LRDD, a novel leucine rich repeat and death domain containing protein (Q22254132)

GOA release 2020-03-11

death receptor binding

1 reference

GOA release 2020-03-11

J B Telliez

J B

Telliez

1 reference

PubMed

30 March 2023

K M Bean

series ordinal

author given names

K M

author last names

Bean

1 reference

PubMed

30 March 2023

L L Lin

series ordinal

author given names

L L

author last names

Lin

1 reference

PubMed

Biochimica et Biophysica Acta

30 March 2023

language of work or name

English

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publication date

23 May 2000

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published in

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volume

1478

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issue

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page(s)

280-8

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Self-association of the Death Domains of the p55 Tumor Necrosis Factor (TNF) Receptor and Fas/APO1 Prompts Signaling for TNF and Fas/APO1 Effects

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FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis

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The TNF receptor 1-associated protein TRADD signals cell death and NF-kappa B activation

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RIP: a novel protein containing a death domain that interacts with Fas/APO-1 (CD95) in yeast and causes cell death

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NMR structure and mutagenesis of the Fas (APO-1/CD95) death domain

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The solution structure of FADD death domain. Structural basis of death domain interactions of Fas and FADD

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NMR structure of the death domain of the p75 neurotrophin receptor

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The CARD domain: a new apoptotic signalling motif

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Detecting homology of distantly related proteins with consensus sequences.

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Structural and functional diversity in the leucine-rich repeat family of proteins

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The tomato Cf-2 disease resistance locus comprises two functional genes encoding leucine-rich repeat proteins

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The myosin-I-binding protein Acan125 binds the SH3 domain and belongs to the superfamily of leucine-rich repeat proteins

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The Drosophila melanogaster flightless-I gene involved in gastrulation and muscle degeneration encodes gelsolin-like and leucine-rich repeat domains and is conserved in Caenorhabditis elegans and humans

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Crystal structure of porcine ribonuclease inhibitor, a protein with leucine-rich repeats

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Vertebrate homologues of C. elegans UNC-5 are candidate netrin receptors

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Identifiers

DOI

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