The kelch repeat superfamily of proteins: propellers of cell function.

By J. Adams, Reed J. Kelso, L. Cooley. Trends in Cell Biology, 2000

605 citations recorded by the source corpus.

Subfields: Molecular Biology, Plant Science

View Paper: https://www.semanticscholar.org/paper/ca986c5995363a28650df5cb056bc8fcf22929b1

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Citations in the corpus

High sensitivity of Nrf2 knockout mice to acetaminophen hepatotoxicity associated with decreased expression of ARE-regulated drug metabolizing enzymes and antioxidant genes. (2001, background): “Keap1, a homologue of the Drosophila actin binding protein Kelch, binds to the N-terminal Neh2 domain of Nrf2, thereby retaining this transcription factor in the cytoplasm (Adams et al., 2000; Itoh et al., 1999; Xue and Cooley, 1993).”
Loss of Keap1 function activates Nrf2 and provides advantages for lung cancer cell growth. (2008, background): “Keap1 is a newly identified Nrf2associated protein (5), containing BTB, IVR, and DGR domains ( 6 ).”
Keap1 Recruits Neh2 through Binding to ETGE and DLG Motifs: Characterization of the Two-Site Molecular Recognition Model (2006, background): “ing region), DGR (double glycine repeat or Kelch repeat) (1, 60),”
The Impact of Oxidative Stress and Inflammation on RPE Degeneration in Non-neovascular AMD (2017, background): “…functions as a substrate adaptor protein for a Cul3-dependent E3 ubiquitin ligase complex, which also helps to maintain steady-state levels of Nrf2 via proteolysis of Nrf2 by the ubiquitin-proteasome pathway (Adams et al., 2000; Kobayashi et al., 2004; Yu and Kensler, 2005; Zhang et al., 2004).”
Control of flowering time: interacting pathways as a basis for diversity. (2002, background): “The -propellers are believed to be implicated in protein–protein interactions (Adams et al., 2000).”
Distinct Cysteine Residues in Keap1 Are Required for Keap1-Dependent Ubiquitination of Nrf2 and for Stabilization of Nrf2 by Chemopreventive Agents and Oxidative Stress (2003, background): “Keap1 is a member of a large family of proteins that contain an N-terminal Broad complex, Tramtrack, and Bric a brac (BTB) domain and a Cterminal Kelch repeat domain (1).”
The Gα Protein Gpa2 Controls Yeast Differentiation by Interacting with Kelch Repeat Proteins that Mimic Gβ Subunits (2002, neutral): “As shown in tein interactions (Adams et al., 2000).”
F-Box Proteins in Rice. Genome-Wide Analysis, Classification, Temporal and Spatial Gene Expression during Panicle and Seed Development, and Regulation by Light and Abiotic Stress1[W][OA] (2007, background): “Although kelch and WD40 repeats have similar tertiary structure like a b-propeller (Smith et al., 1999; Adams et al., 2000), they have no sequence similarity.”
Keap1-null mutation leads to postnatal lethality due to constitutive Nrf2 activation (2003, background): “Keap1 is composed of two distinguishable motifs: the Kelch (or double glycine repeat) domai”
Sequence and structural analysis of BTB domain proteins (2005, background): “These BBK proteins are composed of a long-form BTB domain, the 130 residue BACK domain [79], and a carboxy-terminal region containing four to seven kelch motifs [80-82].”