J
Jialing Lin
Researcher at University of Oklahoma Health Sciences Center
Publications - 46
Citations - 2857
Jialing Lin is an academic researcher from University of Oklahoma Health Sciences Center. The author has contributed to research in topics: Bcl-2-associated X protein & Membrane protein. The author has an hindex of 24, co-authored 41 publications receiving 2659 citations. Previous affiliations of Jialing Lin include University of Oklahoma & University of Tennessee Health Science Center.
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Embedded together: The life and death consequences of interaction of the Bcl-2 family with membranes
TL;DR: The embedding together model proposes that both pro- and anti-apoptotic Bcl-2 family proteins engage in similar dynamic interactions that are governed by membrane dependent conformational changes and culminate in either aborted or productive membrane permeabilization depending on the final oligomeric state of pro-ap optotic Bax and/or Bak.
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Both Lumenal and Cytosolic Gating of the Aqueous ER Translocon Pore Are Regulated from Inside the Ribosome during Membrane Protein Integration
TL;DR: The ribosome first recognizes the transmembrane segment and triggers long-range structural changes at the translocon that may be involved in shifting its function from translocation to integration, as shown by compartment-specific collisional quenching of fluorophores incorporated into the polypeptide.
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The Cotranslational Integration of Membrane Proteins into the Phospholipid Bilayer Is a Multistep Process
TL;DR: During the cotranslational integration of a nascent protein into the endoplasmic reticulum membrane, the transmembrane sequence moves out of an aqueous pore formed by Sec61alpha, TRAM, and other proteins and into the nonpolar lipid bilayer.
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Bcl-2 changes conformation to inhibit Bax oligomerization
Paulina J Dlugosz,Lieven P. Billen,Matthew G. Annis,Weijia Zhu,Zhi Zhang,Jialing Lin,Brian Leber,David W. Andrews +7 more
TL;DR: Bcl‐2 functions as an inhibitor of mitochondrial permeabilization by changing conformation in the mitochondrial membrane to bind membrane‐inserted Bax monomers and prevent productive oligomerization of Bax.
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A Short Nur77-Derived Peptide Converts Bcl-2 from a Protector to a Killer
Siva Kumar Kolluri,Xiuwen Zhu,Xin Zhou,Bingzhen Lin,Ya Chen,Kai Sun,Xuefei Tian,James Town,Xihua Cao,Feng Lin,Dayong Zhai,Shinichi Kitada,Frederick Luciano,Edmond F. O’Donnell,Yu Cao,Feng He,Jialing Lin,John C. Reed,Arnold C. Satterthwait,Xiao-kun Zhang +19 more
TL;DR: The identification of a Nur77-derived Bcl-2-converting peptide with 9 amino acids (NuBCP-9) and its enantiomer, which induce apoptosis of cancer cells in vitro and in animals.