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Chemistry

D-Index
79
Citations
19041
World Ranking
3690
National Ranking
1183

Overview

Daniel P. Raleigh is affiliated with Stony Brook University in the United States. Their research primarily spans the fields of Biochemistry, Genetics and Molecular Biology, and Medicine, with notable contributions to Molecular Biology, Physiology, Materials Chemistry, Surgery, and Cell Biology as subfields of study.

The main topics addressed in their work include Alzheimer's disease research and treatments, Protein Structure and Dynamics, Enzyme Structure and Function, Pancreatic function and diabetes, Endoplasmic Reticulum Stress and Disease, Drug Transport and Resistance Mechanisms, and Supramolecular Self-Assembly in Materials.

Frequent coauthors collaborating with Daniel P. Raleigh include Alexander Zhyvoloup, Lakshan Manathunga, Erwin London, Junjie Zou, and Konstantinos Thalassinos.

Their recent papers illustrate the breadth of their research interests and contributions. These include:

  • "Cyclic Ion Mobility-Collision Activation Experiments Elucidate Protein Behavior in the Gas Phase" (2021), published in the Journal of the American Society for Mass Spectrometry
  • "Islet amyloid polypeptide aggregation exerts cytotoxic and proinflammatory effects on the islet vasculature in mice" (2022), published in Diabetologia
  • "Analysis of Baboon IAPP Provides Insight into Amyloidogenicity and Cytotoxicity of Human IAPP" (2020), published in Biophysical Journal
  • "Analysis of Proline Substitutions Reveals the Plasticity and Sequence Sensitivity of Human IAPP Amyloidogenicity and Toxicity" (2020), published in Biochemistry
  • "Protein unfolded states populated at high and ambient pressure are similarly compact" (2021), published in Biophysical Journal

Daniel P. Raleigh's work regularly appears in journals such as Biochemistry, Biophysical Journal, Biophysical Chemistry, Diabetologia, and the Journal of the American Society for Mass Spectrometry.

Best Publications

  • Rotational resonance in solid state NMR

    D.P. Raleigh;M.H. Levitt;R.G. Griffin

  • Theory and simulations of homonuclear spin pair systems in rotating solids

    M. H. Levitt;D. P. Raleigh;F. Creuzet;R. G. Griffin

  • Histone H2B ubiquitylation disrupts local and higher-order chromatin compaction

    Beat Fierz;Champak Chatterjee;Champak Chatterjee;Robert K McGinty;Maya Bar-Dagan

  • De novo design of helical bundles as models for understanding protein folding and function.

    R B Hill;D P Raleigh;A Lombardi;W F DeGrado

  • The Flavanol (−)-Epigallocatechin 3-Gallate Inhibits Amyloid Formation by Islet Amyloid Polypeptide, Disaggregates Amyloid Fibrils and Protects Cultured Cells Against IAPP Induced Toxicity

    Fanling Meng;Andisheh Abedini;Annette Plesner;C. Bruce Verchere

  • Two-dimensional IR spectroscopy and isotope labeling defines the pathway of amyloid formation with residue-specific resolution

    Sang Hee Shim;Ruchi Gupta;Yun L. Ling;David B. Strasfeld

  • Screening and classifying small-molecule inhibitors of amyloid formation using ion mobility spectrometry-mass spectrometry

    Lydia M. Young;Janet C. Saunders;Rachel A. Mahood;Charlotte H. Revill

  • Mechanism of IAPP amyloid fibril formation involves an intermediate with a transient β-sheet

    Lauren E. Buchanan;Emily B. Dunkelberger;Huong Q. Tran;Pin Nan Cheng

  • Rational modification of protein stability by the mutation of charged surface residues.

    Shari Spector;Minghui Wang;Stefan A. Carp;James Robblee

  • Islet Amyloid Polypeptide: Structure, Function, and Pathophysiology.

    Rehana Akter;Ping Cao;Harris Noor;Zachary Ridgway

  • Protein folding: defining a "standard" set of experimental conditions and a preliminary kinetic data set of two-state proteins.

    Karen L. Maxwell;David Wildes;Arash Zarrine-Afsar;Miguel A. De Los Rios

  • A role for helical intermediates in amyloid formation by natively unfolded polypeptides

    Andisheh Abedini;Daniel P Raleigh

  • Effects of Sequential Proline Substitutions on Amyloid Formation by Human Amylin20-29†

    Daniel F. Moriarty;Daniel P. Raleigh

  • A critical assessment of the role of helical intermediates in amyloid formation by natively unfolded proteins and polypeptides

    Andisheh Abedini;Daniel P. Raleigh

  • Analysis of amylin cleavage products provides new insights into the amyloidogenic region of human amylin.

    Melanie R Nilsson;Daniel P Raleigh

  • Two-dimensional infrared spectroscopy reveals the complex behaviour of an amyloid fibril inhibitor

    Chris T. Middleton;Peter Marek;Ping Cao;Chi Cheng Chiu

  • Ion mobility spectrometry-mass spectrometry defines the oligomeric intermediates in amylin amyloid formation and the mode of action of inhibitors.

    Lydia M. Young;Ping Cao;Daniel P. Raleigh;Alison E. Ashcroft

  • De novo protein design: from molten globules to native-like states

    Stephen F. Betz;Daniel P. Raleigh;William F. DeGrado

  • A single-point mutation converts the highly amyloidogenic human islet amyloid polypeptide into a potent fibrillization inhibitor

    Andisheh Abedini;Fanling Meng;Daniel P Raleigh

  • The role of His-18 in amyloid formation by human islet amyloid polypeptide.

    Andisheh Abedini;Daniel P Raleigh

  • De novo Design of Helical Bundles as Models for Understanding Protein Folding and Function

    R. Blake Hill;Daniel P. Raleigh;Angela Lombardi;William F. Degrado

Frequent Co-Authors

Martin T. Zanni
Martin T. Zanni University of Wisconsin–Madison
Ann Marie Schmidt
Ann Marie Schmidt New York University
Robert Fairman
Robert Fairman Haverford College
Brian Kuhlman
Brian Kuhlman University of North Carolina at Chapel Hill
William F. DeGrado
William F. DeGrado University of California, San Francisco
R. Brian Dyer
R. Brian Dyer Emory University
Sheena E. Radford
Sheena E. Radford University of Leeds
Malcolm H. Levitt
Malcolm H. Levitt University of Southampton
Tom W. Muir
Tom W. Muir Princeton University

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