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Items: 4

1.
Circular permutation of betaB2-crystallin changes the hierarchy of domain assembly.
G. Wright, A. K. Basak, K. Wieligmann, E. M. Mayr, C. Slingsby
Protein Sci. 1998 Jun; 7(6): 1280–1285. doi: 10.1002/pro.5560070602
PMCID:
PMC2144035
SummaryPDF–7.7M
2.
A unique form of autosomal dominant cataract explained by gene conversion between β-crystallin B2 and its pseudogene
Vanita, V. Sarhadi, A. Reis, M. Jung, D. Singh, K. Sperling, J. R. Singh, J. Burger
J Med Genet. 2001 Jun; 38(6): 392–396. doi: 10.1136/jmg.38.6.392
PMCID:
PMC1734905
SummaryPDF–235K
3.
Protein–protein interactions among human lens acidic and basic β-crystallins
Bing-Fen Liu, Jack J.-N. Liang
FEBS Lett. Author manuscript; available in PMC 2007 Oct 31.
Published in final edited form as: FEBS Lett. 2007 Aug 21; 581(21): 3936–3942. Published online 2007 Jul 23. doi: 10.1016/j.febslet.2007.07.022
PMCID:
PMC2045703
AbstractArticlePDF–462K
4.
Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium
Pascale Gaudet, Michael S. Livstone, Suzanna E. Lewis, Paul D. Thomas
Brief Bioinform. 2011 Sep; 12(5): 449–462. Published online 2011 Aug 27. doi: 10.1093/bib/bbr042
PMCID:
PMC3178059
AbstractArticlePDF–1.0M

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