Amyloid as a depot for the formulation of long-acting drugs - Wikidata - awgldk - TriplyDB

Amyloid as a depot for the formulation of long-acting drugs

Amyloid as a depot for the formulation of long-acting drugs

http://www.wikidata.org/entity/Q28472154

about

Lanreotide Depot: An Antineoplastic Treatment of Carcinoid or Neuroendocrine Tumors The NatA acetyltransferase couples Sup35 prion complexes to the [PSI+] phenotype Binding mode of Thioflavin T and other molecular probes in the context of amyloid fibrils-current status Bacterial inclusion bodies contain amyloid-like structure Amyloidogenic determinants are usually not buried Elucidating the role of disulfide bond on amyloid formation and fibril reversibility of somatostatin-14: relevance to its storage and secretion Functional amyloids as natural storage of peptide hormones in pituitary secretory granules.Small heat shock proteins potentiate amyloid dissolution by protein disaggregases from yeast and humans Towards revealing the structure of bacterial inclusion bodies.De novo chemoattractants form supramolecular hydrogels for immunomodulating neutrophils in vivo.Amyloid form of ovalbumin evokes native antigen-specific immune response in the host: prospective immuno-prophylactic potential.Calcium binding to beta-2-microglobulin at physiological pH drives the occurrence of conformational changes which cause the protein to precipitate into amorphous forms that subsequently transform into amyloid aggregates.Arresting amyloid with coulomb's law: acetylation of ALS-linked SOD1 by aspirin impedes aggregation Cytotoxic helix-rich oligomer formation by melittin and pancreatic polypeptide Type 2 diabetes as a protein misfolding disease.Light-triggered disassembly of amyloid fibrils.Amyloid formation of growth hormone in presence of zinc: Relevance to its storage in secretory granules Building Nanostructures with Drugs.Molecular dynamics simulations of mechanical failure in polymorphic arrangements of amyloid fibrils containing structural defects.Biosensor-based label-free assays of amyloid growth.Structure-activity relationship of amyloid fibrils.Amyloid structure--one but not the same: the many levels of fibrillar polymorphism.The nature of amyloid-like glucagon fibrils Protein aggregation and amyloid fibril formation prediction software from primary sequence: towards controlling the formation of bacterial inclusion bodies.Nanomechanics of functional and pathological amyloid materials.Killer peptide: a novel paradigm of antimicrobial, antiviral and immunomodulatory auto-delivering drugs.Nanomaterials: amyloids reflect their brighter side.Control of amyloid assembly by autoregulation.Engineering protein self-assembling in protein-based nanomedicines for drug delivery and gene therapy.Amyloid-based nanosensors and nanodevices.Challenges in the delivery of peptide drugs: an industry perspective.Integrating mechanical and biological control of cell proliferation through bioinspired multieffector materials.Functional protein aggregates: just the tip of the iceberg.Eukaryotic aggresomes: from a model of conformational diseases to an emerging type of immobilized biocatalyzers.Insulin amyloid at injection sites of patients with diabetes.Amyloid Fibrils as Building Blocks for Natural and Artificial Functional Materials.Peptide-drug conjugates as effective prodrug strategies for targeted delivery.Structural and functional diversity among amyloid proteins: Agents of disease, building blocks of biology, and implications for molecular engineering.A nanostructured bacterial bioscaffold for the sustained bottom-up delivery of protein drugs.Self-assembling peptide and protein amyloids: from structure to tailored function in nanotechnology.

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Amyloid as a depot for the formulation of long-acting drugs

http://www.wikidata.org/entity/Q28472154

description

2008 nî lūn-bûn

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2008 թուականի Փետրուարին հրատարակուած գիտական յօդուած

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2008 թվականի փետրվարին հրատարակված գիտական հոդված

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2008年の論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年论文

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name

Amyloid as a depot for the formulation of long-acting drugs

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Amyloid as a depot for the formulation of long-acting drugs

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Amyloid as a depot for the formulation of long-acting drugs

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Amyloid as a depot for the formulation of long-acting drugs

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Amyloid as a depot for the formulation of long-acting drugs

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Amyloid as a depot for the formulation of long-acting drugs

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Amyloid as a depot for the formulation of long-acting drugs

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Amyloid as a depot for the formulation of long-acting drugs

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Amyloid as a depot for the formulation of long-acting drugs

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JOURNAL.PBIO.0060017

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Amyloid as a depot for the formulation of long-acting drugs

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Catherine Rivier

http://www.w3.org/2001/XMLSchema#string

David Schubert

http://www.w3.org/2001/XMLSchema#string

Jean E Rivier

http://www.w3.org/2001/XMLSchema#string

Roland Riek

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Samir K Maji

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Soon Lee

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Functional amyloid formation within mammalian tissue.

Agrin binds to beta-amyloid (Abeta), accelerates abeta fibril formation, and is localized to Abeta deposits in Alzheimer's disease brain

The structural basis of protein folding and its links with human disease

Amyloid aggregates of the HET-s prion protein are infectious.

Serum amyloid P component prevents proteolysis of the amyloid fibrils of Alzheimer disease and systemic amyloidosis

Extensive neurite outgrowth and active synapse formation on self-assembling peptide scaffolds

The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics

Protein misfolding, functional amyloid, and human disease

A yeast prion provides a mechanism for genetic variation and phenotypic diversity

Amyloid fibril formation by an SH3 domain.

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e17

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scholarly article

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10.1371/JOURNAL.PBIO.0060017

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6

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5596869

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18254658

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2225439

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