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Noel Lazo is a Professor in the Carlson School of Chemistry and Biochemistry. His laboratory is currently focusing on the proteolytic degradation and aggregation of proteins associated with late onset disorders including Alzheimer's disease and related dementias and type 2 diabetes. A combination of spectroscopic (e.g., NMR spectroscopy), spectrometric (e.g., mass spectrometry), and biochemical (e.g., limited proteolysis) methods is used to decipher mechanisms for protein oligomerization and proteolytic degradation. Since joining Clark in 2006, Dr. Lazo has mentored over 50 graduate and undergraduate students, some of whom have co-authored publications - a good indicator of their motivation and dedication to contribute to research associated with disease.
Courses Taught:
CHEM 101 (Introductory Chemistry I, Lecture)
CHEM 102 (Introductory Chemistry II, Lecture)
CHEM 289 (Research Methods: Circular Dichroism Spectroscopy)
BCMB 264 (Biophysical Chemistry, Lecture + Laboratory)
BCMB 266 (Biomolecular NMR Spectroscopy)
BCMB 271 (Biochemistry I, Lecture)
BCMB 297 (Amyloid Proteins)Degrees
- Ph.D. in Chemistry, Solid-state NMR, Texas A&M University, 1991
Affiliated Department(s)
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Scholarly and Creative Works
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How Aβ peptides modulate insulin degradation in Alzheimer's and diabetes
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2024
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Highly Toxic Aβ Begets More Aβ
Neural Regeneration Research
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2024
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Vol. 19
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Issue #9
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Modulation of the Activity of the Insulin-degrading Enzyme by Aβ Peptides
ACS Chemical Neuroscience
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2023
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Vol. 14
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Exchange Broadening Underlies the Enhancement of IDE-Dependent Degradation of Insulin by Anionic Membranes
ACS Omega
2022
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2022
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Vol. 7
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Issue #28
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Differential Effects of Polyphenols on Insulin Proteolysis by the Insulin-Degrading Enzyme
Antioxidants (Basel)
2021
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2021
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Vol. 10
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Issue #9
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Helix Dipole and Membrane Electrostatics Delineate Conformational Transitions in the Self-Assembly of Amyloidogenic Peptides
Langmuir
2020
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2020
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Vol. 36
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Issue #29
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Inhibition of the Self-Assembly of Aβ and of Tau by Polyphenols: Mechanistic Studies
Molecules
2019
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2019
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Vol. 24
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Issue #12
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Mechanistic Studies of the Inhibition of Insulin Fibril Formation by Rosmarinic Acid
J Phys Chem B
2018
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2018
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Vol. 122
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Issue #8
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The Longest Amyloid-β Precursor Protein Intracellular Domain Produced with Aβ42 Forms β-Sheet-Containing Monomers That Self-Assemble and Are Proteolyzed by Insulin-Degrading Enzyme
ACS Chem Neurosci
2018
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2018
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Vol. 9
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Issue #12
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Enzyme kinetics from circular dichroism of insulin reveals mechanistic insights into the regulation of insulin-degrading enzyme
Biosci Rep
2018
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2018
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Vol. 38
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Issue #6
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Resveratrol Sustains Insulin-Degrading Enzyme Activity toward Aβ42
ACS Omega
2018
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2018
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Vol. 3
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Issue #10
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A versatile platform for adding functional properties to amyloid fibrils
Org Biomol Chem
2017
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2017
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Vol. 15
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Issue #38
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Binding Modes of Thioflavin T on the Surface of Amyloid Fibrils Studied by NMR
Chemphyschem
2016
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2016
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Vol. 17
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Issue #16
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K114 (trans, trans)-bromo-2,5-bis(4-hydroxystyryl)benzene is an efficient detector of cationic amyloid fibrils
Protein Sci
2015
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2015
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Vol. 24
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Issue #3
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Helix-dipole effects in peptide self-assembly to amyloid
Biochemistry
2012
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2012
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Vol. 51
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Issue #20
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Curcumin modulates the self-assembly of the islet amyloid polypeptide by disassembling α-helix
Biochem Biophys Res Commun
2012
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2012
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Vol. 422
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Issue #4
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Kinetic profile of amyloid formation in the presence of an aromatic inhibitor by nuclear magnetic resonance
ACS Med Chem Lett
2012
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2012
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Vol. 3
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Issue #10
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Conformational analysis of thioflavin T bound to the surface of amyloid fibrils
Langmuir
2012
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2012
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Vol. 28
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Issue #48
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Mechanistic studies of peptide self-assembly: transient α-helices to stable β-sheets
J Am Chem Soc
2010
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2010
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Vol. 132
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Issue #51
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Awards & Grants
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Determinants of the Proteolytic Degradation of Soluble Amyloid-beta
National Institute on Aging/NIH
Mar. 1, 2018 - Nov. 30, 2021
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