Protein–protein interactions and cancer: small molecules going in for the kill
There has been much progress in the discovery of small, organic molecules that inhibit protein–protein interactions, particularly in the field of cancer. Tubulin polymerization represents a classic target whose function can be allosterically modulated by small molecules. Several protein–protein comp...
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| Published in | Current opinion in chemical biology Vol. 9; no. 3; pp. 317 - 324 |
|---|---|
| Main Author | |
| Format | Journal Article |
| Language | English |
| Published |
England
Elsevier Ltd
01.06.2005
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| Subjects | |
| Online Access | Get full text |
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| Abstract | There has been much progress in the discovery of small, organic molecules that inhibit protein–protein interactions, particularly in the field of cancer. Tubulin polymerization represents a classic target whose function can be allosterically modulated by small molecules. Several protein–protein complexes that regulate apoptosis, or programmed cell death, appear to be particularly amenable to inhibition by small molecules, and recently described compounds have helped to characterize Bcl-2, MDM2 and XIAP as drug targets. Additionally, small-molecule antagonists have recently been described for several new targets, including Rac1–Tiam1, β-catenin–T cell factor (Tcf), and Sur-2–ESX. Not only is the list of protein–protein inhibitors growing, but the inhibitors themselves are moving closer to treating disease. |
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| AbstractList | There has been much progress in the discovery of small, organic molecules that inhibit protein-protein interactions, particularly in the field of cancer. Tubulin polymerization represents a classic target whose function can be allosterically modulated by small molecules. Several protein-protein complexes that regulate apoptosis, or programmed cell death, appear to be particularly amenable to inhibition by small molecules, and recently described compounds have helped to characterize Bcl-2, MDM2 and XIAP as drug targets. Additionally, small-molecule antagonists have recently been described for several new targets, including Rac1-Tiam1, beta-catenin-T cell factor (Tcf), and Sur-2-ESX. Not only is the list of protein-protein inhibitors growing, but the inhibitors themselves are moving closer to treating disease. There has been much progress in the discovery of small, organic molecules that inhibit protein–protein interactions, particularly in the field of cancer. Tubulin polymerization represents a classic target whose function can be allosterically modulated by small molecules. Several protein–protein complexes that regulate apoptosis, or programmed cell death, appear to be particularly amenable to inhibition by small molecules, and recently described compounds have helped to characterize Bcl-2, MDM2 and XIAP as drug targets. Additionally, small-molecule antagonists have recently been described for several new targets, including Rac1–Tiam1, β-catenin–T cell factor (Tcf), and Sur-2–ESX. Not only is the list of protein–protein inhibitors growing, but the inhibitors themselves are moving closer to treating disease. |
| Author | Arkin, Michelle |
| Author_xml | – sequence: 1 givenname: Michelle surname: Arkin fullname: Arkin, Michelle email: mra@sunesis.com organization: Sunesis Pharmaceuticals, 341 Oyster Point Blvd, South San Francisco, California 94080, USA |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/15939335$$D View this record in MEDLINE/PubMed |
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| SubjectTerms | Animals Antineoplastic Agents - metabolism Antineoplastic Agents - pharmacology Antineoplastic Agents - therapeutic use Apoptosis - drug effects Humans Ligands Neoplasm Proteins - antagonists & inhibitors Neoplasm Proteins - metabolism Neoplasms - drug therapy Neoplasms - metabolism Neoplasms - pathology Protein Binding |
| Title | Protein–protein interactions and cancer: small molecules going in for the kill |
| URI | https://dx.doi.org/10.1016/j.cbpa.2005.03.001 https://www.ncbi.nlm.nih.gov/pubmed/15939335 https://search.proquest.com/docview/17499991 https://search.proquest.com/docview/67908474 |
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