| Year |
Citation |
Score |
| 2024 |
Hirschbeck SS, Lindberg ET, Jang JH, Jacob MR, Lazar Cantrell KL, Do TD. Investigating a Novel Neurodegenerative Disease Toxic Mechanism Involving Lipid Binding Specificity of Amyloid Oligomers. Acs Chemical Neuroscience. PMID 38488720 DOI: 10.1021/acschemneuro.3c00830 |
0.369 |
|
| 2023 |
Long CC, Antevska A, Mast DH, Okyem S, Sweedler JV, Do TD. Nonenzymatic Posttranslational Modifications and Peptide Cleavages Observed in Peptide Epimers. Journal of the American Society For Mass Spectrometry. PMID 37102735 DOI: 10.1021/jasms.3c00092 |
0.511 |
|
| 2023 |
Gray ALH, Norman V, Oluwatoba DS, Prosser RA, Do TD. Potential Protective Function of Aβ Monomer on Tauopathies. Journal of the American Society For Mass Spectrometry. PMID 36693165 DOI: 10.1021/jasms.2c00343 |
0.35 |
|
| 2021 |
Sade Yazdi D, Laor Bar-Yosef D, Adsi H, Kreiser T, Sigal S, Bera S, Zaguri D, Shaham-Niv S, Oluwatoba DS, Levy D, Gartner M, Do TD, Frenkel D, Gazit E. Homocysteine fibrillar assemblies display cross-talk with Alzheimer's disease β-amyloid polypeptide. Proceedings of the National Academy of Sciences of the United States of America. 118. PMID 34099562 DOI: 10.1073/pnas.2017575118 |
0.325 |
|
| 2020 |
Gray ALH, Antevska A, Oluwatoba DS, Schonfeld G, Lazar Cantrell KL, Do TD. Cytotoxicity of α-Helical, Staphylococcus Aureus PSMα3 Investigated by Post Ion-Mobility Dissociation Mass Spectrometry. Analytical Chemistry. PMID 32786488 DOI: 10.1021/acs.analchem.0c01974 |
0.387 |
|
| 2019 |
Laos V, Do TD, Bishop D, Jin Y, Marsh NM, Quon B, Fetters M, Cantrell KL, Buratto SK, Bowers MT. Characterizing TDP-43(307-319) Oligomeric Assembly : Mechanistic and Structural Implications Involved in the Etiology of Amyotrophic Lateral Sclerosis. Acs Chemical Neuroscience. PMID 31430111 DOI: 10.1021/Acschemneuro.9B00337 |
0.558 |
|
| 2018 |
Neumann EK, Do TD, Comi TJ, Sweedler J. Exploring the Fundamental Structures of Life: Non-targeted, Chemical Analysis of Single Cells and Subcellular Structures. Angewandte Chemie (International Ed. in English). PMID 30500998 DOI: 10.1002/Anie.201811951 |
0.671 |
|
| 2018 |
Do TD, Checco JW, Tro M, Shea JE, Bowers MT, Sweedler JV. Conformational investigation of the structure-activity relationship of GdFFD and its analogues on an achatin-like neuropeptide receptor of Aplysia californica involved in the feeding circuit. Physical Chemistry Chemical Physics : Pccp. PMID 30112548 DOI: 10.1039/C8Cp03661F |
0.71 |
|
| 2018 |
Do TD, Ellis JF, Neumann EK, Comi TJ, Tillmaand EG, Lenhart AE, Rubakhin SS, Sweedler J. Optically Guided Single Cell Mass Spectrometry of Rat Dorsal Root Ganglia to Profile Lipids, Peptides and Proteins. Chemphyschem : a European Journal of Chemical Physics and Physical Chemistry. PMID 29544029 DOI: 10.1002/Cphc.201701364 |
0.701 |
|
| 2018 |
Do TD, Sangwan S, de Almeida NEC, Ilitchev AI, Giammona M, Sawaya MR, Buratto SK, Eisenberg DS, Bowers MT. Distal Amyloid β-Protein Fragments Template Amyloid Assembly. Protein Science : a Publication of the Protein Society. PMID 29349888 DOI: 10.1002/Pro.3375 |
0.585 |
|
| 2017 |
de Almeida NEC, Do TD, LaPointe NE, Tro M, Feinstein SC, Shea JE, Bowers MT. 1,2,3,4,6-penta-O-galloyl-β-D-glucopyranose Binds to the N-terminal Metal Binding Region to Inhibit Amyloid β-protein Oligomer and Fibril Formation. International Journal of Mass Spectrometry. 420: 24-34. PMID 29056865 DOI: 10.1016/J.Ijms.2016.09.018 |
0.548 |
|
| 2017 |
