[1]
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NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Liver;
DOI=10.1021/bi00291a001; PubMed=6606438 [NCBI, ExPASy, EBI, Israel, Japan]
Chandra T.,
Stackhouse R.,
Kidd V.J.,
Robson K.J.H.,
Woo S.L.C.;
"Sequence homology between human alpha 1-antichymotrypsin, alpha 1-antitrypsin, and antithrombin III.";
Biochemistry 22:5055-5061(1983).
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[2]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA], INVOLVEMENT IN COPD, AND VARIANTS BOCHUM-1 PRO-78 AND BONN-1 ALA-252.
DOI=10.1006/geno.1993.1396; PubMed=8244391 [NCBI, ExPASy, EBI, Israel, Japan]
Poller W.,
Faber J.-P.,
Weidinger S.,
Tief K.,
Scholz S.,
Fischer M.,
Olek K.,
Kirchgesser M.,
Heidtmann H.-H.;
"A leucine-to-proline substitution causes a defective alpha 1-antichymotrypsin allele associated with familial obstructive lung disease.";
Genomics 17:740-743(1993).
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[3]
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NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-9.
Kim J.W.;
"Identification of a human cell growth inhibiting gene.";
Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
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[4]
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NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT THR-9.
TISSUE=Brain;
Totoki Y.,
Toyoda A.,
Takeda T.,
Sakaki Y.,
Tanaka A.,
Yokoyama S.,
Ohara O.,
Nagase T.,
Kikuno F.R.;
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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[5]
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NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANTS THR-9 AND ARG-267.
TISSUE=Brain, Liver, and Skin;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
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[6]
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NUCLEOTIDE SEQUENCE [MRNA] OF 1-46, AND TISSUE SPECIFICITY.
TISSUE=Liver;
DOI=10.1016/0092-8674(88)90462-X; PubMed=3257719 [NCBI, ExPASy, EBI, Israel, Japan]
Abraham C.R.,
Selkoe D.J.,
Potter H.;
"Immunochemical identification of the serine protease inhibitor alpha 1-antichymotrypsin in the brain amyloid deposits of Alzheimer's disease.";
Cell 52:487-501(1988).
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[7]
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NUCLEOTIDE SEQUENCE [MRNA] OF 17-423 (ISOFORM 1), AND TISSUE SPECIFICITY.
TISSUE=Hippocampus;
DOI=10.1074/jbc.274.3.1821; PubMed=9880565 [NCBI, ExPASy, EBI, Israel, Japan]
Hwang S.-R.,
Steineckert B.,
Kohn A.,
Palkovits M.,
Hook V.Y.H.;
"Molecular studies define the primary structure of alpha1-antichymotrypsin (ACT) protease inhibitor in Alzheimer's disease brains. Comparison of act in hippocampus and liver.";
J. Biol. Chem. 274:1821-1827(1999).
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[8]
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NUCLEOTIDE SEQUENCE [MRNA] OF 22-86 AND 130-423 (ISOFORM 1).
Rubin H.;
Submitted (OCT-1989) to the EMBL/GenBank/DDBJ databases.
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[9]
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PROTEIN SEQUENCE OF N-TERMINUS.
DOI=10.1016/0167-4838(89)90139-8; PubMed=2787670 [NCBI, ExPASy, EBI, Israel, Japan]
Lindmark B.,
Hilja H.,
Alan R.,
Eriksson S.;
"The microheterogeneity of desialylated alpha 1-antichymotrypsin: the occurrence of two amino-terminal isoforms, one lacking a His-Pro dipeptide.";
Biochim. Biophys. Acta 997:90-95(1989).
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[10]
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NUCLEOTIDE SEQUENCE [MRNA] OF 36-45.
