The NBS-LRR architectures of plant R-proteins and metazoan NLRs evolved in independent events

Proceedings of the National Academy of Sciences of the United States of America

Volumn 114, Issue 5, 2017, Pages 1063-1068

  Urbach, Jonathan M ^a   Ausubel, Frederick M ^a,b  

^a MASSACHUSETTS GENERAL HOSPITAL   (United States)

^b HARVARD MEDICAL SCHOOL   (United States)

Author keywords

Evolution; Innate immunity; NLR; NOD like receptors; R protein

Indexed keywords

NUCLEOTIDE BINDING OLIGOMERIZATION DOMAIN LIKE RECEPTOR; NUCLEOTIDE BINDING SITE LEUCINE RICH REPEAT RESISTANCE PROTEIN; PLANT PROTEIN; R PROTEIN; UNCLASSIFIED DRUG; LEUCINE-RICH REPEAT PROTEINS; NUCLEOSIDE TRIPHOSPHATASE; PROTEIN;

ARTICLE; CONTROLLED STUDY; GENE; GENE TRANSFER; LAST COMMON ANCESTOR; MOLECULAR PHYLOGENY; MONOPHYLY; NONHUMAN; PHYLOGENETIC TREE; PRIORITY JOURNAL; PROTEIN DOMAIN; AMINO ACID REPEAT; ANIMAL; BIOLOGICAL MODEL; CHEMISTRY; DISEASE RESISTANCE; EVOLUTION; GENETICS; INNATE IMMUNITY; MOLECULAR EVOLUTION; MULTIGENE FAMILY; PHYLOGENY; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY; SPECIES DIFFERENCE; STATISTICAL MODEL; STRUCTURE ACTIVITY RELATION; TETRATRICOPEPTIDE REPEAT;

ANIMALS; BIOLOGICAL EVOLUTION; DISEASE RESISTANCE; EVOLUTION, MOLECULAR; IMMUNITY, INNATE; LIKELIHOOD FUNCTIONS; MODELS, GENETIC; MULTIGENE FAMILY; NLR PROTEINS; NUCLEOSIDE-TRIPHOSPHATASE; PHYLOGENY; PLANT PROTEINS; PROTEIN DOMAINS; PROTEINS; REPETITIVE SEQUENCES, AMINO ACID; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; SPECIES SPECIFICITY; STRUCTURE-ACTIVITY RELATIONSHIP; TETRATRICOPEPTIDE REPEAT;

EID: 85010976399     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1619730114     Document Type: Article

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