1,720,971 research outputs found
Comparative modelling of human galactose-1-phosphate uridylyltransferase and of its galactosemia-related mutant Q188R: A molecular explanation of the structural effects of the mutation
No full textStructural features of human galactose-1-phosphate uridylyltransferase and of its galactosemia-related mutant Q188R: an homology modelling study
No full textHomology modeling studies on human Galactose-1-phosphate uridylyltransferase and on its galactosemia-related mutant Q188R provide an explanation of molecular effects of the mutation on homo- and heterodimers
No full textTheoretical model of the three-dimensional structure of a sugar-binding protein from Pyrococcus horikoshii: structural analysis and sugar-binding simulations
No full textThe N-terminal 1-16 peptide derived in vivo from protein seminal vesicle protein IV modulates alpha-thrombin activity: potential clinical implications
No full textA thermostable Sugar-Binding Protein from the archaeon Pyrococcus horikoshii as a probe for the development of a stable fluorescence biosensor for diabetic patients
No full textApplicazione dei bio-processoria DNA allo studio su scala genomica delle modificazioni di espressione genica che caratterizzano il ciclo replicativo cellulare indotto da Estrogeni
No full textAlteration in the ubiquitin structure and function in the human lens: A possible mechanism of senile cataractogenesis
No full textHigh-performance liquid chromatography purification followed by mass spectrometry analyses highlighted that human senile cataractous lens includes a 8182 Da species which is absent in the normal lens, whereas a 8566/8583 Da species is present in both lenses. Western blot analysis identified both species as ubiquitin. The species at lower molecular weight is a shorter form due to the cleavage of the C-terminal residues 73-76. As it is the last amino acid of ubiquitin which is involved in the protein degradation mechanism, we suggest that this structure modification compromises the function of ubiquitin and consequently the physiologically occurring degradation of the lens proteins. © 2002 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.High-performance liquid chromatography purification followed by mass spectrometry analyses highlighted that human senile cataractous lens includes a 8182 Da species which is absent in the normal lens, whereas a 8566/8583 Da species is present in both lenses. Western blot analysis identified both species as ubiquitin. The species at lower molecular weight is a shorter form due to the cleavage of the C-terminal residues 73-76. As it is the last amino acid of ubiquitin which is involved in the protein degradation mechanism, we suggest that this structure modification compromises the function of ubiquitin and consequently the physiologically occurring degradation of the lens proteins. © 2002 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved
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