Results 151 to 160 of about 49,492 (243)

The octapeptide repeats of prion protein play critical roles in the pathogenesis of prion diseases. [PDF]

Acta Neuropathol Commun
Zhang X, Zhang J, Zhang Y, Wang D, Liu G, Wang M, Li C, Shi Q, Dong X, Yuan C, Li W, Ma J.   +11 more
europepmc   +1 more source

Damping amyloid‐associated conformational fluctuations in a protein by an engineered diselenide bridge

Protein Science, Volume 35, Issue 8, August 2026.
Abstract Polypeptide cross‐β assembly, characteristic of diverse proteotoxic diseases, defines a general thermodynamic ground state and limits the shelf lives of peptide‐ and protein therapeutics. A model is provided by insulin. Although the hormone contains a predominance of α‐helix, its fibrils exhibit cross‐β reorganization.
Yanwu Yang, Balamurugan Dhayalan, Andreas Ehnbom, Orit Weil‐Ktorza, Norman Metanis, Michael A. Weiss   +5 more
wiley   +1 more source

Prion-based protein self-assembly tunes mutagenesis to enable rapid adaptation. [PDF]

Cell
Van Elgort A, Jakobson CM, Chen YR, Byers JS, Futia RA, Lozanoski TM, Harvey ZH, Xie JL, Garcia DM, Jarosz DF.   +9 more
europepmc   +1 more source

In Memoriam: J. Richard Baringer, MD (1935–2025)

Annals of Neurology, Volume 100, Issue 2, Page 235-237, August 2026.
John E. Greenlee, John W. Rose, Kathleen B. Digre, Mark B. Bromberg   +3 more
wiley   +1 more source

Advances in the nanostructure characterization of biological hydrogels formed by the prion‐like domain of EARLY FLOWERING 3

Acta Crystallographica Section D, Volume 82, Issue 8, Page 940-946, August 2026.
In biological systems, hydrogels often arise through liquid–liquid phase separation, where biomolecular condensates can age into gel‐like states. SAXS is a key technique to probe the molecular organization of these samples. This study introduces an in‐vacuum Gel‐Cell for SAXS‐based structural analysis of a biologically derived hydrogel formed by the ...
Stephanie Hutin, Pedro L. O. Filho, Anton M. Popov, Petra Pernot, Chloe Zubieta, Mark D. Tully   +5 more
wiley   +1 more source

Understanding the Phenotypic Heterogeneity Within the Sporadic Creutzfeldt-Jakob Disease MV1 Subtype. [PDF]

Neuropathol Appl Neurobiol
Nemani SK, Cortez LM, Myskiw J, Cali I, Booth SA, Jansen GH, Sim VL.   +6 more
europepmc   +1 more source

Infection control in the brain and the eye

Acta Ophthalmologica, Volume 104, Issue 5, Page e478-e490, August 2026.
Abstract The Central Nervous System (CNS), comprising the brain and the eye, is considered to have a ‘privileged’ mechanism for dealing with immunological challenge (immune privilege, IP). CNS IP has been revealed through experiments using foreign protein antigens and cell and tissue alloantigens (grafts), but evidence for a role for IP in modulating ...
John V. Forrester, Paul G. McMenamin, Samantha J. Dando   +2 more
wiley   +1 more source

Prion Diseases-When Proteins Turn Lethal: Creutzfeldt-Jakob Disease (CJD) and the Quest for Classification, Diagnosis, Therapeutic Approaches, and Emerging Research. [PDF]

Molecules
Ramesh TS, Bartusik-Aebisher D, Dynarowicz K, Aebisher D.   +3 more
europepmc   +1 more source

Concurrent Hashimoto's Encephalopathy and Papillary Thyroid Carcinoma: A Case Report

Clinical and Experimental Neuroimmunology, Volume 17, Issue 3, August 2026.
ABSTRACT Background Hashimoto's encephalopathy (HE) is a rare steroid‐responsive autoimmune syndrome. Although HE is associated with anti‐thyroid antibodies, its concurrence with malignant thyroid tumors has rarely been described and its clinical implications remain poorly understood.
Ryo Hara, Toshiyuki Kakumoto, Anna Suzuki, Satoshi Yamashita, Takayoshi Niwa, Kanako Hayashi, Arisa Morizono, Ayaka Sato, Masahiko Tanabe, Noritaka Kudo, Masashi Hamada, Wataru Satake, Tatsushi Toda   +12 more
wiley   +1 more source

Water‐Mediated Phosphoryl Wires Stabilize Pathological Tau Fibrils

Angewandte Chemie, Volume 138, Issue 30, 20 July 2026.
Extended 1D phosphoryl “wires” stabilize in‐register amyloid tau fibrils, as demonstrated by multiple‐quantum spin‐counting NMR, TEM, and MD simulations, using fibrils of tau peptide jR2R3‐P301L (tau295–313) with phosphorylation at S305 or Y310. ABSTRACT Hyperphosphorylation of tau is a hallmark of tauopathies, with specific phosphorylation sites ...
Lokeswara Rao Potnuru, Austin DuBose, Fiona Mon, Mesopotamia S. Nowotarski, Michael Vigers, Boqin Zhang, Chung‐Ta Han, John E. Straub, Songi Han   +8 more
wiley   +2 more sources