Annotation inferences using phylogenetic trees

Combined Automated Annotation using Multiple IEA Methods

A mosaic analysis in Drosophila fat body cells of the control of antimicrobial peptide genes by the Rel proteins Dorsal and DIF.

Toll-related receptors and the control of antimicrobial peptide expression in Drosophila.

Cutting edge: the toll pathway is required for resistance to gram-positive bacterial infections in Drosophila.

Regulation of Easter activity is required for shaping the Dorsal gradient in the Drosophila embryo.

Binding of the Drosophila cytokine Spätzle to Toll is direct and establishes signaling.

Toll gets tied in a knot.

A serpin regulates dorsal-ventral axis formation in the Drosophila embryo.

Multimerization and interaction of Toll and Spätzle in Drosophila.

A Spätzle-processing enzyme required for toll signaling activation in Drosophila innate immunity.

The Drosophila inhibitor of apoptosis protein DIAP2 functions in innate immunity and is essential to resist gram-negative bacterial infection.

RalB GTPase-mediated activation of the IkappaB family kinase TBK1 couples innate immune signaling to tumor cell survival.

Dual detection of fungal infections in Drosophila via recognition of glucans and sensing of virulence factors.

Role of the Spatzle Pro-domain in the generation of an active toll receptor ligand.

Structural insight into the mechanism of activation of the Toll receptor by the dimeric ligand Spätzle.

Sensing of 'danger signals' and pathogen-associated molecular patterns defines binary signaling pathways 'upstream' of Toll.

Biophysical characterization of refolded Drosophila Spätzle, a cystine knot protein, reveals distinct properties of three isoforms.

Drosophila neurotrophins reveal a common mechanism for nervous system formation.

Toll-dependent antimicrobial responses in Drosophila larval fat body require Spätzle secreted by haemocytes.

Cytokine Spatzle binds to the Drosophila immunoreceptor Toll with a neurotrophin-like specificity and couples receptor activation.

Persephone/Spätzle pathogen sensors mediate the activation of Toll receptor signaling in response to endogenous danger signals in apoptosis-deficient Drosophila.

Transformed epithelia trigger non-tissue-autonomous tumor suppressor response by adipocytes via activation of Toll and Eiger/TNF signaling.

Structure of the Toll-Spatzle complex, a molecular hub in Drosophila development and innate immunity.

Dynamic regulation of innate immune responses in Drosophila by Senju-mediated glycosylation.

Spätzle-Processing Enzyme-independent Activation of the Toll Pathway in Drosophila Innate Immunity.

Toll pathway is required for wound-induced expression of barrier repair genes in the Drosophila epidermis.

Spatially Restricted Regulation of Spätzle/Toll Signaling during Cell Competition.

Toll family members bind multiple Spätzle proteins and activate antimicrobial peptide gene expression in Drosophila.

The Drosophila Baramicin polypeptide gene protects against fungal infection.

Damage sensing mediated by serine proteases Hayan and Persephone for Toll pathway activation in apoptosis-deficient flies.

Cactus protein degradation mediates Drosophila dorsal-ventral signaling.

A processed form of the Spätzle protein defines dorsal-ventral polarity in the Drosophila embryo.

The spätzle gene encodes a component of the extracellular signaling pathway establishing the dorsal-ventral pattern of the Drosophila embryo.

The dorsoventral regulatory gene cassette spätzle/Toll/cactus controls the potent antifungal response in Drosophila adults.

Proteolytic processing of the Drosophila Spätzle protein by easter generates a dimeric NGF-like molecule with ventralising activity.

The Toll pathway is required in the epidermis for muscle development in the Drosophila embryo.

Activated PLL kinase is autophosphorylated in TL:MYD88:TUB:PLL 'signalling complex'

PLL kinase binds to TL:MYD88:TUB 'signalling complex'

SPZ dimer bound TL dimerises at the plasma membrane

MYD88:TUB binds to TL receptor

Full-length SPZ dimer is cleaved by EA/SPE serine protease

ProSPZ:SPZ dimer binds to TL receptor at the plasma membrane

CACT and DL dimer are phosphorylated in TL:WEK:MYD88:TUB:PLL 'signalling complex'

Phosphorylated CACT and DL dimer dissociate from the TL:WEK:MYD88:TUB:PLL 'signalling complex'

WEK and MYD88:TUB bind to the TL receptor

DL/DIF dimer binds to TUB and phosphorylated PLL in TL:MYD88:TUB:PLL 'signalling complex'

Activated PLL kinase is autophosphorylated in TL:WEK:MYD88:TUB:PLL 'signalling complex'

CACT and DL/DIF dimer are phosphorylated in TL:MYD88:TUB:PLL 'signalling complex'

Phosphorylated CACT and DL/DIF dimer dissociate from the TL:MYD88:TUB:PLL 'signalling complex'

PLL kinase binds to TL:WEK:MYD88:TUB 'signalling complex'

DL dimer binds to TUB and phosphorylated PLL in TL:WEK:MYD88:TUB:PLL 'signalling complex'