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Nature Communications, ISSN 2041-1723, 2015, Volume 6, Issue 1, pp. 10156 - 10156
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 03/2017, Volume 114, Issue 10, pp. E2053 - E2062
Detection of pathogens by plants is mediated by intracellular nucleotide-binding site leucine-rich repeat (NLR) receptor proteins. NLR proteins are defined by... 
Oligomerization | Type III secretion | NLR | Toll-interleukin-1 receptor homology domain | Plant immunity | TRIGGERED IMMUNITY | PLANT | DOMAIN | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | type III secretion | SELF-ASSOCIATION | oligomerization | STRUCTURE VALIDATION | STRUCTURAL BASIS | THALIANA | plant immunity | DISEASE RESISTANCE | REVEALS | Plant Diseases - immunology | Cell Death - immunology | Arabidopsis - immunology | Crystallography, X-Ray | Plant Diseases - microbiology | Type III Secretion Systems - genetics | Pseudomonas syringae - pathogenicity | Tobacco - immunology | Cell Death - genetics | Plant Proteins - chemistry | Erwinia - pathogenicity | Gene Expression Regulation, Plant | Plant Diseases - genetics | Protein Interaction Domains and Motifs | Binding Sites | Pseudomonas syringae - physiology | Erwinia - physiology | Arabidopsis Proteins - genetics | Arabidopsis - chemistry | Plant Immunity - genetics | Protein Structure, Secondary | Signal Transduction | Models, Molecular | Recombinant Proteins - chemistry | Plant Proteins - immunology | Recombinant Proteins - genetics | Arabidopsis Proteins - immunology | Arabidopsis - genetics | Host-Pathogen Interactions | Type III Secretion Systems - metabolism | Arabidopsis - microbiology | Plant Proteins - genetics | Arabidopsis Proteins - chemistry | Recombinant Proteins - immunology | Tobacco - genetics | Protein Binding | Tobacco - microbiology | Mutation | Arabidopsis thaliana | Physiological aspects | Observations | Cell death | Binding sites (Biochemistry) | Proteins | Bacteria | Cytokines | Binding sites | Immune system | Biological Sciences | Toll–interleukin-1 receptor homology domain | PNAS Plus
Journal Article
The Journal of cell biology, ISSN 0021-9525, 09/2019, Volume 218, Issue 9, pp. 3077 - 3097
Rho family GTPases are activated with precise spatiotemporal control by guanine nucleotide exchange factors (GEFs). Guanine exchange factor H1 (GEF-H1), a RhoA... 
RHOA ACTIVITY | ADHESION | MOTION | GTPASES | INTEGRINS | RHOGEF | TIME-SERIES | MECHANISTIC INSIGHT | PROTEINS | SOFTWARE | CELL BIOLOGY | Exchanging | Neuroimaging | Phosphorylation | RhoA protein | Activation | Nucleotides | Guanine | Depolymerization | Cell activation | Actin | Dynamics | Guanine nucleotide exchange factor | Biosensors
Journal Article
Journal Article
2006, AD-a465 849.
Neurofibromatosis Type 1 (NF1) arises from the aberrant activation of Ras, a GTPases important controlling mitogenic potential. In an effort to control the... 
inhibitors | nf1(neurofibromatosis type 1) | ras | abnormalities | therapy | molecules | gtpase | peripheral nervous system | targets | mental disorders | order disorder transformations | guanine | neurofibromatosis type 1 | cancer | exchange | activation | neoplasms | nucleotides | neurology
Government Document