PDB 4e1h citation summary ‹ Protein Data Bank in Europe (PDBe)

Crystal structure of a human prion protein fragment reveals a motif for oligomer formation. Apostol MI, Perry K, Surewicz WK. J Am Chem Soc 135 10202-10205 (2013)
The dipeptidyl peptidase IV inhibitors vildagliptin and K-579 inhibit a phospholipase C: a case of promiscuous scaffolds in proteins. Chakraborty S, Rendón-Ramírez A, Ásgeirsson B, Dutta M, Ghosh AS, Oda M, Venkatramani R, Rao BJ, Dandekar AM, Goñi FM. F1000Res 2 286 (2013)

Structural, morphological, and functional diversity of amyloid oligomers. Breydo L, Uversky VN. FEBS Lett 589 2640-2648 (2015)
Elucidating the Structures of Amyloid Oligomers with Macrocyclic β-Hairpin Peptides: Insights into Alzheimer's Disease and Other Amyloid Diseases. Kreutzer AG, Nowick JS. Acc Chem Res 51 706-718 (2018)
An Account of Amyloid Oligomers: Facts and Figures Obtained from Experiments and Simulations. Nagel-Steger L, Owen MC, Strodel B. Chembiochem 17 657-676 (2016)
Ion mobility-mass spectrometry and orthogonal gas-phase techniques to study amyloid formation and inhibition. Hoffmann W, von Helden G, Pagel K. Curr Opin Struct Biol 46 7-15 (2017)
Exploring amyloid oligomers with peptide model systems. Samdin TD, Kreutzer AG, Nowick JS. Curr Opin Chem Biol 64 106-115 (2021)
Toward the Atomic Structure of PrP^Sc. Rodriguez JA, Jiang L, Eisenberg DS. Cold Spring Harb Perspect Biol 9 a031336 (2017)
Structural mechanisms of oligomer and amyloid fibril formation by the prion protein. Sengupta I, Udgaonkar JB. Chem Commun (Camb) 54 6230-6242 (2018)
Neurodegenerative disorders: dysregulation of a carefully maintained balance? Swart C, Haylett W, Kinnear C, Johnson G, Bardien S, Loos B. Exp Gerontol 58 279-291 (2014)
Amyloid oligomers as on-pathway precursors or off-pathway competitors of fibrils. Muschol M, Hoyer W. Front Mol Biosci 10 1120416 (2023)

