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STAR Protocols|August 2, 2021
Functional assays with human patient-derived enteroid monolayers to assess the human gut barrierIbrahim M Sayed, Courtney Tindle, Ayden G Fonseca, et al.
The Journal of Biological Chemistry|June 12, 2002
Human mannose 6-phosphate-uncovering enzyme is synthesized as a proenzyme that is activated by the endoprotease furinHung Do, Wang-Sik Lee, Pradipta Ghosh, et al.
Frontiers in Physiology|April 24, 2020
Computational Approach to Identifying Universal Macrophage BiomarkersDharanidhar Dang, Sahar Taheri, Soumita Das, et al.
The American Journal of Pathology|September 28, 2011
Phosphorylation of podocalyxin (Ser415) Prevents RhoA and ezrin activation and disrupts its interaction with the actin cytoskeletonHirotaka Fukasawa, Hiroaki Obayashi, Sandra Schmieder, et al.
Journal of the American Society of Nephrology : JASN|July 12, 2014
GIV/girdin links vascular endothelial growth factor signaling to Akt survival signaling in podocytes independent of nephrinHonghui Wang, Taro Misaki, Vanessa Taupin, et al.
Science Signaling|June 4, 2024
Growth factor-dependent phosphorylation of Gαi shapes canonical signaling by G protein-coupled receptorsSuchismita Roy, Saptarshi Sinha, Ananta James Silas, et al.
The Journal of Biological Chemistry|June 10, 2011
G Protein binding sites on Calnuc (nucleobindin 1) and NUCB2 (nucleobindin 2) define a new class of G(alpha)i-regulatory motifsMikel Garcia-Marcos, Patrick S Kietrsunthorn, Honghui Wang, et al.
Molecular Biology of the Cell|October 13, 2017
A Daple-Akt feed-forward loop enhances noncanonical Wnt signals by compartmentalizing β-cateninNicolas Aznar, Nina Sun, Ying Dunkel, et al.
Iscience|June 27, 2020
GIV/Girdin and Exo70 Collaboratively Regulate the Mammalian Polarized Exocytic MachineryCristina Rohena, Navin Rajapakse, I-Chung Lo, et al.
Biorxiv : the Preprint Server for Biology|July 29, 2024
FORWARD: A Learning Framework for Logical Network Perturbations to Prioritize Targets for Drug DevelopmentSaptarshi Sinha, Ella McLaren, Madhubanti Mullick, et al.
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