PubMed=7521171 [NCBI, ExPASy, EBI, Israel, Japan]
Korzus E.,
Luisetti M.,
Travis J.;
"Interactions of alpha-1-antichymotrypsin, alpha-1-proteinase inhibitor, and alpha-2-macroglobulin with the fungal enzyme, seaprose.";
Biol. Chem. Hoppe-Seyler 375:335-341(1994).
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[11]
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PROTEIN SEQUENCE OF 41-60.
DOI=10.1016/0006-291X(83)90325-X; PubMed=6687683 [NCBI, ExPASy, EBI, Israel, Japan]
Morii M.,
Travis J.;
"Structural alterations in alpha 1-antichymotrypsin from normal and acute phase human plasma.";
Biochem. Biophys. Res. Commun. 111:438-443(1983).
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[12]
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NUCLEOTIDE SEQUENCE [MRNA] OF 87-129 (ISOFORMS 1/2), AND FUNCTION.
TISSUE=Liver;
PubMed=2404007 [NCBI, ExPASy, EBI, Israel, Japan]
Rubin H.,
Wang Z.,
Nickbarg E.B.,
McLarney S.,
Naidoo N.,
Schoenberger O.L.,
Johnson J.L.,
Cooperman B.S.;
"Cloning, expression, purification, and biological activity of recombinant native and variant human alpha 1-antichymotrypsins.";
J. Biol. Chem. 265:1199-1207(1990).
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[13]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 205-423.
DOI=10.1038/311175a0; PubMed=6547997 [NCBI, ExPASy, EBI, Israel, Japan]
Hill R.E.,
Shaw P.H.,
Boyd P.A.,
Baumann H.,
Hastie N.D.;
"Plasma protease inhibitors in mouse and man: divergence within the reactive centre regions.";
Nature 311:175-177(1984).
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[14]
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ACTIVE SITE.
PubMed=6556193 [NCBI, ExPASy, EBI, Israel, Japan]
Morii M.,
Travis J.;
"Amino acid sequence at the reactive site of human alpha 1-antichymotrypsin.";
J. Biol. Chem. 258:12749-12752(1983).
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[15]
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GLYCOSYLATION AT ASN-93 AND ASN-106.
DOI=10.1038/nbt827; PubMed=12754519 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang H.,
Li X.-J.,
Martin D.B.,
Aebersold R.;
"Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry.";
Nat. Biotechnol. 21:660-666(2003).
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[16]
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INTERACTION WITH DNAJC1.
DOI=10.1074/jbc.M310903200; PubMed=14668352 [NCBI, ExPASy, EBI, Israel, Japan]
Kroczynska B.,
Evangelista C.M.,
Samant S.S.,
Elguindi E.C.,
Blond S.Y.;
"The SANT2 domain of the murine tumor cell DnaJ-like protein 1 human homologue interacts with alpha1-antichymotrypsin and kinetically interferes with its serpin inhibitory activity.";
J. Biol. Chem. 279:11432-11443(2004).
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[17]
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REGION RCL.
DOI=10.1007/s00239-004-2640-9; PubMed=15638460 [NCBI, ExPASy, EBI, Israel, Japan]
Horvath A.J.,
Forsyth S.L.,
Coughlin P.B.;
"Expression patterns of murine antichymotrypsin-like genes reflect evolutionary divergence at the Serpina3 locus.";
J. Mol. Evol. 59:488-497(2004).
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[18]
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GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-93, AND MASS SPECTROMETRY.
TISSUE=Plasma;
DOI=10.1002/pmic.200300556; PubMed=14760718 [NCBI, ExPASy, EBI, Israel, Japan]
Bunkenborg J.,
Pilch B.J.,
Podtelejnikov A.V.,
Wisniewski J.R.;
"Screening for N-glycosylated proteins by liquid chromatography mass spectrometry.";
Proteomics 4:454-465(2004).
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[19]
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GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-33; ASN-93; ASN-106; ASN-127; ASN-186 AND ASN-271, AND MASS SPECTROMETRY.
