Noel D. Lazo

4.3k total citations · 1 hit paper
53 papers, 3.6k citations indexed

About

Noel D. Lazo is a scholar working on Molecular Biology, Physiology and Spectroscopy. According to data from OpenAlex, Noel D. Lazo has authored 53 papers receiving a total of 3.6k indexed citations (citations by other indexed papers that have themselves been cited), including 32 papers in Molecular Biology, 30 papers in Physiology and 15 papers in Spectroscopy. Recurrent topics in Noel D. Lazo's work include Alzheimer's disease research and treatments (29 papers), Protein Structure and Dynamics (21 papers) and Supramolecular Self-Assembly in Materials (11 papers). Noel D. Lazo is often cited by papers focused on Alzheimer's disease research and treatments (29 papers), Protein Structure and Dynamics (21 papers) and Supramolecular Self-Assembly in Materials (11 papers). Noel D. Lazo collaborates with scholars based in United States, United Kingdom and Italy. Noel D. Lazo's co-authors include David B. Teplow, Donald T. Downing, Joan–Emma Shea, Summer L. Bernstein, Thomas Wyttenbach, Michael T. Bowers, James F. Haw, Margaret M. Condron, Gal Bitan and Carol V. Robinson and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and Journal of Biological Chemistry.

In The Last Decade

Noel D. Lazo

52 papers receiving 3.5k citations

Hit Papers

align trajectories

What are hit papers?

Hit papers significantly outperform the citation benchmark for their cohort. A paper qualifies if it has ≥500 total citations, achieves ≥1.5× the top-1% citation threshold for papers in the same subfield and year (this is the minimum needed to enter the top 1%, not the average within it), or reaches the top citation threshold in at least one of its specific research topics.

Amyloid-β protein oligomerization and the importance of tetramers and dodecamers in the aetiology of Alzheimer's disease

2009 803 citations Summer L. Bernstein, Nicholas Dupuis et al. Nature Chemistry profile →

Peers

Noel D. Lazo

PHYSI

SPECT

BIOMA

Joseph T. Jarrett United States

Birgit Schiøtt Denmark

Gianni Valensin Italy

Jeffrey Brender United States

Nakul C. Maiti India

Marianna Török United States

Orlando Crescenzi Italy

Elena Gaggelli Italy

Jeffrey Aubé United States

Raimon Sabaté Spain

Joseph T. Jarrett United States

Noel D. Lazo

3.6k ×1.8

3.0k ×1.6

PHYSI

116 ×0.2

SPECT

410 ×0.8

448 ×0.9

BIOMA

Citations per year, relative to Noel D. Lazo Noel D. Lazo (= 1×) peers Joseph T. Jarrett

Countries citing papers authored by Noel D. Lazo

Since Specialization

Citations

This map shows the geographic impact of Noel D. Lazo's research. It shows the number of citations coming from papers published by authors working in each country. You can also color the map by specialization and compare the number of citations received by Noel D. Lazo with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Noel D. Lazo more than expected).

Fields of papers citing papers by Noel D. Lazo

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Noel D. Lazo. Nodes represent research fields, and links connect fields that are likely to share authors. Colored nodes show fields that tend to cite the papers produced by Noel D. Lazo. The network helps show where Noel D. Lazo may publish in the future.

Co-authorship network of co-authors of Noel D. Lazo

This figure shows the co-authorship network connecting the top 25 collaborators of Noel D. Lazo. A scholar is included among the top collaborators of Noel D. Lazo based on the total number of citations received by their joint publications. Widths of edges represent the number of papers authors have co-authored together. Node borders signify the number of papers an author published with Noel D. Lazo. Noel D. Lazo is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

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20 of 20 papers shown

Jakobsche, Charles E., et al.. (2021). Differential Effects of Polyphenols on Insulin Proteolysis by the Insulin-Degrading Enzyme. Antioxidants. 10(9). 1342–1342. 4 indexed citations

Spratt, Donald E., et al.. (2018). Enzyme kinetics from circular dichroism of insulin reveals mechanistic insights into the regulation of insulin-degrading enzyme. Bioscience Reports. 38(6). 8 indexed citations

Sparks, Samuel, Gai Liu, Kevin J. Robbins, & Noel D. Lazo. (2012). Curcumin modulates the self-assembly of the islet amyloid polypeptide by disassembling α-helix. Biochemical and Biophysical Research Communications. 422(4). 551–555. 55 indexed citations

Bernstein, Summer L., Nicholas Dupuis, Noel D. Lazo, et al.. (2009). Amyloid-β protein oligomerization and the importance of tetramers and dodecamers in the aetiology of Alzheimer's disease. Nature Chemistry. 1(4). 326–331. 803 indexed citations breakdown →

