One fold with many functions: the evolutionary relationships between TIM barrel families based on their sequences, structures and functions.

By N. Nagano, Christine A. Orengo, Janet M. Thornton. 2002

625 citations recorded by the source corpus.

Subfields: Immunology, Materials Chemistry, Molecular Biology

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Immunology

M. Hayer-Hartl

In Materials Chemistry

In Molecular Biology

Citations in the corpus

ECOD: An Evolutionary Classification of Protein Domains (2014, background): “However, SCOP tends to be conservative in assessing evolutionary relationships, and many homologous links reported in literature are not currently reflected [6,7,8,9,10,11].”
COFACTOR: an accurate comparative algorithm for structure-based protein function annotation (2012, background): “The classic examples include the proteins with a-/b-barrel fold, which is inhabited by both enzymatic and non-enzymatic proteins (6).”
Chitin Metabolism in Insects (2012, background): “sexta CHI has a (~(X)8 triose phosphate isomerase (TIM) barrel structure (Kramer and Muthukrishnan, 1997; Nagano et al., 2002).”
SCOPmap: Automated assignment of protein structures to evolutionary superfamilies (2004, background): “The homology between these two superfamilies has been previously reported [36].”
Comprehensive structural classification of ligand-binding motifs in proteins. (2008, background): “Among them, the TIM barrel fold was an extreme case with 183 motifs assigned, reflecting the great diversity of its functions (Nagano et al., 2002).”
Discrimination between distant homologs and structural analogs: lessons from manually constructed, reliable data sets. (2008, background): “A significant fraction of the high-scoring pairs between superfamilies but within the same fold are the TIM β/α-barrels, and many of these links have been previously reported in the literature.(42,43) Additionally, different superfamilies in the following SCOP folds are found to be homologous by our”
COFACTOR: improved protein function prediction by combining structure, sequence and protein–protein interaction information (2017, background): “For example, the TIM barrel fold (6) is adopted by many proteins covering 60 distinct EC classification (7) as well as many non-enzyme proteins.”
Proteome-wide analysis of chaperonin-dependent protein folding in Escherichia coli. (2005, background): “Mechanisms for Substrate Selection by GroEL Since the TIM-barrel fold is widely distributed (Nagano et al., 2002), it cannot per se be the sole criterion for the GroEL/GroES dependence of a protein.”