M. Nichols

发表

Differential inhibition of multiple cAMP phosphodiesterase isozymes by isoflavones and tyrphostins.

B. H. Morimoto, M. Nichols, 2000, Molecular pharmacology.

Amyloid-β(1-42) protofibrils stimulate a quantum of secreted IL-1β despite significant intracellular IL-1β accumulation in microglia.

M. J. Mohan, Shana E Terrill-Usery, M. Nichols, 2014, Biochimica et biophysica acta.

Toll‐like receptors 2 and 4 mediate Aβ(1–42) activation of the innate immune response in a human monocytic cell line

Maria L. D. Udan, M. Nichols, Deepa Ajit, 2007, Journal of neurochemistry.

Development of β-sheet structure in Aβ aggregation intermediates diminishes exposed hydrophobic surface area and enhances proinflammatory activity.

M. Nichols, Kapur B. Dhami, Sanjib Karki, 2022, Biochimica et biophysica acta. Proteins and proteomics.

CD47 does not mediate amyloid-β(1-42) protofibril-stimulated microglial cytokine release.

M. Nichols, Sanjib Karki, 2014, Biochemical and biophysical research communications.

Amyloid- β (1-42) Fibrillar Precursors are Optimal for Inducing Tumor Necrosis Factor- α Production in the THP-1 Human Monocytic Cell Line

Geeta S. Paranjape, Maria L. D. Udan, M. Nichols, 2009 .

Aβ42 Protofibrils Interact with and Are Trafficked through Microglial-Derived Microvesicles.

David C Osborn, Nyasha J. Makoni, Evan C. Garrad, 2018, ACS chemical neuroscience.

Expression of NLRP3 inflammasome proteins in ExpiCHO‐S mammalian cells reveals oligomerization properties that are highly sensitive to solution conditions

Nyasha J. Makoni, Evan C. Garrad, M. Nichols, 2021, Biotechnology progress.

Growth of beta-amyloid(1-40) protofibrils by monomer elongation and lateral association. Characterization of distinct products by light scattering and atomic force microscopy.

J. Hoh, Wen‐lang Lin, R. Mukhopadhyay, 2002, Biochemistry.

Amyloid-β42 protofibrils are internalized by microglia more extensively than monomers

Nyasha J. Makoni, Victoria A Rogers, M. Nichols, 2016, Brain Research.

Inhibition of matrix metalloproteinase-9 secretion by dimethyl sulfoxide and cyclic adenosine monophosphate in human monocytes

M. Nichols, D. Denner, Maria Udan-Johns, 2021, World journal of biological chemistry.

Inflammatory mechanisms in neurodegeneration

M. Tremblay, J. Neher, C. Combs, 2019, Journal of neurochemistry.

Human and mouse single-nucleus transcriptomics reveal TREM2-dependent and - independent cellular responses in Alzheimer’s disease

Maxim N. Artyomov, D. Bennett, D. Holtzman, 2019, Nature Medicine.

Human and mouse single-nucleus transcriptomics reveal TREM2-dependent and TREM2-independent cellular responses in Alzheimer’s disease

D. Holtzman, D. Bennett, A. Kakita, 2020, Nature Medicine.

Development of a Simple and Effective Lipid-A Antagonist Based on Computational Prediction.

M. Kontoyianni, A. Demchenko, M. Nichols, 2022, ACS infectious diseases.

Aβ40 has a subtle effect on Aβ42 protofibril formation, but to a lesser degree than Aβ42 concentration, in Aβ42/Aβ40 mixtures.

Benjamin A Colvin, Shana E Terrill-Usery, M. Nichols, 2016, Archives of biochemistry and biophysics.

Amyloid-beta(1-42) fibrillar precursors are optimal for inducing tumor necrosis factor-alpha production in the THP-1 human monocytic cell line.

Geeta S. Paranjape, Maria L. D. Udan, M. Nichols, 2009, Biochemistry.

The intricate biophysical puzzle of caspase-1 activation.

Nyasha J. Makoni, M. Nichols, 2021, Archives of biochemistry and biophysics.

APP Regulates Microglial Phenotype in a Mouse Model of Alzheimer's Disease

Brett A. McGregor, Joshua A. Kulas, D. Darland, 2016, The Journal of Neuroscience.

Characterization of recombinant, soluble beta-secretase from an insect cell expression system.

J. Marcinkeviciene, R. Copeland, C. Eckman, 2001, Molecular pharmacology.

Amyloid-β(1–42) Protofibrils Formed in Modified Artificial Cerebrospinal Fluid Bind and Activate Microglia

Geeta S. Paranjape, M. Nichols, Lisa K. Gouwens, 2012, Journal of Neuroimmune Pharmacology.