Sangwan S, Zhao A, Adams KL, Jayson CK, Sawaya MR, Guenther EL, Pan AC, Ngo J, Moore DM, Soriaga AB, Do TD, Goldschmidt L, Nelson R, Bowers MT, Koehler CM, et al. Atomic structure of a toxic, oligomeric segment of SOD1 linked to amyotrophic lateral sclerosis (ALS). Proceedings of the National Academy of Sciences of the United States of America. PMID 28760994 DOI: 10.1073/Pnas.1705091114 |
0.466 |
|
| 2017 |
Comi TJ, Neumann EK, Do TD, Sweedler JV. microMS: A Python Platform for Image-Guided Mass Spectrometry Profiling. Journal of the American Society For Mass Spectrometry. PMID 28593377 DOI: 10.1007/S13361-017-1704-1 |
0.668 |
|
| 2017 |
Do TD, Comi TJ, Dunham SJ, Rubakhin SS, Sweedler JV. Single Cell Profiling Using Ionic Liquid Matrix-Enhanced Secondary Ion Mass Spectrometry for Neuronal Cell Type Differentiation. Analytical Chemistry. PMID 28194949 DOI: 10.1021/Acs.Analchem.6B04819 |
0.419 |
|
| 2017 |
Comi TJ, Do TD, Rubakhin SS, Sweedler JV. Categorizing Cells based on their Chemical Profiles: Progress in Single Cell Mass Spectrometry. Journal of the American Chemical Society. PMID 28135079 DOI: 10.1021/Jacs.6B12822 |
0.426 |
|
| 2016 |
Kim B, Do TD, Hayden EY, Teplow DB, Bowers MT, Shea JE. Aggregation of Chameleon Peptides: Implications of α-Helicity in Fibril Formation. The Journal of Physical Chemistry. B. PMID 27001160 DOI: 10.1021/Acs.Jpcb.6B00830 |
0.521 |
|
| 2016 |
Feinstein HE, Benbow SJ, LaPointe NE, Patel N, Ramachandran S, Do TD, Gaylord MR, Huskey NE, Dressler N, Korff M, Quon B, Cantrell KL, Bowers MT, Lal R, Feinstein SC. Oligomerization of the Microtubule Associated Protein Tau is Mediated by its N-Terminal Sequences: Implications for Normal and Pathological Tau Action. Journal of Neurochemistry. PMID 26953146 DOI: 10.1111/Jnc.13604 |
0.489 |
|
| 2016 |
Ilitchev AI, Giammona MJ, Do TD, Wong AG, Buratto SK, Shea JE, Raleigh DP, Bowers MT. Human Islet Amyloid Polypeptide N-Terminus Fragment Self-Assembly: Effect of Conserved Disulfide Bond on Aggregation Propensity. Journal of the American Society For Mass Spectrometry. PMID 26894887 DOI: 10.1007/S13361-016-1347-7 |
0.545 |
|
| 2016 |
Economou NJ, Giammona MJ, Do TD, Zheng X, Teplow DB, Buratto SK, Bowers MT. Amyloid β-protein assembly and Alzheimer's disease: Dodecamers of Aβ42, but not of Aβ40, seed fibril formation. Journal of the American Chemical Society. PMID 26839237 DOI: 10.1021/Jacs.5B11913 |
0.715 |
|
| 2015 |
Do TD, LaPointe NE, Nelson R, Krotee P, Hayden EY, Ulrich B, Quan S, Feinstein SC, Teplow DB, Eisenberg D, Shea JE, Bowers MT. Amyloid β-Protein C-terminal Fragments: Formation of Cylindrins and β-barrels. Journal of the American Chemical Society. PMID 26700445 DOI: 10.1021/Jacs.5B09536 |
0.548 |
|
| 2015 |
Do TD, de Almeida NE, Lapointe NE, Chamas A, Feinstein SC, Bowers MT. Amino Acid Metaclusters: Implications of Growth Trends on Peptide Self-Assembly and Structure. Analytical Chemistry. PMID 26632663 DOI: 10.1021/Acs.Analchem.5B03454 |
0.506 |
|
| 2015 |
de Almeida NE, Do TD, Tro M, LaPointe NE, Feinstein SC, Shea JE, Bowers MT. Opposing Effects of Cucurbit[7]uril and 1,2,3,4,6-penta-O-galloyl-β-D-glucopyranose on Amyloid β25-35 Assembly. Acs Chemical Neuroscience. PMID 26629788 DOI: 10.1021/Acschemneuro.5B00280 |
0.536 |
|
| 2015 |
Eschmann NA, Do TD, LaPointe NE, Shea JE, Feinstein SC, Bowers MT, Han S. Tau Aggregation Propensity Engrained in Its Solution State. The Journal of Physical Chemistry. B. PMID 26484390 DOI: 10.1021/Acs.Jpcb.5B08092 |
