Article
Diverse recognition of non-PxxP peptide ligands by the SH3 domains from p67(phox), Grb2 and Pex13p.
Department of Structural Biology, Biomolecular Engineering Research Institute, 6-2-3 Furuedai, Suita, Osaka 565-0874, Japan.
The EMBO Journal (impact factor:
9.2).
09/2002;
21(16):4268-76.
pp.4268-76
Source: PubMed
-
Article: Perspective: human contact patterns and the spread of airborne infectious diseases.
[show abstract] [hide abstract]
ABSTRACT: Networks of social contacts channel the transmission of airborne infections. Emerging insights from fields of science as diverse as mathematics, population biology and the social sciences are beginning to reveal how the contact pattern of the hosts determines the spread and evolution of airborne infectious agents.Trends in Microbiology 10/1999; 7(9):372-7. · 7.91 Impact Factor
Data provided are for informational purposes only. Although carefully collected, accuracy cannot be guaranteed.
The impact factor represents a rough estimation of the journal's impact factor and does not reflect the actual
current impact factor.
Publisher conditions are provided by RoMEO. Differing provisions from the publisher's actual policy or licence
agreement may be applicable.
Keywords
22 residue peptide
basic function
binding
binding site
C-terminal SH3 domain
compact helix-turn-helix structure
conventional PxxP-binding site
different surface regions
N-terminus
NMR cross-saturation method
non-PxxP peptide
non-PxxP peptide segment interacted
non-PxxP peptides
PDB entry 1K4U
Src homology 3