Bernstein, Summer L., Andrij Baumketner, Margaret M. Condron, et al.. (2009). Amyloid β-Protein: Experiment and Theory on the 21−30 Fragment. The Journal of Physical Chemistry B. 113(17). 6041–6046. 43 indexed citations

Baumketner, Andrij, Summer L. Bernstein, Thomas Wyttenbach, et al.. (2008). Effects of Familial Alzheimer’s Disease Mutations on the Folding Nucleation of the Amyloid β-Protein. Journal of Molecular Biology. 381(1). 221–228. 90 indexed citations

Maier, Marcel, Timothy J. Seabrook, Noel D. Lazo, et al.. (2006). Short Amyloid-β (Aβ) Immunogens Reduce Cerebral Aβ Load and Learning Deficits in an Alzheimer's Disease Mouse Model in the Absence of an Aβ-Specific Cellular Immune Response. Journal of Neuroscience. 26(18). 4717–4728. 114 indexed citations

Baumketner, Andrij, Summer L. Bernstein, Thomas Wyttenbach, et al.. (2006). Structure of the 21–30 fragment of amyloid β‐protein. Protein Science. 15(6). 1239–1247. 123 indexed citations

Cruz, Luis, Brigita Urbanc, Jose M. Borreguero, et al.. (2005). Solvent and mutation effects on the nucleation of amyloid β-protein folding. Proceedings of the National Academy of Sciences. 102(51). 18258–18263. 99 indexed citations

10.

Lazo, Noel D. & Donald T. Downing. (2001). Effects of Na₂SO₄ on hydrophobic and electrostatic interactions between amphipathic α‐helices. Journal of Peptide Research. 58(6). 457–463. 6 indexed citations

11.

Lazo, Noel D. & Donald T. Downing. (1999). A Mixture of α-Helical and 310-Helical Conformations for Involucrin in the Human Epidermal Corneocyte Envelope Provides a Scaffold for the Attachment of Both Lipids and Proteins. Journal of Biological Chemistry. 274(52). 37340–37344. 15 indexed citations

12.

Lazo, Noel D. & Donald T. Downing. (1999). Fibril formation by amyloid‐β proteins may involve β‐helical protofibrils. Journal of Peptide Research. 53(6). 633–640. 21 indexed citations

13.

Lazo, Noel D. & Donald T. Downing. (1998). Stabilization of amphipathic α‐helical and β‐helical conformations in synthetic peptides in the presence and absence of ionic interactions. Journal of Peptide Research. 51(1). 85–89. 7 indexed citations

14.

Lazo, Noel D. & Donald T. Downing. (1997). β-Helical Fibrils from a Model Peptide. Biochemical and Biophysical Research Communications. 235(3). 675–679. 29 indexed citations

15.

Hu, W., Noel D. Lazo, & Timothy A. Cross. (1995). Tryptophan Dynamics and Structural Refinement in a Lipid Bilayer Environment: Solid State NMR of the Gramicidin Channel. Biochemistry. 34(43). 14138–14146. 66 indexed citations

16.

Lazo, Noel D., W. Hu, & Timothy A. Cross. (1995). Low-Temperature Solid-State 15N NMR Characterization of Polypeptide Backbone Librations. Journal of Magnetic Resonance Series B. 107(1). 43–50. 31 indexed citations

17.

Lazo, Noel D., J Meine, & Donald T. Downing. (1995). Lipids Are Covalently Attached to Rigid Corneocyte Protein Envelopes Existing Predominantly as β-Sheets: A Solid-State Nuclear Magnetic Resonance Study. Journal of Investigative Dermatology. 105(2). 296–300. 37 indexed citations

18.

Lazo, Noel D., et al.. (1993). Rapidly Frozen Polypeptide Samples for Characterization of High-Definition Dynamics by Solid-State NMR Spectroscopy. Biochemical and Biophysical Research Communications. 197(2). 904–909. 17 indexed citations

19.

Lazo, Noel D., et al.. (1992). In situ carbon-13 solid-state NMR study of the Cu/ZnO/Al2O3 methanol synthesis catalyst. Journal of the American Chemical Society. 114(22). 8552–8559. 53 indexed citations

20.

Haw, James F., et al.. (1989). Reactions of propene on zeolite HY catalyst studied by in situ variable temperature solid-state nuclear magnetic resonance spectroscopy. Journal of the American Chemical Society. 111(6). 2052–2058. 245 indexed citations

Rankless uses publication and citation data sourced from OpenAlex, an open and comprehensive bibliographic database. While OpenAlex provides broad and valuable coverage of the global research landscape, it—like all bibliographic datasets—has inherent limitations. These include incomplete records, variations in author disambiguation, differences in journal indexing, and delays in data updates. As a result, some metrics and network relationships displayed in Rankless may not fully capture the entirety of a scholar's output or impact.

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