A combined atomic force microscopy imaging and docking study to investigate the complex between p53 DNA binding domain and Azurin.
about
p28, a first in class peptide inhibitor of cop1 binding to p53.A nanotechnological, molecular-modeling, and immunological approach to study the interaction of the anti-tumorigenic peptide p28 with the p53 family of proteinsInteraction of an anticancer peptide fragment of azurin with p53 and its isolated domains studied by atomic force spectroscopy.Surface Plasmon Resonance Sensing of Biorecognition Interactions within the Tumor Suppressor p53 Network.Structural Characterization of the Intrinsically Disordered Protein p53 Using Raman Spectroscopy.
P2860
A combined atomic force microscopy imaging and docking study to investigate the complex between p53 DNA binding domain and Azurin.
description
2009 nî lūn-bûn
@nan
2009年の論文
@ja
2009年学术文章
@wuu
2009年学术文章
@zh
2009年学术文章
@zh-cn
2009年学术文章
@zh-hans
2009年学术文章
@zh-my
2009年学术文章
@zh-sg
2009年學術文章
@yue
2009年學術文章
@zh-hant
name
A combined atomic force micros ...... DNA binding domain and Azurin.
@en
A combined atomic force micros ...... DNA binding domain and Azurin.
@nl
type
label
A combined atomic force micros ...... DNA binding domain and Azurin.
@en
A combined atomic force micros ...... DNA binding domain and Azurin.
@nl
prefLabel
A combined atomic force micros ...... DNA binding domain and Azurin.
@en
A combined atomic force micros ...... DNA binding domain and Azurin.
@nl
P356
P1476
A combined atomic force micros ...... DNA binding domain and Azurin
@en
P2093
Anna Rita Bizzarri
Laura Andolfi
P304
P356
10.1002/JMR.975
P577
2009-11-01T00:00:00Z