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Biochemistry|November 8, 2008
Structures of rat and human islet amyloid polypeptide IAPP(1-19) in micelles by NMR spectroscopyRavi Prakash Reddy Nanga, Jeffrey R Brender, Jiadi Xu, et al.The Journal of Physical Chemistry Letters|August 15, 2015
In Search of Aggregation Pathways of IAPP and Other Amyloidogenic Proteins: Finding Answers through NMR SpectroscopyHiren R Patel, Amit S Pithadia, Jeffrey R Brender, et al.Biochimica Et Biophysica Acta|July 31, 2007
Membrane fragmentation by an amyloidogenic fragment of human Islet Amyloid Polypeptide detected by solid-state NMR spectroscopy of membrane nanotubesJeffrey R Brender, Ulrich H N Dürr, Deborah Heyl, et al.Cancer Research|April 10, 2021
Multimodal Molecular Imaging Detects Early Responses to Immune Checkpoint BlockadeYu Saida, Jeffrey R Brender, Kazutoshi Yamamoto, et al.Journal of the American Chemical Society|May 22, 2009
Three-dimensional structure and orientation of rat islet amyloid polypeptide protein in a membrane environment by solution NMR spectroscopyRavi Prakash Reddy Nanga, Jeffrey R Brender, Jiadi Xu, et al.Biochemistry|April 18, 2013
Lipid composition-dependent membrane fragmentation and pore-forming mechanisms of membrane disruption by pexiganan (MSI-78)Dong-Kuk Lee, Jeffrey R Brender, Michele F M Sciacca, et al.Journal of the American Chemical Society|March 5, 2009
Determining the effects of lipophilic drugs on membrane structure by solid-state NMR spectroscopy: the case of the antioxidant curcuminJeffrey Barry, Michelle Fritz, Jeffrey R Brender, et al.Journal of the American Chemical Society|May 1, 2008
Amyloid fiber formation and membrane disruption are separate processes localized in two distinct regions of IAPP, the type-2-diabetes-related peptideJeffrey R Brender, Edgar L Lee, Marchello A Cavitt, et al.Biophysical Journal|November 4, 2009
Helical conformation of the SEVI precursor peptide PAP248-286, a dramatic enhancer of HIV infectivity, promotes lipid aggregation and fusionJeffrey R Brender, Kevin Hartman, Lindsey M Gottler, et al.Biochimica Et Biophysica Acta|January 26, 2011
The amyloidogenic SEVI precursor, PAP248-286, is highly unfolded in solution despite an underlying helical tendencyJeffrey R Brender, Ravi Prakash Reddy Nanga, Nataliya Popovych, et al.Pageof 10