0.557 |
|
| 2015 |
Do TD, Kincannon WM, Bowers MT. Phenylalanine Oligomers and Fibrils: The Mechanism of Assembly and the Importance of Tetramers and Counterions. Journal of the American Chemical Society. 137: 10080-3. PMID 26244895 DOI: 10.1021/Jacs.5B05482 |
0.506 |
|
| 2015 |
Do TD, Chamas A, Zheng X, Barnes A, Chang D, Veldstra T, Takhar H, Dressler N, Trapp B, Miller K, McMahon A, Meredith SC, Shea JE, Lazar Cantrell K, Bowers MT. Elucidation of the Aggregation Pathways of Helix-Turn-Helix Peptides: Stabilization at the Turn Region Is Critical for Fibril Formation. Biochemistry. PMID 26070092 DOI: 10.1021/Acs.Biochem.5B00414 |
0.733 |
|
| 2015 |
Do TD, Bowers MT. Diphenylalanine self assembly: novel ion mobility methods showing the essential role of water. Analytical Chemistry. 87: 4245-52. PMID 25785477 DOI: 10.1021/Ac5046774 |
0.429 |
|
| 2015 |
Ganguly P, Do TD, Larini L, LaPointe NE, Sercel AJ, Shade MF, Feinstein SC, Bowers MT, Shea JE. Tau assembly: the dominant role of PHF6 (VQIVYK) in microtubule binding region repeat R3. The Journal of Physical Chemistry. B. 119: 4582-93. PMID 25775228 DOI: 10.1021/Acs.Jpcb.5B00175 |
0.445 |
|
| 2014 |
Do TD, Economou NJ, Chamas A, Buratto SK, Shea JE, Bowers MT. Interactions between amyloid-β and Tau fragments promote aberrant aggregates: implications for amyloid toxicity. The Journal of Physical Chemistry. B. 118: 11220-30. PMID 25153942 DOI: 10.1021/Jp506258G |
0.574 |
|
| 2014 |
Do TD, LaPointe NE, Sangwan S, Teplow DB, Feinstein SC, Sawaya MR, Eisenberg DS, Bowers MT. Factors that drive peptide assembly from native to amyloid structures: experimental and theoretical analysis of [leu-5]-enkephalin mutants. The Journal of Physical Chemistry. B. 118: 7247-56. PMID 24915112 DOI: 10.1021/Jp502473S |
0.611 |
|
| 2013 |
Bleiholder C, Do TD, Wu C, Economou NJ, Bernstein SS, Buratto SK, Shea JE, Bowers MT. Ion mobility spectrometry reveals the mechanism of amyloid formation of Aβ(25-35) and its modulation by inhibitors at the molecular level: epigallocatechin gallate and scyllo-inositol. Journal of the American Chemical Society. 135: 16926-37. PMID 24131107 DOI: 10.1021/Ja406197F |
0.57 |
|
| 2013 |
Do TD, LaPointe NE, Economou NJ, Buratto SK, Feinstein SC, Shea JE, Bowers MT. Effects of pH and charge state on peptide assembly: the YVIFL model system. The Journal of Physical Chemistry. B. 117: 10759-68. PMID 23937333 DOI: 10.1021/Jp406066D |
0.571 |
|
| 2013 |
Do TD, Economou NJ, LaPointe NE, Kincannon WM, Bleiholder C, Feinstein SC, Teplow DB, Buratto SK, Bowers MT. Factors that drive peptide assembly and fibril formation: experimental and theoretical analysis of Sup35 NNQQNY mutants. The Journal of Physical Chemistry. B. 117: 8436-46. PMID 23802812 DOI: 10.1021/Jp4046287 |
0.595 |
|
| 2013 |
Larini L, Gessel MM, LaPointe NE, Do TD, Bowers MT, Feinstein SC, Shea JE. Initiation of assembly of tau(273-284) and its ΔK280 mutant: an experimental and computational study. Physical Chemistry Chemical Physics : Pccp. 15: 8916-28. PMID 23515417 DOI: 10.1039/C3Cp00063J |
0.74 |
|
| 2013 |
Bleiholder C, Contreras S, Do TD, Bowers MT. A novel projection approximation algorithm for the fast and accurate computation of molecular collision cross sections (II). Model parameterization and definition of empirical shape factors for proteins International Journal of Mass Spectrometry. 345: 89-96. DOI: 10.1016/J.Ijms.2012.08.027 |
0.349 |
|
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