[1]
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NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 314-337; 347-363 AND 424-441.
TISSUE=Neutrophil;
PubMed=2164002 [NCBI, ExPASy, EBI, Israel, Japan]
Hasty K.A.,
Pourmotabbed T.F.,
Goldberg G.I.,
Thompson J.P.,
Spinella D.G.,
Stevens R.M.,
Mainardi C.L.;
"Human neutrophil collagenase. A distinct gene product with homology to other matrix metalloproteinases.";
J. Biol. Chem. 265:11421-11424(1990).
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[2]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS CYS-3; ILE-32; GLU-87; GLU-154; VAL-193; TYR-246; ALA-436 AND THR-460.
Livingston R.J.,
Rieder M.J.,
Shaffer T.,
Bertucci C.,
Baier C.N.,
Rajkumar N.,
Willa H.T.,
Daniels M.,
Downing T.K.,
Stanaway I.B.,
Nguyen C.P.,
Gildersleeve H.,
Cassidy C.M.,
Johnson E.J.,
Swanson J.E.,
McFarland I.,
Yool B.,
Park C.,
Nickerson D.A.;
"NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu).";
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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[3]
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NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
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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[4]
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PROTEIN SEQUENCE OF 21-140, AND VARIANT ILE-32.
TISSUE=Neutrophil;
PubMed=2159879 [NCBI, ExPASy, EBI, Israel, Japan]
Knaeuper V.,
Kraemer S.,
Reinke H.,
Tschesche H.;
"Characterization and activation of procollagenase from human polymorphonuclear leucocytes. N-terminal sequence determination of the proenzyme and various proteolytically activated forms.";
Eur. J. Biochem. 189:295-300(1990).
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[5]
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PROTEIN SEQUENCE OF 21-103.
TISSUE=Neutrophil;
PubMed=1662606 [NCBI, ExPASy, EBI, Israel, Japan]
Blaeser J.,
Knaeuper V.,
Osthues A.,
Reinke H.,
Tschesche H.;
"Mercurial activation of human polymorphonuclear leucocyte procollagenase.";
Eur. J. Biochem. 202:1223-1230(1991).
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[6]
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PROTEIN SEQUENCE OF 85-120, AND CHARACTERIZATION.
TISSUE=Neutrophil;
DOI=10.1021/bi00499a008; PubMed=2176876 [NCBI, ExPASy, EBI, Israel, Japan]
Mallya S.K.,
Mookthiar K.A.,
Gao Y.,
Brew K.,
Dioszegi M.,
Birkedal-Hansen H.,
van Wart H.E.;
"Characterization of 58-kilodalton human neutrophil collagenase: comparison with human fibroblast collagenase.";
Biochemistry 29:10628-10634(1990).
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[7]
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PARTIAL PROTEIN SEQUENCE.
PubMed=2169256 [NCBI, ExPASy, EBI, Israel, Japan]
Knaeuper V.,
Kraemer S.,
Reinke H.,
Tschesche H.;
"Partial amino acid sequence of human PMN leukocyte procollagenase.";
Biol. Chem. Hoppe-Seyler 371:295-304(1990).
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[8]
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ERRATUM.
PubMed=2169766 [NCBI, ExPASy, EBI, Israel, Japan]
Knaeuper V.,
Kraemer S.,
Reinke H.,
Tschesche H.;
Biol. Chem. Hoppe-Seyler 371:733-733(1990).
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[9]
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CYSTEINE-SWITCH MECHANISM.
TISSUE=Neutrophil;
DOI=10.1016/0014-5793(92)81184-N; PubMed=1330697 [NCBI, ExPASy, EBI, Israel, Japan]
Blaeser J.,
Triebel S.,
Reinke H.,
Tschesche H.;
"Formation of a covalent Hg-Cys-bond during mercurial activation of PMNL procollagenase gives evidence of a cysteine-switch mechanism.";
FEBS Lett. 313:59-61(1992).
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[10]
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X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 100-262.
PubMed=8137810 [NCBI, ExPASy, EBI, Israel, Japan]
Bode W.,
Reinemer P.,
Huber R.,
Klein T.,
Schnierer S.,
Tschesche H.;
"The X-ray crystal structure of the catalytic domain of human neutrophil collagenase inhibited by a substrate analogue reveals the essentials for catalysis and specificity.";
EMBO J. 13:1263-1269(1994).
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[11]
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X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 100-262.
DOI=10.1016/0014-5793(94)80370-6; PubMed=8307185 [NCBI, ExPASy, EBI, Israel, Japan]
Reinemer P.,
Grams F.,
Huber R.,
Kleine T.,
Schnierer S.,
Piper M.,
Tschesche H.,
Bode W.;
"Structural implications for the role of the N-terminus in the 'superactivation' of collagenases. A crystallographic study.";
FEBS Lett. 338:227-233(1994).
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[12]
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X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 100-262.
DOI=10.1038/nsb0294-119; PubMed=7656015 [NCBI, ExPASy, EBI, Israel, Japan]
Stams T.,
Spurlino J.C.,
Smith D.L.,
Wahl R.C.,
Ho T.F.,
Qoronfleh M.W.,
Banks T.M.,
Rubin B.;
"Structure of human neutrophil collagenase reveals large S1' specificity pocket.";
Nat. Struct. Biol. 1:119-123(1994).
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[13]
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X-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS) OF 100-262.
PubMed=9249047 [NCBI, ExPASy, EBI, Israel, Japan]
Betz M.,
Huxley P.,
Davies S.J.,
Mushtaq Y.,
Pieper M.,
Tschesche H.,
Bode W.,
Gomis-Rueth F.-X.;
"1.8-A crystal structure of the catalytic domain of human neutrophil collagenase (matrix metalloproteinase-8) complexed with a peptidomimetic hydroxamate primed-side inhibitor with a distinct selectivity profile.";
Eur. J. Biochem. 247:356-363(1997).
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[14]
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X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 105-262.
PubMed=9655333 [NCBI, ExPASy, EBI, Israel, Japan]
Brandstetter H.,
Engh R.A.,
von Roedern E.G.,
Moroder L.,
Huber R.,
Bode W.,
Grams F.;
"Structure of malonic acid-based inhibitors bound to human neutrophil collagenase. A new binding mode explains apparently anomalous data.";
Protein Sci. 7:1303-1309(1998).
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