Xiao_Yiling

Yiling Xiao | Postdoctoral Scholar

yiling.xiao at utsouthwestern.edu

Yiling received her B.S. in chemistry from Peking University in China, and Ph.D. in chemistry from University of Illinois at Chicago, IL, under the mentorship of Dr. Yoshitaka Ishii. Her Ph.D. thesis work focused on studying the structures and propagation properties of misfolded aggregates of Aβ(1–42), which show pathological significance in Alzheimer’s Disease, using solid-state NMR and other methods. She received Baxter Young Investigator Award in August 2014. Her work on the structure of Aβ(1–42) fibrils was honored with the poster award at the 2014 International Conference on Magnetic Resonance in Biological Systems and was published in Nature Structure & Molecular Biology.

In January 2017, she joined Dr. Kendra Frederick’s lab and is working to determine atomic-level structures of the metastable, aggregation prone proteins involved in the progression of Alzheimer’s disease.

PEER REVIEWED PUBLICATIONS

DNP-assisted NMR investigation of proteins at endogenous levels in cellular milieu
Costello, W. N., Xiao, Y., Frederick, K. K.
Methods in Enzymology (2018) in press.

Solid State NMR Studies of Amyloid Materials: A Protocol to Define An Atomic Model of Aβ(1–42) in Amyloid Fibrils.
Xiao, Y., McElheny, D.,  Hoshi, M.  and Ishii, Y.
Methods Mol. Biol. (2018) 1777:407

E22G Pathogenic Mutation of β-Amyloid (Aβ) Enhances Misfolding of Aβ40 by Unexpected Prion-like Cross Talk between Aβ42 and Aβ40.
Yoo BK, Xiao Y, McElheny D, Ishii Y.
JACS (2018) 140:2781-2784.

Aβ(1–42) Fibril Structure Illuminates Self-recognition and Replication of Amyloid in Alzheimer’s Disease.
Xiao, Y., Ma, B., McElheny, D., Parthasarathy, S., Long, F., Hoshi, M., Nussinov, R., Ishii, Y.
Nature Structural and Molecular Biology, 22:499-505 (2015).

Structural Insight into An Alzheimer’s Brain-Derived Spherical Assembly of Amyloid β by Solid-State NMR.
Parthasarathy, S., Inoue, M.,  Xiao, Y., Nabeshima,Y., Hoshi, M., Ishii, Y.
Journal of the American Chemical Society, 137: 6480-6483 (2015).

Nano-mole Scale Sequential Signal Assignment by 1H-Detected Protein Solid-State NMR.
Wang, W., Parthasarathy, S., Xiao, Y.,  Nishiyama, Y., Long, F., Matsuda, I., Endo, Y., Nemoto, T., Yamauchi, K., Asakura, T., Takeda, M., Terauchi, T., Kainoshogi, M., Ishii. Y.
Chemical Communications, 51:15055-15058 (2015).

Molecular-Level Examination of Cu2+ Binding Structure for Amyloid Fibrils of 40-Residue Alzheimer’s β by Solid-State NMR Spectroscopy.
Parthasarathy, S., Long, F., Miller, Y., Xiao, Y., McElheny, D., Thurber, K., Ma, B., Nussinov, R., Ishii, Y.
Journal of the American Chemical Society, 133:3390-3400 (2011).

Simultaneous Discrimination of Jasmonic Acid Stereoisomers by CE-QTOF-MS Employing the Partial Filling Technique.
Han, Y., Bai, Y., Xiao, Y., Du, F., Liang, Y., Tan, Z., Zhao, M., Liu, H.
Electrophoresis, 32:2693-2699 (2011).

ORAL PRESENTATIONS (selected)

  • International Council on Magnetic Resonance in Biological Systems, Solid-state NMR Studies Reveal Distinctive Structural and Kinetic Features of 42-Residue β-Amyloid Aggregate (2014).
  • Baxter-UIC NMR Exchange Meeting, Elucidating Structure of Two Distinct Amyloid Fibrils of Aβ(1–42) (2013).
  • Chicago Area NMR Discussion Group Meeting, Structural Studies of Aβ (1–42) in Fibrillar and Spherical Assemblies by SSNMR (2012).

POSTER PRESENTATIONS

  • Practical Applications of NMR in industry Conference, Aβ(1–42) Fibril Structure Illuminates Cross-Propagation Barrier in Alzheimer’s (2015).
  • International Council on Magnetic Resonance in Biological Systems, Solid-state NMR Studies Reveal Distinctive Structural and Kinetic Features of 42-Residue β-Amyloid Aggregate (2014).
  • Rocky Mountain Conference on Magnetic Resonance, Aβ(1–42) Fibril Structure Illuminates Propagation Barrier in Alzheimer’s (2014).
  • 54th Experimental Nuclear Magnetic Resonance Conference, SSNMR Studies of Amyloid Fibril and Pathologically Relevant Spherical Amyloid Amylospheroid for Aβ(1–42)(2013).
  • 53rd Experimental Nuclear Magnetic Resonance Conference, Structural Studies of Aβ (1–42) in Fibrillar and Spherical Assemblies by SSNMR (April, 2012).
  • 6th Midwest Conference on Protein Folding, Assembly and Molecular Motions, Solid-state NMR Analysis of Misfolding Kinetics and Structure for Amyloid Fibril of 42-Residue Alzheimer’s β Peptide (2011).
  • 52nd Experimental Nuclear Magnetic Resonance Conference, Solid-state NMR Analysis of Misfolding Kinetics and Structure for Amyloid Fibril of 42-Residue Alzheimer’s β Peptide (2011).