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Peggy C. Stolt, Ph.D. - Publications

Affiliations: 
2004 Harvard University, Cambridge, MA, United States 
Area:
structure and function of cell surface receptor molecules
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6 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2006 Stolt PC, Bock HH. Modulation of lipoprotein receptor functions by intracellular adaptor proteins. Cellular Signalling. 18: 1560-71. PMID 16725309 DOI: 10.1016/J.Cellsig.2006.03.008  0.573
2006 Beffert U, Durudas A, Weeber EJ, Stolt PC, Giehl KM, Sweatt JD, Hammer RE, Herz J. Functional dissection of Reelin signaling by site-directed disruption of Disabled-1 adaptor binding to apolipoprotein E receptor 2: distinct roles in development and synaptic plasticity. The Journal of Neuroscience : the Official Journal of the Society For Neuroscience. 26: 2041-52. PMID 16481437 DOI: 10.1523/Jneurosci.4566-05.2006  0.538
2005 Stolt PC, Chen Y, Liu P, Bock HH, Blacklow SC, Herz J. Phosphoinositide binding by the disabled-1 PTB domain is necessary for membrane localization and Reelin signal transduction. The Journal of Biological Chemistry. 280: 9671-7. PMID 15632144 DOI: 10.1074/Jbc.M413356200  0.595
2004 Stolt PC, Vardar D, Blacklow SC. The dual-function disabled-1 PTB domain exhibits site independence in binding phosphoinositide and peptide ligands. Biochemistry. 43: 10979-87. PMID 15323557 DOI: 10.1021/Bi049092L  0.558
2004 Beffert U, Stolt PC, Herz J. Functions of lipoprotein receptors in neurons. Journal of Lipid Research. 45: 403-9. PMID 14657206 DOI: 10.1194/Jlr.R300017-Jlr200  0.458
2003 Stolt PC, Jeon H, Song HK, Herz J, Eck MJ, Blacklow SC. Origins of peptide selectivity and phosphoinositide binding revealed by structures of disabled-1 PTB domain complexes. Structure (London, England : 1993). 11: 569-79. PMID 12737822 DOI: 10.1016/S0969-2126(03)00068-6  0.602
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