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English
Structural basis for binding of Smac/DIABLO to the XIAP BIR3 domain
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title
Structural basis for binding of Smac/DIABLO to the XIAP BIR3 domain
(English)
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author name string
Z Liu
series ordinal
1
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C Sun
series ordinal
2
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E T Olejniczak
series ordinal
3
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R P Meadows
series ordinal
4
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S F Betz
series ordinal
5
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T Oost
series ordinal
6
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J Herrmann
series ordinal
7
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J C Wu
series ordinal
8
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S W Fesik
series ordinal
9
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language of work or name
English
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publication date
December 2000
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PubMed
published in
Nature
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volume
408
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issue
6815
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page(s)
1004-8
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cites work
An apoptosis-inhibiting baculovirus gene with a zinc finger-like motif
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Inhibition of interleukin 1 beta-converting enzyme-mediated apoptosis of mammalian cells by baculovirus IAP.
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X-linked IAP is a direct inhibitor of cell-death proteases
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The c-IAP-1 and c-IAP-2 proteins are direct inhibitors of specific caspases
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Cleavage of human inhibitor of apoptosis protein XIAP results in fragments with distinct specificities for caspases
1 reference
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Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition
1 reference
stated in
Crossref
reference URL
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retrieved
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inferred from DOI database lookup
Identification of DIABLO, a mammalian protein that promotes apoptosis by binding to and antagonizing IAP proteins
1 reference
stated in
Crossref
reference URL
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retrieved
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inferred from DOI database lookup
Molecular determinants of the caspase-promoting activity of Smac/DIABLO and its role in the death receptor pathway
1 reference
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Crossref
reference URL
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Structural and biochemical basis of apoptotic activation by Smac/DIABLO
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The inhibitors of apoptosis (IAPs) and their emerging role in cancer
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NMR structure and mutagenesis of the inhibitor-of-apoptosis protein XIAP
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reference URL
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NMR structure and mutagenesis of the third Bir domain of the inhibitor of apoptosis protein XIAP
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A methionine aminopeptidase and putative regulator of translation initiation is required for cell growth and patterning in Drosophila
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Multidimensional heteronuclear nuclear magnetic resonance of proteins
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Torsion-angle molecular dynamics as a new efficient tool for NMR structure calculation.
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Determination of three-dimensional structures of proteins by simulated annealing with interproton distance restraints. Application to crambin, potato carboxypeptidase inhibitor and barley serine proteinase inhibitor 2.
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Automated NOESY interpretation with ambiguous distance restraints: the refined NMR solution structure of the pleckstrin homology domain from beta-spectrin
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AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR
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Identifiers
DOI
10.1038/35050006
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
3376132
Dimensions Publication ID
1043306363
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Fatcat ID
release_r3h4wwgspvfpfjkdijj4j2jpfa
0 references
OpenCitations bibliographic resource ID
3376132
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
3376132
PubMed publication ID
11140637
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
3376132
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