Lin Jiang

发表

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.

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

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

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

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.

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.

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

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

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.

Inhibition of synucleinopathic seeding by rationally designed inhibitors

E. L. Guenther, D. Eisenberg, H. Vinters, 2020, eLife.

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.

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.

Asparagine and glutamine ladders promote cross-species prion conversion

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

Structure-Based Peptide Inhibitor Design of Amyloid-β Aggregation

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

Uncovering the Mechanism of Aggregation of Human Transthyretin

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

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

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

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

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

Inhibiting amyloid β‐protein assembly: Size–activity relationships among grape seed‐derived polyphenols

D. Teplow, G. Pasinetti, L. Ho, 2015, Journal of neurochemistry.

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

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

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

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

Common fibrillar spines of amyloid-β and human islet amyloid polypeptide revealed by microelectron diffraction and structure-based inhibitors

D. Eisenberg, José A. Rodríguez, M. Sawaya, 2017, The Journal of Biological Chemistry.

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.

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.

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.

The mouse nicotinamide mononucleotide adenylyltransferase chaperones diverse pathological amyloid client proteins

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

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

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

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.

Antiparallel Triple-strand Architecture for Prefibrillar Aβ42 Oligomers*

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

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.

Toward the Atomic Structure of PrPSc.

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

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

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

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 .

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

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

Cryo-EM structure of amyloid fibril formed by α-synuclein hereditary A53E mutation

Z. Zhou, M. Sawaya, Chuanqi Sun, 2022, bioRxiv.

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

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

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

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

Nicotinamide mononucleotide adenylyltransferase uses its NAD+ substrate-binding site to chaperone phosphorylated Tau

R. Zhai, Dan Li, Yaoyang Zhang, 2020, eLife.

Mechanistic insights into NAD synthase NMNAT chaperoning phosphorylated Tau from pathological aggregation

R. Zhai, Dan Li, Yaoyang Zhang, 2019, bioRxiv.

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.

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.

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.

Precise and Reversible Protein-Microtubule-Like Structure with Helicity Driven by Dual Supramolecular Interactions.

Xueming Li, Cong Liu, Yan Lu, 2016, Journal of the American Chemical Society.

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

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

Asparagine and glutamine ladders promote cross-species prion conversion

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