI=10.1016/0022-2836(91)80185-W; PubMed=1942038 [NCBI, ExPASy, EBI, Israel, Japan]
Stein P.E.,
Leslie A.G.W.,
Finch J.T.,
Carrell R.W.;
"Crystal structure of uncleaved ovalbumin at 1.95-A resolution.";
J. Mol. Biol. 221:941-959(1991).
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[15]
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X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
DOI=10.1016/S0022-2836(05)80212-8; PubMed=2352279 [NCBI, ExPASy, EBI, Israel, Japan]
Wright H.T.,
Qian H.X.,
Huber R.;
"Crystal structure of plakalbumin, a proteolytically nicked form of ovalbumin. Its relationship to the structure of cleaved alpha-1-proteinase inhibitor.";
J. Mol. Biol. 213:513-528(1990).
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