Evita Paraskevi Tsiolaki, PhD

Department of Biochemistry & Biophysics
University of California, San Francisco
600 16th St., S416
San Francisco CA
94143-2240
(415) 476-5143 (Ph)
email

Research

My research goal is to elucidate the molecular mechanisms by which Hsp70 blocks alpha-synuclein (ASyn) oligomerization at atomic resolution using “State-of-the-Art” cryoEM methods. A joint collaboration between the Agard and McConlogue labs has recently discovered that Hsp70 can block ASyn oligomerization by a novel mechanism that surprisingly does not involve the canonical substrate binding site of Hsp70. This potentially specific and targetable action of Hsp70 could be a key component of its protection against ASyn pathogenicity. Our strategy is technically innovative utilizing a broad combination of cryoEM, single molecule and biochemical methodologies to determine the molecular mechanisms of non-canonical Hsp70-ASyn interactions. The mechanistic understanding gained here may apply to other amyloidogenic proteins and to additional Hsp70 family members.

 

Publications

(* denotes equal contribution)

 

Tsiolaki, P.L., Katsafana, A.D., Baltoumas, F.A., Louros, N.N., Iconomidou, V.A. 2019, Hidden Aggregation Hot-Spots on Human Apolipoprotein E: a Structural Study, International Journal of Molecular Sciences, 20(9): E2274

 

Tsiolaki, P.L., Nasi, G.I., Baltoumas, F.A., Fishman S., Tu H.C., Iconomidou, V.A. 2019. Delving into the Amyloidogenic Core of Human Leukocyte Chemotactic Factor 2, Journal of Structural Biology 207 (3), 260-269

 

Nastou, K.C.*, Nasi, G.I.*, Tsiolaki, P.L.*, Litou, Z.I. and Iconomidou, V.A. 2019. AmyCo: the Amyloidoses Collection, Amyloid 26, 3

Tsiolaki, P.L., Louros N.N., Iconomidou V.A. 2018. Hexapeptide Tandem Repeats Dictate the Fibrillogenesis of Silkmoth Chorion Protective Amyloids, Journal of Molecular Biology 430 (20), 3774 – 3783.

 

Tsiolaki, P.L., Nastou K.C., Louros N.N., Hamodrakas S.J., Iconomidou V.A. 2018. Exploring amyloidogenicity of Clusterin: a structural and bioinformatics analysis, Advances in Experimental Medicine and Biology, 989, 93 – 107.

 

Tsiolaki, P.L., Nasi, G.I., Baltoumas, F.A., Louros, N.N., Magafa, V., Hamodrakas, S.J. and Iconomidou, V.A. 2017. αCGRP, another amyloidogenic member of the CGRP family.  Journal of Structural Biology 203 (1), 27 – 36.

 

Louros, N.N., Tsiolaki, P.L., Baltoumas, F.A., Chryssikos, G.D., Gionis, V., Hamodrakas, S.J.  and Iconomidou, V.A. 2017. Tracking the amyloidogenic core of IAPP amyloid fibrils: Insights from micro-Raman spectroscopy. Journal of Structural Biology 199(2), 140 – 152.

 

Tsiolaki, P.L.*, Nastou, K.C.*1, Hamodrakas, S.J., Iconomidou, V.A. 2017. Mining Databases for Protein Aggregation: a Review. Amyloid 24, 3.

Biza, K.V.*, Nastou, K.C.*, Tsiolaki, P.L.*, Mastrokalou, C.V., Hamodrakas, S.J., Iconomidou, V.A. 2017. The amyloid interactome: Exploring protein aggregation. PLoS ONE 12(3): e0173163.

 

Tsiolaki, P.L., Louros, N.N., Zompra, A.A., Hamodrakas, S.J., Iconomidou, V.A. 2016. Unraveling the aggregation propensity of the insulin C-peptide, Biopolymers:Peptide Science, 108.

 

Louros, N.N., Bolas G.M.P, Tsiolaki, P.L., Hamodrakas, S.J., Iconomidou, V.A. 2016. Curli Fiber Formation Is Initiated by the Intrinsic Aggregation Propensity of the CsgB Nucleator Protein. Journal of Structural Biology 195 (2), 179 – 89.

 

Tsiolaki, P.L., Louros, N.N., Hamodrakas, S.J., Iconomidou, V.A., 2015. Exploring the 'aggregation-prone' core of human Cystatin C: A structural study. Journal of Structural Biology 191 (3), 272 – 280.

 

Louros, N.N., Tsiolaki, P.L., Griffin, M.D., Howlett, G.J., Hamodrakas, S.J., Iconomidou, V.A., 2015. Chameleon 'aggregation-prone' segments of apoA-I: A model of amyloid fibrils formed in apoA-I amyloidosis. International Journal of Biological Macromolecules 79, 711-718.

 

Louros, N.N., Tsiolaki, P.L., Zompra, A.A., Pappa, E.V., Magafa, V., Pairas, G., Cordopatis, P., Cheimonidou, C., Trougakos, I.P., Iconomidou, V.A., Hamodrakas, S.J., 2015. Structural studies and cytotoxicity assays of "aggregation-prone" IAPP8-16 and its non-amyloidogenic variants suggest its important role in fibrillogenesis and cytotoxicity of human amylin. Biopolymers 104, 196-205.

 

Tsiolaki, P.L., Hamodrakas, S.J., Iconomidou, V.A., 2015. The pentapeptide LQVVR plays a pivotal role in human cystatin C fibrillization. FEBS Letters 589, 159-164.

Louros, N.N., Iconomidou, V.A., Tsiolaki, P.L., Chrysina, E.D., Baltatzis, G.E., Patsouris, E.S., Hamodrakas, S.J., 2014. An N-terminal pro-atrial natriuretic peptide (NT-proANP) 'aggregation-prone' segment involved in isolated atrial amyloidosis. FEBS Letters 588, 52-57.