Web of Science: 4 cites, Scopus: 5 cites, Google Scholar: cites,
Protein aggregation profile of the human kinome
Graña Montes, Ricardo (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
Sant'Anna de Oliveira, Ricardo (Universidade Federal do Rio de Janeiro. Instituto de Bioquímica Médica)
Ventura, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)

Data: 2012
Resum: Protein aggregation into amyloid fibrils is associated with the onset of an increasing number of human disorders, including Alzheimer's disease, diabetes, and some types of cancer. The ability to form toxic amyloids appears to be a property of most polypeptides. Accordingly, it has been proposed that reducing aggregation and its effect in cell fitness is a driving force in the evolution of proteins sequences. This control of protein solubility should be especially important for regulatory hubs in biological networks, like protein kinases. These enzymes are implicated in practically all processes in normal and abnormal cell physiology, and phosphorylation is one of the most frequent protein modifications used to control protein activity. Here, we use the AGGRESCAN algorithm to study the aggregation propensity of kinase sequences. We compared them with the rest of globular proteins to decipher whether they display differential aggregation properties. In addition, we compared the human kinase complement with the kinomes of other organisms to see if we can identify any evolutionary trend in the aggregational properties of this protein superfamily. Our analysis indicates that kinase domains display significant aggregation propensity, a property that decreases with increasing organism complexity.
Ajuts: Ministerio de Ciencia e Innovación BFU2010-14901
Ministerio de Ciencia e Innovación FPU AP 2009-0948
Nota: This work was supported by 2009-SGR from AGAUR (Generalitat de Catalunya). Salvador Ventura has been granted an ICREA ACADEMIA award.
Drets: Aquest document està subjecte a una llicència d'ús Creative Commons. Es permet la reproducció total o parcial, la distribució, la comunicació pública de l'obra i la creació d'obres derivades, fins i tot amb finalitats comercials, sempre i quan es reconegui l'autoria de l'obra original. Creative Commons
Llengua: Anglès
Document: Article ; recerca ; Versió publicada
Matèria: Protein kinases ; Protein aggregation ; Amyloid ; Protein evolution ; AGGRESCAN
Publicat a: Frontiers in physiology, Vol. 3 (2012) , ISSN 1664-042X

DOI: 10.3389/fphys.2012.00438
PMID: 23181023


10 p, 4.3 MB

El registre apareix a les col·leccions:
Documents de recerca > Documents dels grups de recerca de la UAB > Centres i grups de recerca (producció científica) > Ciències de la salut i biociències > Institut de Biotecnologia i de Biomedicina (IBB)
Articles > Articles de recerca
Articles > Articles publicats

 Registre creat el 2018-01-26, darrera modificació el 2021-09-25



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