Showing results (341-350 of 536) with videos related to
Sort By:
Pageof 54
American Journal of Physiology. Lung Cellular and Molecular Physiology|November 22, 2018
Tissue-informed engineering strategies for modeling human pulmonary diseasesKolene E Bailey, Michael L Floren, Tyler J D'Ovidio, et al.Dysphagia|August 20, 2015
The Physiologic Impact of Unilateral Recurrent Laryngeal Nerve (RLN) Lesion on Infant Oropharyngeal and Esophageal PerformanceFrancois D H Gould, Andrew R Lammers, Jocelyn Ohlemacher, et al.Journal of Applied Physiology (Bethesda, Md. : 1985)|December 19, 2015
Central nervous system integration of sensorimotor signals in oral and pharyngeal structures: oropharyngeal kinematics response to recurrent laryngeal nerve lesionFrancois D H Gould, Jocelyn Ohlemacher, Andrew R Lammers, et al.The Biochemical Journal|March 10, 2001
Comparative study of protein tyrosine phosphatase-epsilon isoforms: membrane localization confers specificity in cellular signallingJ N Andersen, A Elson, R Lammers, et al.Microbiology (Reading, England)|December 5, 2009
Connecting parts with processes: SubtiWiki and SubtiPathways integrate gene and pathway annotation for Bacillus subtilisChristoph R Lammers, Lope A Flórez, Arne G Schmeisky, et al.Journal of Biomechanical Engineering|May 24, 2011
A microstructurally driven model for pulmonary artery tissuePhilip H Kao, Steven R Lammers, Lian Tian, et al.European Journal of Biochemistry|November 15, 1995
Phosphotyrosine residues in the nerve-growth-factor receptor (Trk-A). Their role in the activation of inositolphospholipid metabolism and protein kinase cascades in phaeochromocytoma (PC12) cellsR M Baxter, P Cohen, A Obermeier, et al.The Journal of Biological Chemistry|June 23, 1995
Shc binding to nerve growth factor receptor is mediated by the phosphotyrosine interaction domainI Dikic, A G Batzer, P Blaikie, et al.Physical Review Letters|October 8, 2016
Spin-Orbit Twisted Spin Waves: Group Velocity ControlF Perez, F Baboux, C A Ullrich, et al.Cell Regulation|January 1, 1990
Domain deletion in the extracellular portion of the EGF-receptor reduces ligand binding and impairs cell surface expressionI Lax, F Bellot, A M Honegger, et al.Pageof 54