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Wyświetlanie 1-2 z 2
Tytuł:
A Few Examples and Counterexamples in Spectral Graph Theory
Autorzy:
Stevanović, Dragan
Milosavljević, Nikola
Vukičević, Damir
Powiązania:
https://bibliotekanauki.pl/articles/31563587.pdf
Data publikacji:
2020-05-01
Wydawca:
Uniwersytet Zielonogórski. Wydział Matematyki, Informatyki i Ekonometrii
Tematy:
communicability distance
spectral radius
integral graph
second Zagreb index
Wiener index
estrada index
almost cospectral graphs
NEPS of graphs
Opis:
We present a small collection of examples and counterexamples for selected problems, mostly in spectral graph theory, that have occupied our minds over a number of years without being completely resolved.
Źródło:
Discussiones Mathematicae Graph Theory; 2020, 40, 2; 637-662
2083-5892
Pojawia się w:
Discussiones Mathematicae Graph Theory
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Identification of proteins associated with amyloidosis by polarity index method
Autorzy:
Polanco, Carlos
Samaniego, José
Uversky, Vladimir
Castañón-González, Jorge
Buhse, Thomas
Leopold-Sordo, Marili
Madero-Arteaga, Alejandro
Morales-Reyes, Alicia
Tavera-Sierra, Lourdes
González-Bernal, Jesus
Arias-Estrada, Miguel
Powiązania:
https://bibliotekanauki.pl/articles/1039130.pdf
Data publikacji:
2015
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
Polarity index method
natively unfolded proteins
intrinsically disordered proteins
natively folded proteins
neurons
amyloidosis
amyloid
amyloidogenic protein
Opis:
There is a natural protein form, insoluble and resistant to proteolysis, adopted by many proteins independently of their amino acid sequences via specific misfolding-aggregation process. This dynamic process occurs in parallel with or as an alternative to physiologic folding, generating toxic protein aggregates that are deposited and accumulated in various organs and tissues. These proteinaceous deposits typically represent bundles of β-sheet-enriched fibrillar species known as the amyloid fibrils that are responsible for serious pathological conditions, including but not limited to neurodegenerative diseases, grouped under the term amyloidoses. The proteins that might adopt this fibrillar conformation are some globular proteins and natively unfolded (or intrinsically disordered) proteins. Our work shows that intrinsically disordered and intrinsically ordered proteins can be reliably identified, discriminated, and differentiated by analyzing their polarity profiles generated using a computational tool known as the polarity index method (Polanco & Samaniego, 2009; Polanco et al., 2012; 2013; 2013a; 2014; 2014a; 2014b; 2014c; 2014d). We also show that proteins expressed in neurons can be differentiated from proteins in these two groups based on their polarity profiles, and also that this computational tool can be used to identify proteins associated with amyloidoses. The efficiency of the proposed method is high (i.e. 70%) as evidenced by the analysis of peptides and proteins in the APD2 database (2012), AVPpred database (2013), and CPPsite database (2013), the set of selective antibacterial peptides from del Rio et al. (2001), the sets of natively unfolded and natively folded proteins from Oldfield et al. (2005), the set of human revised proteins expressed in neurons, and non-human revised proteins expressed in neurons, from the Uniprot database (2014), and also the set of amyloidogenic proteins from the AmyPDB database (2014).
Źródło:
Acta Biochimica Polonica; 2015, 62, 1; 41-55
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
    Wyświetlanie 1-2 z 2

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