Lin Jiang

发表

Amyloid β-protein oligomers promote the uptake of tau fibril seeds potentiating intracellular tau aggregation

G. Bitan, W. S. Shin, J. Di, 2019, Alzheimer's Research & Therapy.

David Eisenberg, Meytal Landau, Michael R. Sawaya, 2011, PLoS biology.

Annotating Protein Functional Residues by Coupling High-Throughput Fitness Profile and Homologous-Structure Analysis

R. Sun, N. Wu, Yushen Du, 2016, mBio.

Mechanistic basis for receptor-mediated pathological α-synuclein fibril cell-to-cell transmission in Parkinson's disease

T. Dawson, V. Dawson, Renxiao Wang, 2021, Proceedings of the National Academy of Sciences.

Amyloid β-protein oligomers promote the uptake of tau fibril seeds potentiating intracellular tau aggregation

G. Bitan, W. S. Shin, J. Di, 2019, Alzheimer's & Dementia.

Correction: Structure-based discovery of fiber-binding compounds that reduce the cytotoxicity of amyloid beta

M. P. Hughes, D. Eisenberg, M. Landau, 2013, eLife.

Different Amyloid-β Self-Assemblies Have Distinct Effects on Intracellular Tau Aggregation

G. Bitan, Chuanqi Sun, W. S. Shin, 2019, Front. Mol. Neurosci..

Out-of-register β-sheets suggest a pathway to toxic amyloid aggregates

D. Eisenberg, M. Sawaya, J. Nowick, 2012, Proceedings of the National Academy of Sciences.

The Amyloid State of Proteins

E. L. Guenther, David Eisenberg, Meytal Landau, 2015 .

Structural basis for reversible amyloids of hnRNPA1 elucidates their role in stress granule assembly

Xueming Li, Minglei Zhao, Dan Li, 2019, Nature Communications.

The α-synuclein hereditary mutation E46K unlocks a more stable, pathogenic fibril structure

D. Eisenberg, M. Sawaya, Chuanqi Sun, 2019, Proceedings of the National Academy of Sciences.

Structures of fibrils formed by α-synuclein hereditary disease mutant H50Q reveal new polymorphs

D. Eisenberg, M. Sawaya, Chuanqi Sun, 2019, Nature Structural & Molecular Biology.

Cryo-EM of full-length α-synuclein reveals fibril polymorphs with a common structural kernel

D. Eisenberg, Z. Zhou, M. Sawaya, 2018, Alzheimer's & Dementia.

Uncovering the Mechanism of Aggregation of Human Transthyretin

Duilio Cascio, Roland Riek, Lin Jiang, 2015, The Journal of Biological Chemistry.

Structure-Based Peptide Inhibitor Design of Amyloid-β Aggregation

D. Eisenberg, J. Nowick, Dan Li, 2019, Front. Mol. Neurosci..

A new structural model of Alzheimer's Aβ42 fibrils based on electron paramagnetic resonance data and Rosetta modeling.

Lei Gu, Zhefeng Guo, Lin Jiang, 2016, Journal of structural biology.

Human prion protein sequence elements impede cross-species chronic wasting disease transmission.

D. Eisenberg, C. Sigurdson, J. Castilla, 2015, The Journal of clinical investigation.

Cryo-EM structure of amyloid fibril formed by α-synuclein hereditary A53E mutation reveals a distinct protofilament interface.

M. Sawaya, Chuanqi Sun, Lin Jiang, 2023, The Journal of biological chemistry.

Cryo-EM structures of α-synuclein fibrils with the H50Q hereditary mutation reveal new polymorphs

D. Eisenberg, M. Sawaya, Chuanqi Sun, 2019, bioRxiv.

Structure of the toxic core of α-synuclein from invisible crystals

Nicholas K. Sauter, Sébastien Boutet, E. L. Guenther, 2015, Nature.

Atomic structures of fibrillar segments of hIAPP suggest tightly mated β-sheets are important for cytotoxicity

D. Eisenberg, José A. Rodríguez, M. Sawaya, 2016, eLife.

Structure-based discovery of fiber-binding compounds that reduce the cytotoxicity of amyloid beta

D. Eisenberg, M. Landau, Minglei Zhao, 2013, eLife.

Toward the Atomic Structure of PrPSc.

D. Eisenberg, José A. Rodríguez, Lin Jiang, 2017, Cold Spring Harbor perspectives in biology.

Antiparallel Triple-strand Architecture for Prefibrillar Aβ42 Oligomers*

J. Stroud, Lei Gu, Zhefeng Guo, 2014, The Journal of Biological Chemistry.

Asparagine and glutamine ladders promote cross-species prion conversion

D. Eisenberg, José A. Rodríguez, C. Sigurdson, 2017, The Journal of Biological Chemistry.

Human prion protein sequence elements impede cross-species chronic wasting disease transmission.

D. Eisenberg, C. Sigurdson, J. Castilla, 2015, The Journal of clinical investigation.

A Proposed Mechanism for the Promotion of Prion Conversion Involving a Strictly Conserved Tyrosine Residue in the β2-α2 Loop of PrPC*

D. Eisenberg, C. Sigurdson, Lin Jiang, 2014, The Journal of Biological Chemistry.

of PrP 2 α2 β Conserved Tyrosine Residue in the of Prion Conversion Involving a Strictly A Proposed Mechanism for the Promotion Molecular Bases of Disease :

D. Eisenberg, C. Sigurdson, Lin Jiang, 2014 .

Structural basis for reversible amyloids of hnRNPA1 elucidates their role in stress granule assembly

Xueming Li, Minglei Zhao, Dan Li, 2019, Nature Communications.

The mouse nicotinamide mononucleotide adenylyltransferase chaperones diverse pathological amyloid client proteins

Dan Li, Yaoyang Zhang, Cong Liu, 2022, The Journal of biological chemistry.

Cryo-EM of full-length α-synuclein reveals fibril polymorphs with a common structural kernel

D. Eisenberg, M. Sawaya, P. Ge, 2018, Nature Communications.

Inhibiting Amyloid-ß cytotoxicity through its interaction with the cell surface receptor LilrB2 by structure-based design

D. Black, D. Eisenberg, M. Sawaya, 2018, Nature Chemistry.

INHIBITING AMYLOID-BETA CYTOTOXICITY THROUGH ITS INTERACTION WITH THE CELL SURFACE RECEPTOR LILRB2 BY STRUCTURE-BASED DESIGN

D. Eisenberg, Q. Cao, Lin Jiang, 2019, Alzheimer's & Dementia.

Author Correction: Inhibiting amyloid-β cytotoxicity through its interaction with the cell surface receptor LilrB2 by structure-based design

D. Black, D. Eisenberg, M. Sawaya, 2018, Nature Chemistry.

Ischemic axonal injury up-regulates MARK4 in cortical neurons and primes tau phosphorylation and aggregation

Mandavi R. Oberoi, G. Bitan, A. MacKenzie-Graham, 2019, Acta Neuropathologica Communications.