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Sep 25, 2024 | 
pubs.acs.org | James Griffin |Michael J. Ferracane |Adam G Kreutzer |Jeramiah Small
This publication is Open Access under the license indicated. Learn MoreAddition/CorrectionSeptember 25, 2024*The Journal of Organic ChemistryCite this: J. Org. Chem. 2024, XXXX, XXXClick to copy citationCitation copied!correction. This publication is licensed under CC-BY-NC-ND 4.0 . You are free to share (copy and redistribute) this article in any medium or format within the parameters below:Creative Commons (CC): This is a Creative Commons license.
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Sep 25, 2024 | 
dx.doi.org | James Griffin |Michael J. Ferracane |Adam G Kreutzer |Jeramiah Small
This publication is Open Access under the license indicated. Learn MoreAddition/CorrectionSeptember 25, 2024*The Journal of Organic ChemistryCite this: J. Org. Chem. 2024, XXXX, XXXClick to copy citationCitation copied!correction. This publication is licensed under CC-BY-NC-ND 4.0 . You are free to share (copy and redistribute) this article in any medium or format within the parameters below:Creative Commons (CC): This is a Creative Commons license.
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Dec 8, 2023 | 
pubs.rsc.org | Tuan D. Samdin |Chelsea Jones |Gretchen Guaglianone |Adam G Kreutzer
A β-barrel-like tetramer formed by a β-hairpin derived from Aβ†
β-Hairpins formed by the β-amyloid peptide Aβ are building blocks of Aβ oligomers. Three different alignments of β-hairpins have been observed in the structures of Aβ oligomers or fibrils. Differences in β-hairpin alignment likely contribute to the heterogeneity of Aβ oligomers and thus impede their study at high-resolution.
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Nov 28, 2023 | 
pubs.rsc.org | Chelsea Jones |Gretchen Guaglianone |Adam G Kreutzer |Tuan Dilshad Samdin
A β-Barrel-Like Tetramer Formed by a β-Hairpin Derived From Aβ
β-Hairpins formed by the β-amyloid peptide Aβ are building blocks of Aβ oligomers. Three different alignments of β-hairpins have been observed in the structures of Aβ oligomers or fibrils. Differences in β-hairpin alignment likely contribute to the heterogeneity of Aβ oligomers and thus impede their study at high-resolution.
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Nov 13, 2023 | 
dx.doi.org | Hyunjun Yang |Adam G Kreutzer |James S Nowick |K. Ashley
Download Hi-Res ImageDownload to MS-PowerPointCite This:J. Org. Chem. 2024, XXXX, XXXRETURN TO ARTICLES ASAPPREVNoteNEXTHyunjun YangDepartment of Chemistry, University of California Irvine, Irvine, California 92697, United States, , and *James S. NowickDepartment of Chemistry, University of California Irvine, Irvine, California 92697, United StatesDepartment of Pharmaceutical Sciences, University of California Irvine, Irvine, California 92697, United States*Email: [email protected] this: J. Org.
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Nov 13, 2023 | 
pubs.acs.org | Hyunjun Yang |Adam G Kreutzer |James S Nowick |K. Ashley
Download Hi-Res ImageDownload to MS-PowerPointCite This:J. Org. Chem. 2024, XXXX, XXXHyunjun YangDepartment of Chemistry, University of California Irvine, Irvine, California 92697, United States, , and *James S. NowickDepartment of Chemistry, University of California Irvine, Irvine, California 92697, United StatesDepartment of Pharmaceutical Sciences, University of California Irvine, Irvine, California 92697, United States*Email: [email protected] this: J. Org. Chem. 2024, XXXX, XXX.
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Nov 1, 2023 | 
biorxiv.org | Hyunjun Yang |Adam G Kreutzer |James S Nowick
AbstractTeixobactin is a potent peptide antibiotic against Gram-positive bacteria that binds to lipid II and related peptidoglycan precursors and disrupts the cell membrane. This paper presents the X-ray crystallographic structure of the N-methylated teixobactin analogue N-Me-D-Gln4,Lys10-teixobactin (1). N-Methylation at position 4 prevents uncontrolled aggregation and enables the crystallization of the teixobactin analogue.
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Sep 18, 2023 | 
onlinelibrary.wiley.com | Adam G Kreutzer |Ryan J. Malonis |Karen Tong |Gretchen Guaglianone
1 INTRODUCTION Understanding the structures of the toxic oligomers formed by the β-amyloid peptide (Aβ) is crucial for unraveling the molecular basis of Alzheimer's disease and for creating better Alzheimer's disease therapies.[1, 2] Elucidating the structures of Aβ oligomers that form in the brain is challenging, because the oligomers are unstable and heterogeneous, constituting a multitude of assemblies that differ in size, stoichiometry, and morphology.[3] Furthermore, isolation of Aβ...
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Sep 11, 2023 | 
frontiersin.org | Pedro Fernandez-Funez |Osamu Onodera |Adam G Kreutzer
IntroductionRecent cryo-electron microscopy (cryo-EM) studies have revealed the accumulation of C-terminal fragments (CTF) (residues 120-254/274) of transmembrane protein 106B (TMEM106B) as amyloid fibrils in the sarkosyl-insoluble fractions of postmortem brain tissue from elderly individuals and patients with neurodegenerative diseases (Chang et al., 2022; Jiang et al., 2022; Schweighauser et al., 2022). Initially, no antibodies were available to detect CTF using immunohistochemistry (IHC).
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May 12, 2023 | 
biorxiv.org | Adam G Kreutzer |Sepehr Haerianardakani |Gretchen Guaglianone |Jennifer Nguyen
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