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Zoology and wildlife conservation

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Abstracts » Zoology and wildlife conservation

Human lysozyme gene mutations cause hereditary systemic amyloidosis

Article Abstract:

A study of hereditary non-neuropathic systemic amyloidosis is presented. This rare autosomal dominant disease is characterized by amyloid deposition in the viscera which is usually fatal by the fifth decade of life. In some families it is due to mutations in the apolipoprotein AI gene. However, genetic studies in two English families showed that amyloidosis was caused by substitutions in two different, highly conserved sites of the lysozyme gene. This is the first report of naturally-occurring variants of human lysozyme and of lysozema-associated disease, and could be an important tool for understanding amyloidogenesis.

Author: Tennent, G.A., Pepys, M.B., Hawkins, P.N., Booth, D.R., Vigushin, D.M., Soutar, A.K., Totty, N., Nguyen, O., Blake, C.C.F., Terry, C.J., Feest, T.G., Zalin, A.M., Hsuan, J.J.
Publisher: Macmillan Publishing Ltd.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1993
Amyloidosis, Protein metabolism disorders

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In search of molecular darwinism

Article Abstract:

A study conducted by Walter Messier and Caro-Beth Stewart seeks to trace molecular evolution by examining the enzyme lysozyme in colobine monkeys. Leaf-eating colobine monkeys, particularly the hanuman langur, has a foregut with lysozyme functioning in the same way as those in ruminants. Lysozyme has amino-acid changes similarly found in cows. The researchers claim to have identified the proposed adaptive changes to a brief period during the early years of the colobine monkeys' ancestors.

Author: Sharp, Paul M.
Publisher: Macmillan Publishing Ltd.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1997
Monkeys, Chemical evolution, Molecular evolution

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Redox-mediated substrate recognition by Sdp1 defines a new group of tyrosine phosphatases

Article Abstract:

Structural and biochemical evidence has shown that the stress-inducible mitogen-activated protein kinase (MAPK) phosphatase (Sdp1) has used an intramolecular disulphide bridge and an invariant histidine side chain to selectively recognize a tyrosine-phosphorylated MAPK substrate. The analysis has shown that Sdp1 and its paralogue Msg5 have similar properties and belong to a new group of phosphatases unique to yeast and fungal taxa.

Author: Briggs, D.C., Totty, N., Fox, G.C., Shafiq, M., Knowles, P.P., Collister, M., Didmon, M.J., Makrantoni, V., Dickinson, R.J., Hanrahan, S., Stark, M.J.R., Keyse, S.M., McDonald, N.Q.
Publisher: Macmillan Publishing Ltd.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2007
Science & research, Physiological aspects, Protein kinases, Oxidation-reduction reaction, Oxidation-reduction reactions, Tyrosine metabolism, Chemical properties

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Subjects list: Genetic aspects, Lysozyme, Research
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