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3gqf
From Proteopedia
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[[Image:3gqf.png|left|200px]] | [[Image:3gqf.png|left|200px]] | ||
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{{STRUCTURE_3gqf| PDB=3gqf | SCENE= }} | {{STRUCTURE_3gqf| PDB=3gqf | SCENE= }} | ||
===Structural and Biophysical Properties of the Pathogenic SOD1 Variant H46R/H48Q=== | ===Structural and Biophysical Properties of the Pathogenic SOD1 Variant H46R/H48Q=== | ||
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{{ABSTRACT_PUBMED_19227972}} | {{ABSTRACT_PUBMED_19227972}} | ||
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==See Also== | ==See Also== | ||
| - | *[[Superoxide Dismutase]] | + | *[[Superoxide Dismutase|Superoxide Dismutase]] |
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:019227972</ref><references group="xtra"/> |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Superoxide dismutase]] | [[Category: Superoxide dismutase]] | ||
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[[Category: Schuermann, J P.]] | [[Category: Schuermann, J P.]] | ||
[[Category: Winkler, D D.]] | [[Category: Winkler, D D.]] | ||
| - | [[Category: Acetylation]] | ||
[[Category: Amyotrophic lateral sclerosis]] | [[Category: Amyotrophic lateral sclerosis]] | ||
[[Category: Antioxidant]] | [[Category: Antioxidant]] | ||
| - | [[Category: Copper]] | ||
| - | [[Category: Cytoplasm]] | ||
[[Category: Disease mutation]] | [[Category: Disease mutation]] | ||
[[Category: Disulfide bond]] | [[Category: Disulfide bond]] | ||
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[[Category: Phosphoprotein]] | [[Category: Phosphoprotein]] | ||
[[Category: Superoxide acceptor]] | [[Category: Superoxide acceptor]] | ||
| - | [[Category: Ubl conjugation]] | ||
| - | [[Category: Zinc]] | ||
Revision as of 00:31, 27 July 2012
Contents |
Structural and Biophysical Properties of the Pathogenic SOD1 Variant H46R/H48Q
Template:ABSTRACT PUBMED 19227972
About this Structure
3gqf is a 6 chain structure of Superoxide Dismutase with sequence from Homo sapiens. Full crystallographic information is available from OCA.
See Also
Reference
- Winkler DD, Schuermann JP, Cao X, Holloway SP, Borchelt DR, Carroll MC, Proescher JB, Culotta VC, Hart PJ. Structural and biophysical properties of the pathogenic SOD1 variant H46R/H48Q. Biochemistry. 2009 Apr 21;48(15):3436-47. PMID:19227972 doi:10.1021/bi8021735
Categories: Homo sapiens | Superoxide dismutase | Hart, P J. | Schuermann, J P. | Winkler, D D. | Amyotrophic lateral sclerosis | Antioxidant | Disease mutation | Disulfide bond | Familial amyotrophic lateral sclerosis mutant | Human cu-zn superoxide dismutase | Metal-binding | Oxidoreductase | Phosphoprotein | Superoxide acceptor
