@article{
 title = {Allosteric regulation of PKM2 allows cellular adaptation to different physiological states.},
 type = {article},
 year = {2013},
 identifiers = {[object Object]},
 keywords = {Adaptation, Physiological,Allosteric Regulation,Carrier Proteins,Carrier Proteins: physiology,Humans,Membrane Proteins,Membrane Proteins: physiology,Thyroid Hormones,Thyroid Hormones: physiology},
 pages = {pe7},
 volume = {6},
 websites = {http://www.ncbi.nlm.nih.gov/pubmed/23423437},
 month = {2},
 day = {19},
 id = {c836c3ab-e1aa-3140-8171-bf60845a03f5},
 created = {2016-04-27T01:22:45.000Z},
 accessed = {2016-04-27},
 file_attached = {false},
 profile_id = {95ad1c8a-ddc5-3572-ab20-1b5660ace0c4},
 group_id = {409b6953-b59c-338c-b6e7-a89d45a37162},
 last_modified = {2016-04-27T01:22:45.000Z},
 read = {false},
 starred = {false},
 authored = {false},
 confirmed = {true},
 hidden = {false},
 abstract = {Pyruvate kinase isoform M2 (PKM2) activity is subject to complex allosteric regulation. Recently, serine and SAICAR (succinylaminoimidazolecarboxamide ribose-5'-phosphate) were identified as previously unrecognized activators of PKM2. These findings add additional complexity to how PKM2 is regulated in cells and support the notion that modulating PKM2 activity enables cells to adapt their metabolic state to specific physiological contexts.},
 bibtype = {article},
 author = {Gui, Dan Y and Lewis, Caroline A and Vander Heiden, Matthew G},
 journal = {Science signaling},
 number = {263}
}

{"_id":"pZAR4FNNoQmB84BWr","bibbaseid":"gui-lewis-vanderheiden-allostericregulationofpkm2allowscellularadaptationtodifferentphysiologicalstates-2013","downloads":0,"creationDate":"2016-04-27T01:34:32.809Z","title":"Allosteric regulation of PKM2 allows cellular adaptation to different physiological states.","author_short":["Gui, D., Y.","Lewis, C., A.","Vander Heiden, M., G."],"year":2013,"bibtype":"article","biburl":null,"bibdata":{"title":"Allosteric regulation of PKM2 allows cellular adaptation to different physiological states.","type":"article","year":"2013","identifiers":"[object Object]","keywords":"Adaptation, Physiological,Allosteric Regulation,Carrier Proteins,Carrier Proteins: physiology,Humans,Membrane Proteins,Membrane Proteins: physiology,Thyroid Hormones,Thyroid Hormones: physiology","pages":"pe7","volume":"6","websites":"http://www.ncbi.nlm.nih.gov/pubmed/23423437","month":"2","day":"19","id":"c836c3ab-e1aa-3140-8171-bf60845a03f5","created":"2016-04-27T01:22:45.000Z","accessed":"2016-04-27","file_attached":false,"profile_id":"95ad1c8a-ddc5-3572-ab20-1b5660ace0c4","group_id":"409b6953-b59c-338c-b6e7-a89d45a37162","last_modified":"2016-04-27T01:22:45.000Z","read":false,"starred":false,"authored":false,"confirmed":"true","hidden":false,"abstract":"Pyruvate kinase isoform M2 (PKM2) activity is subject to complex allosteric regulation. Recently, serine and SAICAR (succinylaminoimidazolecarboxamide ribose-5'-phosphate) were identified as previously unrecognized activators of PKM2. These findings add additional complexity to how PKM2 is regulated in cells and support the notion that modulating PKM2 activity enables cells to adapt their metabolic state to specific physiological contexts.","bibtype":"article","author":"Gui, Dan Y and Lewis, Caroline A and Vander Heiden, Matthew G","journal":"Science signaling","number":"263","bibtex":"@article{\n title = {Allosteric regulation of PKM2 allows cellular adaptation to different physiological states.},\n type = {article},\n year = {2013},\n identifiers = {[object Object]},\n keywords = {Adaptation, Physiological,Allosteric Regulation,Carrier Proteins,Carrier Proteins: physiology,Humans,Membrane Proteins,Membrane Proteins: physiology,Thyroid Hormones,Thyroid Hormones: physiology},\n pages = {pe7},\n volume = {6},\n websites = {http://www.ncbi.nlm.nih.gov/pubmed/23423437},\n month = {2},\n day = {19},\n id = {c836c3ab-e1aa-3140-8171-bf60845a03f5},\n created = {2016-04-27T01:22:45.000Z},\n accessed = {2016-04-27},\n file_attached = {false},\n profile_id = {95ad1c8a-ddc5-3572-ab20-1b5660ace0c4},\n group_id = {409b6953-b59c-338c-b6e7-a89d45a37162},\n last_modified = {2016-04-27T01:22:45.000Z},\n read = {false},\n starred = {false},\n authored = {false},\n confirmed = {true},\n hidden = {false},\n abstract = {Pyruvate kinase isoform M2 (PKM2) activity is subject to complex allosteric regulation. Recently, serine and SAICAR (succinylaminoimidazolecarboxamide ribose-5'-phosphate) were identified as previously unrecognized activators of PKM2. These findings add additional complexity to how PKM2 is regulated in cells and support the notion that modulating PKM2 activity enables cells to adapt their metabolic state to specific physiological contexts.},\n bibtype = {article},\n author = {Gui, Dan Y and Lewis, Caroline A and Vander Heiden, Matthew G},\n journal = {Science signaling},\n number = {263}\n}","author_short":["Gui, D., Y.","Lewis, C., A.","Vander Heiden, M., G."],"urls":{"Website":"http://www.ncbi.nlm.nih.gov/pubmed/23423437"},"bibbaseid":"gui-lewis-vanderheiden-allostericregulationofpkm2allowscellularadaptationtodifferentphysiologicalstates-2013","role":"author","keyword":["Adaptation","Physiological","Allosteric Regulation","Carrier Proteins","Carrier Proteins: physiology","Humans","Membrane Proteins","Membrane Proteins: physiology","Thyroid Hormones","Thyroid Hormones: physiology"],"downloads":0},"search_terms":["allosteric","regulation","pkm2","allows","cellular","adaptation","different","physiological","states","gui","lewis","vander heiden"],"keywords":["adaptation","physiological","allosteric regulation","carrier proteins","carrier proteins: physiology","humans","membrane proteins","membrane proteins: physiology","thyroid hormones","thyroid hormones: physiology"],"authorIDs":[]}