Probing the interaction between p53 and the bacterial protein azurin by single molecule force spectroscopy.
about
Single-molecule dynamics and mechanisms of metalloregulators and metallochaperonesStructural characteristics of the hydrophobic patch of azurin and its interaction with p53: a site-directed spin labeling study.A novel and rapid LC/MS/MS assay for bioanalysis of Azurin p28 in serum and its pharmacokinetics in miceVariation in the mechanical unfolding pathway of p53DBD induced by interaction with p53 N-terminal region or DNA.p28, a first in class peptide inhibitor of cop1 binding to p53.Microbial-based therapy of cancer: current progress and future prospects.Engineering of bacterial strains and their products for cancer therapy.SERS-based nanobiosensing for ultrasensitive detection of the p53 tumor suppressor.A nanotechnological, molecular-modeling, and immunological approach to study the interaction of the anti-tumorigenic peptide p28 with the p53 family of proteinsA cell penetrating peptide derived from azurin inhibits angiogenesis and tumor growth by inhibiting phosphorylation of VEGFR-2, FAK and Akt.Interaction of an anticancer peptide fragment of azurin with p53 and its isolated domains studied by atomic force spectroscopy.MDM2-MDM4 molecular interaction investigated by atomic force spectroscopy and surface plasmon resonance.Discovery of Azurin-Like Anticancer Bacteriocins from Human Gut Microbiome through Homology Modeling and Molecular Docking against the Tumor Suppressor p53Unbinding forces of single pertussis toxin-antibody complexes measured by atomic force spectroscopy correlate with their dissociation rates determined by surface plasmon resonance.Free energy evaluation of the p53-Mdm2 complex from unbinding work measured by dynamic force spectroscopy.Single and multiple bonds in (strept)avidin-biotin interactions.Binding of azurin to cytochrome c 551 as investigated by surface plasmon resonance and fluorescence.Bacterial cupredoxin azurin hijacks cellular signaling networks: Protein-protein interactions and cancer therapy.Surface Plasmon Resonance Sensing of Biorecognition Interactions within the Tumor Suppressor p53 Network.Imaging and kinetics of the bimolecular complex formed by the tumor suppressor p53 with ubiquitin ligase COP1 as studied by atomic force microscopy and surface plasmon resonance.Mechanisms of angiogenesis in microbe-regulated inflammatory and neoplastic conditions.
P2860
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P2860
Probing the interaction between p53 and the bacterial protein azurin by single molecule force spectroscopy.
description
2008 nî lūn-bûn
@nan
2008 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
Probing the interaction betwee ...... e molecule force spectroscopy.
@ast
Probing the interaction betwee ...... e molecule force spectroscopy.
@en
Probing the interaction betwee ...... e molecule force spectroscopy.
@nl
type
label
Probing the interaction betwee ...... e molecule force spectroscopy.
@ast
Probing the interaction betwee ...... e molecule force spectroscopy.
@en
Probing the interaction betwee ...... e molecule force spectroscopy.
@nl
prefLabel
Probing the interaction betwee ...... e molecule force spectroscopy.
@ast
Probing the interaction betwee ...... e molecule force spectroscopy.
@en
Probing the interaction betwee ...... e molecule force spectroscopy.
@nl
P356
P1476
Probing the interaction betwee ...... e molecule force spectroscopy.
@en
P2093
Anna Rita Bizzarri
Monia Taranta
P356
10.1002/JMR.869
P577
2008-01-01T00:00:00Z