Cell
Letter to the editorHuman genetic diseases due to codon reiteration: Relationship to an evolutionary mechanism
References (28)
- et al.
Cell
(1992) - et al.
Cell
(1986) - et al.
J. Biol. Chem.
(1992) - et al.
J. Biol. Chem.
(1993) - et al.
Cell
(1979) - et al.
Cell
(1985) - et al.
Cell
(1985) - et al.
Science
(1992) - et al.
- et al.
Mol. Biol. Evol.
(1993)
Science
Mol. Biol. Evol.
FASEB
Cited by (217)
Cofactors and coenzymes: Cysteamine
2021, Encyclopedia of Biological Chemistry: Third EditionIdentification of brain substrates of transglutaminase by functional proteomics supports its role in neurodegenerative diseases
2017, Neurobiology of DiseaseCitation Excerpt :The idea that the crosslinking activity of transglutaminase stabilizes protein aggregates in neurological disease rests on the notion that the isodipeptide bond is resistant to proteolysis and that the crosslinked aggregates would therefore accumulate. Dennis Selkoe proposed in 1982 that neurofibrillary tangles were crosslinked by transglutaminase in Alzheimer's disease brain (Selkoe et al., 1982a) and Howard Green hypothesized in 1993 that as a result of excessive polyQ length, huntingtin became a preferred substrate for neuronal transglutaminase (Green, 1993). Since then, a number of studies have lent support to these hypotheses (reviewed in (Hoffner et al., 2011; Iannaccone et al., 2014; Wilhelmus et al., 2014)).
An attractive route to transamidation catalysis: Facile synthesis of new o-aryloxide-N-heterocyclic carbene ruthenium(II) complexes containing trans triphenylphosphine donors
2015, Journal of Molecular Catalysis A: ChemicalTissue transglutaminase overexpression does not modify the disease phenotype of the R6/2 mouse model of Huntington's disease
2012, Experimental NeurologyCitation Excerpt :Thus, the etiology of HD likely involves a complex interplay between multiple mechanisms, and determining the contribution of specific factors to the pathogenesis of HD should provide rational targets for therapeutic intervention. Green suggested that an increase in the number of glutamine residues beyond a certain threshold may result in a protein becoming a transglutaminase (TG) substrate (Green, 1993). Indeed, one suggested contributor to the dysfunction and loss of neurons in HD is the type 2 TG (TG2, also called tissue transglutaminase, tTG), a multifunctional calcium dependent enzyme and member of the transglutaminase family (Iismaa et al., 2009; Lesort et al., 2000a; Lorand and Graham, 2003).