Using peptides to study the interaction between the p53 tetramerization domain and HIV-1 tat-Reference-Cited by-同舟云学术

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Using peptides to study the interaction between the p53 tetramerization domain and HIV-1 tat

Published:2008 Issue:2 Volume:90 Page:105-116
ISSN:0006-3525
Container-title:Biopolymers
language:en
Short-container-title:Biopolymers

Author:

Gabizon Ronen,Mor Michal,Rosenberg Masha M.,Britan Lena,Hayouka Zvi,Kotler Moshe,Shalev Deborah E.,Friedler Assaf

Publisher

Wiley

Subject

Organic Chemistry,Biomaterials,Biochemistry,General Medicine,Biophysics

Reference45 articles.

1. Binding of Rad51 and Other Peptide Sequences to a Promiscuous, Highly Electrostatic Binding Site in p53

2. Molecular Mechanism of the Interaction between MDM2 and p53

3. Nine hydrophobic side chains are key determinants of the thermodynamic stability and oligomerization status of tumour suppressor p53 tetramerization domain

4. Peptide Mapping of a Novel Discontinuous Epitope of the Major Surface Adhesin from Streptococcus mutans

5. Tat gets the "green" light on transcription initiation

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1. Theoretical Investigation of Interactions between HIV-1 Tat and p53 proteins;2024-07-11

2. The Oligomerization Domains of the APC Protein Mediate Liquid-Liquid Phase Separation That Is Phosphorylation Controlled;International Journal of Molecular Sciences;2023-03-30

3. Using a Single Peptide to Electrochemically Sense Multiple Kinases;Biochemistry;2022-10-14

4. Peptide‐Based Inhibitors that Target the Docking Site of ERK2;Israel Journal of Chemistry;2022-10

5. Electrochemical biosensors based on peptide-kinase interactions at the kinase docking site;Biosensors and Bioelectronics;2022-07

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