Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Lauren R. Sheckler"'
Autor:
Lauren R. Sheckler, Irving L. Weissman, Stephen A. Stimpson, Massimiliano Cerletti, Joshua J. Schroeder, Amy J. Wagers, John T. Moore, Matthew A. Inlay, Tata Nageswara Rao, Dave J. Becherer, Derrick J. Rossi, Tsu T. Chuang, Deepti A. Cole
Publikováno v:
SSRN Electronic Journal.
Skeletal muscle normally exhibits robust regenerative potential in youth; however, myogenic activity declines with age, resulting in defective muscle repair after injury. In this study, we identified signaling pathways in mouse muscle stem cells that
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::bb09ee48d13552e4d63a0315a8951b12
https://doi.org/10.2139/ssrn.3244794
https://doi.org/10.2139/ssrn.3244794
Autor:
David M. Bickett, Francis X. Tavares, Pamela L. Golden, Lauren R. Sheckler, Stephen A. Thomson, Dulce Garrido, Andrew J. Peat, Pierette Banker, James E. Weiel, Steven M. Sparks, Scott Howard Dickerson, Daphne C. Clancy
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 19:981-985
Optimization of the amino acid residue of a series of anthranilimide-based glycogen phosphorylase inhibitors is described leading to the identification of serine and threonine ether analogs. t-Butylthreonine analog 20 displayed potent in vitro inhibi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5159b246433fa9027e6bcec99dce7745
https://doi.org/10.1016/j.bmcl.2008.11.084
https://doi.org/10.1016/j.bmcl.2008.11.084
Autor:
Pierette Banker, Daphne C. Clancy, Francis X. Tavares, Pamela L. Golden, Liping Wang, James E. Weiel, Steven M. Sparks, Stephen A. Thomson, Lauren R. Sheckler, Dulce Garrido, Scott Howard Dickerson, Andrew J. Peat, David M. Bickett, H. Luke Carter, Kate A. Dwornik, Robert T. Nolte
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 19:976-980
Optimization of the amino acid residue within a series of anthranilimide-based glycogen phosphorylase inhibitors is described. These studies culminated in the identification of anthranilimides 16 and 22 which displayed potent in vitro inhibition of G
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ccab5b862050e9a20580b438b03c30f9
https://doi.org/10.1016/j.bmcl.2008.11.085
https://doi.org/10.1016/j.bmcl.2008.11.085
Publikováno v:
Journal of Biological Chemistry. 281:22896-22905
Neurexins mediate protein interactions at the synapse, playing an essential role in synaptic function. Extracellular domains of neurexins, and their fragments, bind a distinct profile of different proteins regulated by alternative splicing and Ca2+.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5d925f0f37eae888a46b1fa7d0c44c81
https://doi.org/10.1074/jbc.m603464200
https://doi.org/10.1074/jbc.m603464200
Autor:
David M. Bickett, Pierette Banker, Daphne C. Clancy, Joyce A. Boucheron, Stephen A. Thomson, James E. Weiel, and Andrew J. Peat, Dulce Garrido, Steven M. Sparks, Francis X. Tavares, Lauren R. Sheckler, Joel P. Cooper, Scott Howard Dickerson, Liping Wang, Tony Y. Wang, Robert T. Nolte, H.L. Carter
Publikováno v:
Bioorganicmedicinal chemistry letters. 19(4)
Key binding interactions of the anthranilimide based glycogen phosphorylase a (GPa) inhibitor 2 from X-ray crystallography studies are described. This series of compounds bind to the AMP site of GP. Using the binding information the core and the phen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::315bf00dccdab187675054ab81ac0fef
https://pubmed.ncbi.nlm.nih.gov/19138846
https://pubmed.ncbi.nlm.nih.gov/19138846
Publikováno v:
The Journal of biological chemistry. 281(32)
Neurexins mediate protein interactions at the synapse, playing an essential role in synaptic function. Extracellular domains of neurexins, and their fragments, bind a distinct profile of different proteins regulated by alternative splicing and Ca2+.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::5ca5bf7fa3da9a2c14e7d99ddedc31de
https://pubmed.ncbi.nlm.nih.gov/16772286
https://pubmed.ncbi.nlm.nih.gov/16772286
Autor:
Kaiser C. Shen, Dorota A. Kuczynska, Gabrielle Rudenko, Irene J. Wu, Beverly Murray, Lauren R. Sheckler
Publikováno v:
Structure. (3):422-431
Neurexins and neuroligins play an essential role in synapse function, and their alterations are linked to autistic spectrum disorder. Interactions between neurexins and neuroligins regulate inhibitory and excitatory synaptogenesis in vitro through a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c5619fc9899495f70a41a476fe58edce