Abstract
Many biological functions involve the formation of protein–protein complexes, and the inhibition of this process has garnered significant interest in pharmaceutical research investigating novel therapies for several human diseases. From an evolutionary perspective, proteins have evolved to optimize and differentiate their functions, a process that is mediated by the modulation of the interacting surfaces.
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Abbreviations
- Aβ:
-
β-amyloid
- AβPP:
-
β-amyloid protein precursor
- Aib:
-
α-aminoisobutyric acid
- BIR:
-
Baculoviral inhibitory repeat
- c-kit:
-
Tyrosine kinase receptor
- dTMP:
-
2′-deoxythymidine-5′-monophosphate
- dUMP:
-
2′-deoxyuridine-5′-monophosphate
- FRET:
-
Förster resonance energy transfer
- GAPs:
-
GTPase-activating proteins
- GEFs:
-
Guanine nucleotide exchange factors
- HDM2:
-
Human double minute 2
- HeLa:
-
Human cervical carcinoma cancer cell line
- HTS:
-
High-throughput screening
- hTS:
-
Human thymidylate synthase
- IAPs:
-
Inhibitors of apoptosis proteins
- MAP:
-
Mitogen-activated protein
- MDM2:
-
Mouse double minute 2
- NCI:
-
National Cancer Institute
- NSAIDs:
-
Non-steroidal anti-inflammatory drugs
- O-PHDEs:
-
Oxy-polyhalogenated diphenyl ethers
- PAC:
-
Proteasome assembling chaperone
- PBD:
-
Polo-box domain
- PDPA:
-
1,3-propanediphosphonic acid
- PI3K:
-
Phosphoinositol-3′-kinase
- PPIs:
-
Protein–protein interactions
- PS:
-
Presenilin
- SCF:
-
Stem cell factor
- Tcf4:
-
T-cell factor 4
- XIAP:
-
X-linked Inhibitor of apoptosis protein
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Ferrari, S., Pellati, F., Costi, M.P. (2013). Protein–Protein Interaction Inhibitors: Case Studies on Small Molecules and Natural Compounds. In: Mangani, S. (eds) Disruption of Protein-Protein Interfaces. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-37999-4_2
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