[1]
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NUCLEOTIDE SEQUENCE [MRNA].
Relle M.;
Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
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[2]
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NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta, Skin, Spleen, and Testis;
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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[3]
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NUCLEOTIDE SEQUENCE [MRNA] OF 8-253.
PubMed=1374388 [NCBI, ExPASy, EBI, Israel, Japan]
White R.T.,
Damm D.,
Hancock N.,
Rosen B.S.,
Lowell B.B.,
Usher P.,
Flier J.S.,
Spiegelman B.M.;
"Human adipsin is identical to complement factor D and is expressed at high levels in adipose tissue.";
J. Biol. Chem. 267:9210-9213(1992).
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[4]
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PROTEIN SEQUENCE OF 26-252.
DOI=10.1021/bi00306a025; PubMed=6383466 [NCBI, ExPASy, EBI, Israel, Japan]
Niemann M.A.,
Bhown A.S.,
Bennett J.C.,
Volanakis J.E.;
"Amino acid sequence of human D of the alternative complement pathway.";
Biochemistry 23:2482-2486(1984).
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[5]
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PARTIAL PROTEIN SEQUENCE OF 26-252.
DOI=10.1016/0014-5793(84)80110-6; PubMed=6363133 [NCBI, ExPASy, EBI, Israel, Japan]
Johnson D.M.A.,
Gagnon J.,
Reid K.B.M.;
"Amino acid sequence of human factor D of the complement system. Similarity in sequence between factor D and proteases of non-plasma origin.";
FEBS Lett. 166:347-351(1984).
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[6]
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PARTIAL PROTEIN SEQUENCE OF 26-82.
PubMed=6987665 [NCBI, ExPASy, EBI, Israel, Japan]
Volanakis J.E.,
Bhown A.S.,
Bennett J.C.,
Mole J.E.;
"Partial amino acid sequence of human factor D: homology with serine proteases.";
Proc. Natl. Acad. Sci. U.S.A. 77:1116-1119(1980).
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[7]
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PARTIAL PROTEIN SEQUENCE OF 26-78.
PubMed=6776531 [NCBI, ExPASy, EBI, Israel, Japan]
Davis A.E. III;
"Active site amino acid sequence of human factor D.";
Proc. Natl. Acad. Sci. U.S.A. 77:4938-4942(1980).
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[8]
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PARTIAL PROTEIN SEQUENCE OF 26-61 AND 194-220.
PubMed=6821372 [NCBI, ExPASy, EBI, Israel, Japan]
Johnson D.M.A.,
Gagnon J.,
Reid K.B.M.;
"Factor D of the alternative pathway of human complement. Purification, alignment and N-terminal amino acid sequences of the major cyanogen bromide fragments, and localization of the serine residue at the active site.";
Biochem. J. 187:863-874(1980).
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[9]
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X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
DOI=10.1006/jmbi.1994.1021; PubMed=8289289 [NCBI, ExPASy, EBI, Israel, Japan]
Narayana S.V.L.,
Carson M.,
El-Kabbani O.,
Kilpatrick J.M.,
Moore D.,
Chen X.,
Bugg C.E.,
Volanakis J.E.,
Delucas L.J.;
"Structure of human factor D. A complement system protein at 2.0-A resolution.";
J. Mol. Biol. 235:695-708(1994).
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[10]
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X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
DOI=10.1074/jbc.270.41.24399; PubMed=7592653 [NCBI, ExPASy, EBI, Israel, Japan]
Kim S.,
Narayana S.V.,
Volanakis J.E.;
"Crystal structure of a complement factor D mutant expressing enhanced catalytic activity.";
J. Biol. Chem. 270:24399-24405(1995).
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[11]
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VARIANTS COMPLEMENT FACTOR D DEFICIENCY GLY-213 AND ARG-214.
DOI=10.1182/blood-2005-07-2820; PubMed=16527897 [NCBI, ExPASy, EBI, Israel, Japan]
Sprong T.,
Roos D.,
Weemaes C.,
Neeleman C.,
Geesing C.L.,
Mollnes T.E.,
van Deuren M.;
"Deficient alternative complement pathway activation due to factor D deficiency by 2 novel mutations in the complement factor D gene in a family with meningococcal infections.";
Blood 107:4865-4870(2006).
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