The Biological Function of the Prion Protein: A Cell Surface Scaffold of Signaling Modules. Linden R. Front Mol Neurosci 10 77 (2017)
X-ray crystallographic structures of trimers and higher-order oligomeric assemblies of a peptide derived from Aβ(17-36). Spencer RK, Li H, Nowick JS. J Am Chem Soc 136 5595-5598 (2014)
Amyloid β-Protein C-Terminal Fragments: Formation of Cylindrins and β-Barrels. Do TD, LaPointe NE, Nelson R, Krotee P, Hayden EY, Ulrich B, Quan S, Feinstein SC, Teplow DB, Eisenberg D, Shea JE, Bowers MT. J Am Chem Soc 138 549-557 (2016)
Stable, metastable, and kinetically trapped amyloid aggregate phases. Miti T, Mulaj M, Schmit JD, Muschol M. Biomacromolecules 16 326-335 (2015)
Origin of metastable oligomers and their effects on amyloid fibril self-assembly. Hasecke F, Miti T, Perez C, Barton J, Schölzel D, Gremer L, Grüning CSR, Matthews G, Meisl G, Knowles TPJ, Knowles TPJ, Willbold D, Neudecker P, Heise H, Ullah G, Hoyer W, Muschol M. Chem Sci 9 5937-5948 (2018)
X-ray Crystallographic Structure of Oligomers Formed by a Toxic β-Hairpin Derived from α-Synuclein: Trimers and Higher-Order Oligomers. Salveson PJ, Spencer RK, Nowick JS. J Am Chem Soc 138 4458-4467 (2016)
Structural mapping of oligomeric intermediates in an amyloid assembly pathway. Karamanos TK, Jackson MP, Calabrese AN, Goodchild SC, Cawood EE, Thompson GS, Kalverda AP, Hewitt EW, Radford SE. Elife 8 e46574 (2019)
Structures of oligomers of a peptide from β-amyloid. Pham JD, Chim N, Goulding CW, Nowick JS. J Am Chem Soc 135 12460-12467 (2013)
X-ray Crystallographic Structures of Oligomers of Peptides Derived from β2-Microglobulin. Spencer RK, Kreutzer AG, Salveson PJ, Li H, Nowick JS. J Am Chem Soc 137 6304-6311 (2015)
Polymorphism of oligomers of a peptide from β-amyloid. Pham JD, Demeler B, Nowick JS. J Am Chem Soc 136 5432-5442 (2014)
A Hexamer of a Peptide Derived from Aβ_16-36. Kreutzer AG, Spencer RK, McKnelly KJ, Yoo S, Hamza IL, Salveson PJ, Nowick JS. Biochemistry 56 6061-6071 (2017)
Amyloid oligomers and protofibrils, but not filaments, self-replicate from native lysozyme. Mulaj M, Foley J, Muschol M. J Am Chem Soc 136 8947-8956 (2014)
Crystal Structure of the DFNKF Segment of Human Calcitonin Unveils Aromatic Interactions between Phenylalanines. Bertolani A, Pizzi A, Pirrie L, Gazzera L, Morra G, Meli M, Colombo G, Genoni A, Cavallo G, Terraneo G, Metrangolo P. Chemistry 23 2051-2058 (2017)
Cyclic peptides as inhibitors of amyloid fibrillation. Luo J, Abrahams JP. Chemistry 20 2410-2419 (2014)
Factors that drive peptide assembly from native to amyloid structures: experimental and theoretical analysis of [leu-5]-enkephalin mutants. Do TD, LaPointe NE, Sangwan S, Teplow DB, Feinstein SC, Sawaya MR, Eisenberg DS, Bowers MT. J Phys Chem B 118 7247-7256 (2014)
Structural basis for the complete resistance of the human prion protein mutant G127V to prion disease. Zheng Z, Zhang M, Wang Y, Ma R, Guo C, Feng L, Wu J, Yao H, Lin D. Sci Rep 8 13211 (2018)
Controlling the Oligomerization State of Aβ-Derived Peptides with Light. Salveson PJ, Haerianardakani S, Thuy-Boun A, Kreutzer AG, Nowick JS. J Am Chem Soc 140 5842-5852 (2018)
X-ray Crystallography Reveals Parallel and Antiparallel β-Sheet Dimers of a β-Hairpin Derived from Aβ_16-36 that Assemble to Form Different Tetramers. Kreutzer AG, Samdin TD, Guaglianone G, Spencer RK, Nowick JS. ACS Chem Neurosci 11 2340-2347 (2020)
In Silico Modeling of the Influence of Environment on Amyloid Folding Using FOD-M Model. Roterman I, Stapor K, Fabian P, Konieczny L. Int J Mol Sci 22 10587 (2021)
Following the aggregation of human prion protein on Au(111) surface in real-time. Wang B, Guo C, Lou Z, Xu B. Chem Commun (Camb) 51 2088-2090 (2015)
Square channels formed by a peptide derived from transthyretin. Yoo S, Kreutzer AG, Truex NL, Nowick JS. Chem Sci 7 6946-6951 (2016)
Theory of amyloid fibril nucleation from folded proteins. Zhang L, Schmit JD. Isr J Chem 57 738-749 (2017)
On cooperative effects and aggregation of GNNQQNY and NNQQNY peptides. Nochebuena J, Ireta J. J Chem Phys 143 135103 (2015)
Origin, toxicity and characteristics of two amyloid oligomer polymorphs. Niyangoda C, Barton J, Bushra N, Karunarathne K, Strauss G, Fakhre F, Koria P, Muschol M. RSC Chem Biol 2 1631-1642 (2021)
Probing differences among Aβ oligomers with two triangular trimers derived from Aβ. Kreutzer AG, Guaglianone G, Yoo S, Parrocha CMT, Ruttenberg SM, Malonis RJ, Tong K, Lin YF, Nguyen JT, Howitz WJ, Diab MN, Hamza IL, Lai JR, Wysocki VH, Nowick JS. Proc Natl Acad Sci U S A 120 e2219216120 (2023)
Effect of the electrostatic surface potential on the oligomerization of full-length human recombinant prion protein at single-molecule level. Wang B, Lou Z, Zhang H, Xu B. J Chem Phys 144 114701 (2016)
The part of a long beta hairpin from the scrapie form of the human prion protein is reconstructed in the synthetic CC36 protein. Khrustalev VV, Khrustaleva TA, Szpotkowski K, Poboinev VV, Kakhanouskaya KY. Proteins 84 1462-1479 (2016)
The polar clasps of a bank vole PrP(168-176) prion protofibril revisiting. Zhang J. J Mol Model 25 108 (2019)

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Crystal structure of a human prion protein fragment reveals a motif for oligomer formation.

Abstract

Articles - 4e1h mentioned but not cited (2)

Reviews citing this publication (9)

Articles citing this publication (28)

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4e1h › Citations

Crystal structure of a human prion protein fragment reveals a motif for oligomer formation.

Abstract

Articles - 4e1h mentioned but not cited (2)

Reviews citing this publication (9)

Articles citing this publication (28)

Quick links