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10.1586/14789450.2015.1079487 http://scihub22266oqcxt.onion/10.1586/14789450.2015.1079487 C4858316!4858316 !26400464     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=26400464 &cmd=llinks): Failed to open stream: HTTP request failed! 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Unlocking the secrets to protein-protein interface drug targets using structural mass spectrometry techniques |pdf=|usr=}}{{26400464 }} gab.com Text Unlocking the secrets to protein-protein interface drug targets using structural mass spectrometry techniques JO: Expert Rev Proteomics http://www.kidney.de/pget.php?&tw=1&pmid=26400464 #FOAvip Protein-protein interactions (PPIs) drive all biologic systems at the subcellular and extracellular level. Changes in the specificity and affinity of these interactions can lead to cellular malfunctions and disease. Consequently, the binding interfaces between interacting protein partners are important drug targets for the next generation of therapies that block such interactions. Unfortunately, protein-protein contact points have proven to be very difficult pharmacological targets because they are hidden within complex 3D interfaces. For the vast majority of characterized binary PPIs, the specific amino acid sequence of their close contact regions remains unknown. There has been an important need for an experimental technology that can rapidly reveal the functionally important contact points of native protein complexes in solution. In this review, experimental techniques employing mass spectrometry to explore protein interaction binding sites are discussed. Hydrogen-deuterium exchange, hydroxyl radical footprinting, crosslinking and the newest technology protein painting are compared and contrasted. Twit Text FOAVip Unlocking the secrets to protein-protein interface drug targets using structural mass spectrometry techniques ????Expert Rev Proteomics http://www.kidney.de/pget.php?&tw=1&pmid=26400464 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26400464 #FOAvip English Wikipedia <ref>{{Cite pmid|26400464 }}</ref> Unlocking the secrets to protein-protein interface drug targets using structural mass spectrometry techniques #MMPMID26400464 Dailing A ; Luchini A ; Liotta L Expert Rev Proteomics 2015[]; 12 (5 ): 457-67 PMID26400464 show ga Protein-protein interactions (PPIs) drive all biologic systems at the subcellular and extracellular level. Changes in the specificity and affinity of these interactions can lead to cellular malfunctions and disease. Consequently, the binding interfaces between interacting protein partners are important drug targets for the next generation of therapies that block such interactions. Unfortunately, protein-protein contact points have proven to be very difficult pharmacological targets because they are hidden within complex 3D interfaces. For the vast majority of characterized binary PPIs, the specific amino acid sequence of their close contact regions remains unknown. There has been an important need for an experimental technology that can rapidly reveal the functionally important contact points of native protein complexes in solution. In this review, experimental techniques employing mass spectrometry to explore protein interaction binding sites are discussed. Hydrogen-deuterium exchange, hydroxyl radical footprinting, crosslinking and the newest technology protein painting are compared and contrasted. |Animals [MESH] |Humans [MESH] |Mass Spectrometry/*methods [MESH] |Molecular Targeted Therapy/*methods [MESH] |Protein Interaction Mapping/*methods [MESH] |Proteome/chemistry/drug effects/*metabolism [MESH]Unlocking the secrets to protein-protein interface drug targets using (epmc).pdf DeepDyve Pubget Overpricing