Atomic structure of the cross-β spine of islet amyloid polypeptide (amylin) (Q27650849)

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English	Atomic structure of the cross-β spine of islet amyloid polypeptide (amylin)	scientific article

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instance of

scholarly article

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title

Atomic structure of the cross-β spine of islet amyloid polypeptide (amylin) (English)

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author

Duilio Cascio

series ordinal

4

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David Eisenberg

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7

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Michael R Sawaya

object named as

Michael R Sawaya

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3

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author name string

Jed J W Wiltzius

series ordinal

1

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Stuart A Sievers

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2

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Dmitriy Popov

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5

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Christian Riekel

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6

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publication date

September 2008

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published in

Protein Science

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volume

17

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issue

9

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page(s)

1467-74

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cites work

Atomic structures of amyloid cross-beta spines reveal varied steric zippers

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20 March 2017

Structure of the cross-beta spine of amyloid-like fibrils

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Purification and characterization of a peptide from amyloid-rich pancreases of type 2 diabetic patients

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Amyloid fibrils in human insulinoma and islets of Langerhans of the diabetic cat are derived from a neuropeptide-like protein also present in normal islet cells

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Shape complementarity at protein/protein interfaces

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New perspectives into the molecular pathogenesis and treatment of type 2 diabetes

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20 March 2017

Conservation of the sequence of islet amyloid polypeptide in five mammals is consistent with its putative role as an islet hormone

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20 March 2017

Islet amyloid polypeptide: pinpointing amino acid residues linked to amyloid fibril formation

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20 March 2017

Peptide conformation and supramolecular organization in amylin fibrils: constraints from solid-state NMR.

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29 September 2017

Membrane interaction of islet amyloid polypeptide

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29 September 2017

Polymorphism in the intermediates and products of amyloid assembly

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29 September 2017

Obesity and diabetes in the developing world--a growing challenge

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29 September 2017

The aggregation potential of human amylin determines its cytotoxicity towards islet beta-cells

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29 September 2017

Design of a mimic of nonamyloidogenic and bioactive human islet amyloid polypeptide (IAPP) as nanomolar affinity inhibitor of IAPP cytotoxic fibrillogenesis

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29 September 2017

Contribution of the intrinsic disulfide to the assembly mechanism of islet amyloid

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29 September 2017

Amylin agonists: a novel approach in the treatment of diabetes

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29 September 2017

Progress towards a molecular-level structural understanding of amyloid fibrils

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29 September 2017

Full-length rat amylin forms fibrils following substitution of single residues from human amylin

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PubMed Central

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29 September 2017

Role of islet amyloid in type 2 diabetes mellitus: consequence or cause?

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PubMed Central

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29 September 2017

Amyloidogenicity and cytotoxicity of islet amyloid polypeptide

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PubMed Central

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29 September 2017

A possible role for pi-stacking in the self-assembly of amyloid fibrils

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PubMed Central

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29 September 2017

Islet amyloid and type 2 diabetes mellitus

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PubMed Central

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29 September 2017

Identification of a penta- and hexapeptide of islet amyloid polypeptide (IAPP) with amyloidogenic and cytotoxic properties

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PubMed Central

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29 September 2017

Intra- and extracellular amyloid fibrils are formed in cultured pancreatic islets of transgenic mice expressing human islet amyloid polypeptide

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PubMed Central

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29 September 2017

Amylin compared with calcitonin gene-related peptide: structure, biology, and relevance to metabolic disease

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29 September 2017

Structural characterisation of islet amyloid polypeptide fibrils

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PubMed Central

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2 June 2018

Human islet amyloid polypeptide oligomers disrupt cell coupling, induce apoptosis, and impair insulin secretion in isolated human islets.

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PubMed Central

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27 November 2018

The parallel superpleated beta-structure as a model for amyloid fibrils of human amylin

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PubMed Central

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27 November 2018

Role of aromatic interactions in amyloid formation by peptides derived from human Amylin

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PubMed Central

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27 November 2018

Identifying structural features of fibrillar islet amyloid polypeptide using site-directed spin labeling

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PubMed Central

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27 November 2018

Human amylin oligomer growth and fibril elongation define two distinct phases in amyloid formation

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PubMed Central

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27 November 2018

The mechanism of insulin action on islet amyloid polypeptide fiber formation

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PubMed Central

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27 November 2018

Analysis of the minimal amyloid-forming fragment of the islet amyloid polypeptide. An experimental support for the key role of the phenylalanine residue in amyloid formation

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PubMed Central

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27 November 2018

Islet amyloid polypeptide: identification of long-range contacts and local order on the fibrillogenesis pathway

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PubMed Central

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27 November 2018

Effects of sequential proline substitutions on amyloid formation by human amylin20-29.

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PubMed Central

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27 November 2018

Human islet amyloid polypeptide transgenic mice as a model of non-insulin-dependent diabetes mellitus (NIDDM).

1 reference

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PubMed Central

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27 November 2018

Islet amyloid polypeptide gene promoter polymorphisms are not associated with Type 2 diabetes or with the severity of islet amyloidosis

1 reference

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PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/18556473

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Amyloid Fibril Formation from Full-Length and Fragments of Amylin

1 reference

stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/18556473

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

X-ray diffraction studies on amyloid filaments

1 reference

stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/18556473

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Polymorphic Fibrillar Assembly of Human Amylin

1 reference

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PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/18556473

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

DOI

10.1110/PS.036509.108

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

3621958

OpenCitations bibliographic resource ID

3621958

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

3621958

PMC publication ID

2525530

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

3621958

PubMed publication ID

18556473

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

3621958

ResearchGate publication ID

5299214

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