TISSUE=Plasma;
DOI=10.1021/pr0502065; PubMed=16335952 [NCBI, ExPASy, EBI, Israel, Japan]
Liu T.,
Qian W.-J.,
Gritsenko M.A.,
Camp D.G. II,
Monroe M.E.,
Moore R.J.,
Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
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[20]
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X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 24-423.
DOI=10.1016/0022-2836(91)90704-A; PubMed=2016749 [NCBI, ExPASy, EBI, Israel, Japan]
Baumann U.,
Huber R.,
Bode W.,
Grosse D.,
Lesjak M.,
Laurell C.-B.;
"Crystal structure of cleaved human alpha 1-antichymotrypsin at 2.7-A resolution and its comparison with other serpins.";
J. Mol. Biol. 218:595-606(1991).
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[21]
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X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF 43-423 OF MUTANTS ARG-370 AND ARG-372.
DOI=10.1038/nsb1096-888; PubMed=8836107 [NCBI, ExPASy, EBI, Israel, Japan]
Lukacs C.M.,
Zhong J.Q.,
Plotnick M.I.,
Rubin H.,
Cooperman B.S.,
Christianson D.W.;
"Arginine substitutions in the hinge region of antichymotrypsin affect serpin beta-sheet rearrangement.";
Nat. Struct. Biol. 3:888-893(1996).
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[22]
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X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 43-423 OF MUTANTS ARG-370; ARG-372 AND ARG-374.
DOI=10.1021/bi972359e; PubMed=9521649 [NCBI, ExPASy, EBI, Israel, Japan]
Lukacs C.M.,
Rubin H.,
Christianson D.W.;
"Engineering an anion-binding cavity in antichymotrypsin modulates the 'spring-loaded' serpin-protease interaction.";
Biochemistry 37:3297-3304(1998).
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[23]
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X-RAY CRYSTALLOGRAPHY (2.27 ANGSTROMS) OF 26-423.
DOI=10.1073/pnas.97.1.67; PubMed=10618372 [NCBI, ExPASy, EBI, Israel, Japan]
Gooptu B.,
Hazes B.,
Chang W.-S.W.,
Dafforn T.R.,
Carrell R.W.,
Read R.J.,
Lomas D.A.;
"Inactive conformation of the serpin alpha(1)-antichymotrypsin indicates two-stage insertion of the reactive loop: implications for inhibitory function and conformational disease.";
Proc. Natl. Acad. Sci. U.S.A. 97:67-72(2000).
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[24]
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VARIANT ISEHARA-1 VAL-401.
DOI=10.1016/0014-5793(92)80590-D; PubMed=1618300 [NCBI, ExPASy, EBI, Israel, Japan]
Tsuda M.,
Sei Y.,
Yamamura M.,
Yamamoto M.,
Shinohara Y.;
"Detection of a new mutant alpha-1-antichymotrypsin in patients with occlusive-cerebrovascular disease.";
FEBS Lett. 304:66-68(1992).
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[25]
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VARIANT BONN-1 ALA-252.
DOI=10.1016/0140-6736(92)91301-N; PubMed=1351206 [NCBI, ExPASy, EBI, Israel, Japan]
Poller W.,
Faber J.-P.,
Scholz S.,
Weindinger S.,
Bartholome K.,
Olek K.,
Eriksson S.;
"Mis-sense mutation of alpha 1-antichymotrypsin gene associated with chronic lung disease.";
Lancet 339:1538-1538(1992).
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[26]
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VARIANT VAL-401.
DOI=10.1007/s100380170125; PubMed=11289720 [NCBI, ExPASy, EBI, Israel, Japan]
Tachikawa H.,
Tsuda M.,
Onoe K.,
Ueno M.,
Takagi S.,
Shinohara Y.;
"Alpha-1-antichymotrypsin gene A1252G variant (ACT Isehara-1) is associated with a lacunar type of ischemic cerebrovascular disease.";
J. Hum. Genet. 46:45-47(2001).
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