Amyloid-β Protofibrils Differ from Amyloid-β Aggregates Induced in Dilute Hexafluoroisopropanol in Stability and Morphology*

J. Hoh, T. Rosenberry, M. Moss, 2005, Journal of Biological Chemistry.

Oligomeric amyloid-β(1–42) induces THP-1 human monocyte adhesion and maturation

Maria L. D. Udan, M. Nichols, Deepa Ajit, 2009, Brain Research.

Effect of mesoporous silica nanoparticles loaded with α-tomatine on HepG2 cancer cells studied in vitro

K. Stine, Jay K. Bhattarai, Bishal Nepal, 2023, Journal of Drug Delivery Science and Technology.

Biophysical comparison of soluble amyloid-β(1-42) protofibrils, oligomers, and protofilaments.

Michael R Nichols, Benjamin A Colvin, Elizabeth A Hood, 2015, Biochemistry.

Growth of β-amyloid(1-40) protofibrils by monomer elongation and lateral association. Characterization of distinct products by light scattering and atomic force microscopy

J. Hoh, Wen‐lang Lin, R. Mukhopadhyay, 2002 .

The peptide KLVFF-K(6) promotes beta-amyloid(1-40) protofibril growth by association but does not alter protofibril effects on cellular reduction of 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT).

J. Hoh, T. Rosenberry, M. Moss, 2003, Molecular pharmacology.

Amyloid‐β aggregates formed at polar–nonpolar interfaces differ from amyloid‐β protofibrils produced in aqueous buffers

J. Hoh, T. Rosenberry, M. Moss, 2005 .

Amyloid-beta aggregates formed at polar-nonpolar interfaces differ from amyloid-beta protofibrils produced in aqueous buffers.

J. Hoh, T. Rosenberry, M. Moss, 2005, Microscopy research and technique (Print).

Amyloid-beta protofibrils differ from amyloid-beta aggregates induced in dilute hexafluoroisopropanol in stability and morphology.

J. Hoh, T. Rosenberry, M. Moss, 2005, The Journal of biological chemistry.

Nordihydroguaiaretic acid does not disaggregate beta-amyloid(1-40) protofibrils but does inhibit growth arising from direct protofibril association.

T. Rosenberry, Nicholas H. Varvel, M. Moss, 2004, Molecular pharmacology.

A new class of monoclonal Aβ antibodies selectively targets and triggers deposition of Aβ protofibrils

Nyasha J. Makoni, Kunhua Chen, Evan C. Garrad, 2023, Journal of neurochemistry.

The conformational epitope for a new Aβ42 protofibril‐selective antibody partially overlaps with the peptide N‐terminal region

Joshua A. Kulas, C. Combs, Benjamin A Colvin, 2017, Journal of neurochemistry.

Amyloid-β(1–42) Protofibrils Formed in Modified Artificial Cerebrospinal Fluid Bind and Activate Microglia

Geeta S. Paranjape, M. Nichols, Lisa K. Gouwens, 2013, Journal of Neuroimmune Pharmacology.

Isolated amyloid-β(1-42) protofibrils, but not isolated fibrils, are robust stimulators of microglia.

David C Osborn, Geeta S. Paranjape, M. Nichols, 2012, ACS chemical neuroscience.

Substituted tryptophans at amyloid-β(1-40) residues 19 and 20 experience different environments after fibril formation.

F. Gallazzi, Geeta S. Paranjape, M. Nichols, 2011, Archives of biochemistry and biophysics.

Probing the amyloid-beta(1-40) fibril environment with substituted tryptophan residues.

F. Gallazzi, J. Touchette, M. Nichols, 2010, Archives of biochemistry and biophysics.

Rapid Assembly of Amyloid-β Peptide at a Liquid/Liquid Interface Produces Unstable β-Sheet Fibers†

J. Hoh, T. Rosenberry, M. Moss, 2005 .

Stability of early-stage amyloid-β(1-42) aggregation species.

Geeta S. Paranjape, M. Nichols, Sanjib Karki, 2013, Biochimica et biophysica acta.

Rapid assembly of amyloid-beta peptide at a liquid/liquid interface produces unstable beta-sheet fibers.

J. Hoh, T. Rosenberry, M. Moss, 2005, Biochemistry.

A comparative first-principles study of structural and electronic properties among memantine, amantadine and rimantadine

Kirsten A. Middleton, T. George, M. Nichols, 2012 .

Antisense Evidence for Nuclear Factor-κB–Dependent Embryopathies Initiated by Phenytoin-Enhanced Oxidative Stress

P. G. Wells, K. Ha, J. Im, 2004 .

Tyrosine kinase-independent inhibition of cyclic-AMP phosphodiesterase by genistein and tyrphostin 51.

B. H. Morimoto, M. Nichols, Michael R. Nichols, 1999, Archives of biochemistry and biophysics.

The influence of gold surface texture on microglia morphology and activation.

K. Stine, Y. Tan, Geeta S. Paranjape, 2014, Biomaterials science.