Exploring Non-obvious Hydrophobic Binding Pockets on Protein Surfaces: Increasing Affinities in Peptide-Protein Interactions-Reference-Cited by-同舟云学术

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Exploring Non-obvious Hydrophobic Binding Pockets on Protein Surfaces: Increasing Affinities in Peptide-Protein Interactions

Published:2017-06-07 Issue:14 Volume:18 Page:1396-1407
ISSN:1439-4227
Container-title:ChemBioChem
language:en
Short-container-title:ChemBioChem

Author:

Balliu Aleksandra¹,Baltzer Lars¹^ORCID

Affiliation:

1. Department of Chemistry; BMC; Uppsala University; P. O. Box 576 751 23 Uppsala Sweden

Funder

Vetenskapsrådet

Publisher

Wiley

Subject

Organic Chemistry,Molecular Biology,Molecular Medicine,Biochemistry

Reference45 articles.

1. Motif mediated protein-protein interactions as drug targets

2. Small molecules, big targets: drug discovery faces the protein–protein interaction challenge

3. Challenges and Hurdles to Business as Usual in Drug Development for Treatment of Rare Diseases

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1. Probing the functional hotspots inside protein hydrophobic pockets by in situ photochemical trifluoromethylation and mass spectrometry;Chemical Science;2024

2. Effect of Supporter on the Activity and Stability of Immobilized Cellulase to Hydrolyze Cellulose;Catalysis Letters;2023-10-07

3. Towards rational computational peptide design;Frontiers in Bioinformatics;2022-10-21

4. Predicting Binding Affinity Between MHC-I Receptor and Peptides Based on Molecular Docking and Protein-peptide Interaction Interface Characteristics;Letters in Drug Design & Discovery;2022-08-19

5. Conjugation of a Dipicolyl Chelate to Polypeptide Conjugates Increases Binding Affinities for Human Serum Albumin and Survival Times in Human Serum;ChemBioChem;2017-05-05

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