JiaBei Lin
University of Pennsylvania
33 Papers
20 Citations
JiaBei Lin is an academic researcher from University of Pennsylvania. The author has contributed to research in topics: CLPB & Biology. The author has an hindex of 11, co-authored 24 publications. Previous affiliations of JiaBei Lin include University of Alabama at Birmingham & University of Alabama.
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Papers
Ratchet-like polypeptide translocation mechanism of the AAA+ disaggregase Hsp104.
Stephanie N. Gates,Adam L. Yokom,JiaBei Lin,Meredith E. Jackrel,Alexandrea N. Rizo,Nathan M. Kendsersky,Courtney E. Buell,Elizabeth A. Sweeny,Korrie L. Mack,Edward Chuang,Mariana P. Torrente,Mariana P. Torrente,Min Su,James Shorter,Daniel R. Southworth +14 more
TL;DR: Cryo-electron microscopy structures of the Hsp104 disaggregase bound to an unfolded polypeptide substrate in its channel reveal substrate interactions and two different translocation states and helps explain how this molecular machine can solubilize protein aggregates and amyloids.
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Structural basis for substrate gripping and translocation by the ClpB AAA+ disaggregase.
Alexandrea N. Rizo,Alexandrea N. Rizo,JiaBei Lin,Stephanie N. Gates,Eric Tse,Stephen M. Bart,Laura M. Castellano,Frank DiMaio,James Shorter,Daniel R. Southworth +9 more
TL;DR: NBD conformations at the seam interface reveal how ATP hydrolysis-driven substrate disengagement and re-binding are precisely tuned to drive a directional, stepwise translocation cycle.
Conformational plasticity of the ClpAP AAA+ protease couples protein unfolding and proteolysis.
Kyle E. Lopez,Alexandrea N. Rizo,Eric Tse,JiaBei Lin,Nathaniel W. Scull,Aye C. Thwin,Aaron L. Lucius,James Shorter,Daniel R. Southworth +8 more
TL;DR: Cryo-EM structures of Escherichia coli ClpAP undergoing active substrate unfolding and proteolysis reveal contacts that drive substrate translocation and a dynamic switch mechanism at the ClpA–ClpP interface.
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DAXX represents a new type of protein-folding enabler
Liangqian Huang,Trisha Agrawal,Guixin Zhu,Sixiang Yu,Liming Tao,JiaBei Lin,Ronen Marmorstein,James Shorter,Xiaolu Yang +8 more
TL;DR: In this paper, a polyD/E protein called DAXX has been shown to have several protein-folding activities, such as preventing aggregation, solubilizing pre-existing aggregates and unfolding misfolded species of model substrates and neurodegeneration-associated proteins.
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Potentiating Hsp104 activity via phosphomimetic mutations in the middle domain.
Amber Tariq,JiaBei Lin,Megan M. Noll,Mariana P. Torrente,Korrie L. Mack,Oscar A. Hernandez Murillo,Meredith E. Jackrel,James Shorter +7 more
TL;DR: It is suggested that phosphorylation of T499 or S535 may elicit enhanced Hsp104 disaggregase activity in a reversible and regulated manner.
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