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Volumn 51, Issue 1, 2012, Pages 1-3
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Structural analysis of HopPmaL reveals the presence of a second adaptor domain common to the HopAB family of pseudomonas syringae type III effectors
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Author keywords
[No Author keywords available]
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Indexed keywords
C-TERMINAL DOMAINS;
HOST PROTEINS;
N-TERMINAL DOMAINS;
PHYTOPATHOGENS;
PSEUDOMONAS SYRINGAE;
SEQUENCE SIMILARITY;
X RAY CRYSTALLOGRAPHY;
BACTERIA;
PROTEIN;
PROTEIN HOPPMAL;
UNCLASSIFIED DRUG;
ARTICLE;
CARBOXY TERMINAL SEQUENCE;
NONHUMAN;
NUCLEAR MAGNETIC RESONANCE;
PRIORITY JOURNAL;
PROTEIN DOMAIN;
PROTEIN FAMILY;
PROTEIN STRUCTURE;
PSEUDOMONAS SYRINGAE;
STRUCTURE ANALYSIS;
X RAY CRYSTALLOGRAPHY;
BACTERIAL PROTEINS;
CONSERVED SEQUENCE;
CRYSTALLOGRAPHY, X-RAY;
HYDROPHOBIC AND HYDROPHILIC INTERACTIONS;
LYCOPERSICON ESCULENTUM;
MULTIGENE FAMILY;
PEPTIDE FRAGMENTS;
PLANT DISEASES;
PLANT PROTEINS;
PROTEIN BINDING;
PROTEIN FOLDING;
PROTEIN STRUCTURE, TERTIARY;
PROTEIN-SERINE-THREONINE KINASES;
PSEUDOMONAS SYRINGAE;
SEQUENCE ALIGNMENT;
PSEUDOMONAS SYRINGAE;
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EID: 84863014802
PISSN: 00062960
EISSN: 15204995
Source Type: Journal
DOI: 10.1021/bi2013883 Document Type: Article |
Times cited : (5)
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References (10)
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