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Showing 1–29 of 29 results
Advanced filters: Author: "Adriano Aguzzi" Clear advanced filters

  • Funders should award competitive grants directly to journals to underwrite the costs of open access, urges Adriano Aguzzi.

    • Adriano Aguzzi
    Comments & Opinion
    Nature
    Volume: 570, P: 139

  • Adriano Aguzzi discusses the endeavours of the Gitler team to identify the causes underlying the fatal human neurological disease amyotrophic lateral sclerosis (ALS).

    • Adriano Aguzzi
    Research Highlights
    Nature Reviews Molecular Cell Biology
    Volume: 20, P: 67

  • The H-latch is a well-defined structural change occurring in PrPC bound to the neurotoxic antibody POM1, and its presence shows a positive correlation with neurotoxicity. Inhibition of the H-latch prolongs the lifespan of prion-diseased mice.

    • Karl Frontzek
    • Marco Bardelli
    • Adriano Aguzzi
    ResearchOpen Access
    Nature Structural & Molecular Biology
    Volume: 29, P: 831-840

  • The adaptation of the protein misfolding cyclic amplification assay (PMCA) to use recombinant hamster prion protein (PrP) as a substrate shows promise for both basic research applications and clinical diagnostic assays.

    • Adriano Aguzzi
    News & Views
    Nature Methods
    Volume: 4, P: 614-616

  • It seems that many misfolded proteins can act like prions — spreading disease by imparting their misshapen structure to normal cellular counterparts. But how common are bona fide prions really?

    • Adriano Aguzzi
    News & Views
    Nature
    Volume: 459, P: 924-925

  • Human prion diseases are sometimes difficult to diagnose because few clinical features distinguish them reliably from other neurological disorders. A new study suggests that analysis of movement disorders might contribute to the clinical differentiation of sporadic Creutzfeldt–Jakob disease from Alzheimer disease and dementia with Lewy bodies.

    • Michael Weller
    • Adriano Aguzzi
    News & Views
    Nature Reviews Neurology
    Volume: 5, P: 185-186

  • Improved photostability of fluorescent proteins would benefit many applications but is usually an afterthought in selection screens. Setting photostability as the primary selection criterion in screens for improved fluorescent proteins yielded highly photostable variants of existing orange and red fluorescent proteins without compromising other beneficial characteristics.

    • Christina J Sigurdson
    • K Peter R Nilsson
    • Adriano Aguzzi
    Research
    Nature Methods
    Volume: 4, P: 1023-1030

  • Prions are infectious proteins that cause fatal neurodegenerative diseases. The prion itself is a misfolded conformer of a normal host protein, which explains why it is difficult for the immune system to respond to it effectively. The authors explain how prions evade, and indeed exploit, immune components to spread to the central nervous system, and they discuss the immunotherapies that are being developed to combat these lethal infections.

    • Adriano Aguzzi
    • Mario Nuvolone
    • Caihong Zhu
    Reviews
    Nature Reviews Immunology
    Volume: 13, P: 888-902

  • The signals ensuring maintenance of the myelin sheath on peripheral nerves are distinct from those instructing myelination and are largely unknown. Here, the authors report that neuronal expression and regulated proteolysis of the prion protein are essential for myelin maintenance.

    • Juliane Bremer
    • Frank Baumann
    • Adriano Aguzzi
    Research
    Nature Neuroscience
    Volume: 13, P: 310-318

  • Diseases such as Alzheimer's disease and systemic amyloidoses are associated with inappropriate deposition of proteins containing a characteristic highly ordered, β-sheet-rich structural motif. The common structural and pathogenic features of these diverse protein aggregation diseases may offer opportunities to develop overarching therapeutic strategies.

    • Adriano Aguzzi
    • Tracy O'Connor
    Reviews
    Nature Reviews Drug Discovery
    Volume: 9, P: 237-248

  • In this perspective, the authors review new developments that suggest that many diseases share features with prion infections. They also highlight some of the critical open questions in prion biology, including how prions damage their hosts and how hosts attempt to neutralize invading prions.

    • Adriano Aguzzi
    • Jeppe Falsig
    Reviews
    Nature Neuroscience
    Volume: 15, P: 936-939

  • Although it is now accepted that the infectious agent that causes transmissible spongiform encephalopathies is PrPSc, recent insights into the existence of prion strains pose a fascinating challenge to prion research. What is the nature of prion strains? And how can they be discriminated?

    • Adriano Aguzzi
    • Mathias Heikenwalder
    • Magdalini Polymenidou
    Reviews
    Nature Reviews Molecular Cell Biology
    Volume: 8, P: 552-561

  • In recent years, significant progress has been made in our understanding of the biology of prions, yet many fundamental questions remain unanswered. Aguzzi and Heikenwalder discuss some of these unanswered questions, focusing on the role of the immune system in prion pathogenesis.

    • Adriano Aguzzi
    • Mathias Heikenwalder
    Reviews
    Nature Reviews Microbiology
    Volume: 4, P: 765-775

  • There's a lot of disagreement among prion scientists, as a recent conference made very clear. Even the revered 'prion hypothesis' came under attack.

    • Adriano Aguzzi
    • Mathias Heikenwalder
    News & Views
    Nature
    Volume: 423, P: 127-128

  • Two studies of amyloid-β protein aggregates, which cause Alzheimer's disease, find that different conformations of the aggregates can define different strains of the disorder, drawing parallels with prion diseases.

    • Adriano Aguzzi
    News & Views
    Nature
    Volume: 512, P: 32-34

  • Blood has not generally been regarded as a significant route of transmission for variant Creutzfeldt–Jakob disease (vCJD), but three cases of vCJD transmission through blood transfusion have recently come to light. In this review, Aguzzi and Glatzel discuss these findings in relation to experimental data on prion disease transmission, and consider the possible implications for the safety of blood products.

    • Adriano Aguzzi
    • Markus Glatzel
    Reviews
    Nature Clinical Practice Neurology
    Volume: 2, P: 321-329

  • A recent paper reported the in vitro generation of new prion strains, supporting the idea that 'strain-ness' is encoded in the protein structure itself. This lays the groundwork for a reinvigorated study of prion structure–pathology relationships.

    • Adriano Aguzzi
    News & Views
    Nature Neuroscience
    Volume: 11, P: 1239-1240

  • Parallels are increasingly being drawn between prion diseases and other aggregate-mediated neurodegenerative disorders. While prion diseases are a distinct subclass of protein misfolding disorders (PMDs), a better understanding of shared mechanisms is likely to benefit treatment of all PMDs.

    • Claudia Scheckel
    • Adriano Aguzzi
    Reviews
    Nature Reviews Genetics
    Volume: 19, P: 405-418

  • Cultured brain slices from mice spontaneously upregulate senescence-associated genes over time and reproduce the transcriptional characteristics of aged brains; prions accelerate brain aging in brain slice cultures, animal models and human patients.

    • Yingjun Liu
    • Assunta Senatore
    • Adriano Aguzzi
    ResearchOpen Access
    Communications Biology
    Volume: 5, P: 1-11