Zn(II) ions co-secreted with insulin suppress inherent amyloidogenic properties of monomeric insulin. (Q51679466)

9 April 2018

title

Zn(II) ions co-secreted with insulin suppress inherent amyloidogenic properties of monomeric insulin. (English)

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9 April 2018

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Andra Noormägi

1

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Julia Smirnova

object named as

Julia Smirnova

3

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Vello Tõugu

object named as

Vello Tõugu

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author name string

Julia Gavrilova

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9 April 2018

Peep Palumaa

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9 April 2018

language of work or name

English

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publication date

1 September 2010

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9 April 2018

published in

Biochemical Journal

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9 April 2018

volume

430

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9 April 2018

issue

3

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9 April 2018

page(s)

511-518

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9 April 2018

Direct identification of prohormone conversion site in insulin-secreting cells

cites work

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The role of assembly in insulin's biosynthesis

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Survey of mRNAs encoding zinc transporters and other metal complexing proteins in pancreatic islets of rats from birth to adulthood: similar patterns in the Sprague-Dawley and Wistar BB strains.

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In vivo expression and functional characterization of the zinc transporter ZnT8 in glucose-induced insulin secretion

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Insulin crystallization depends on zinc transporter ZnT8 expression, but is not required for normal glucose homeostasis in mice.

21 January 2018

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Formation of insulin amyloid fibrils followed by FTIR simultaneously with CD and electron microscopy.

21 January 2018

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Toward understanding insulin fibrillation

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Stimulation of insulin fibrillation by urea-induced intermediates

21 January 2018

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Elemental composition of secretory granules in pancreatic islets of Langerhans

21 January 2018

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Effect of environmental factors on the kinetics of insulin fibril formation: elucidation of the molecular mechanism

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Partially folded intermediates in insulin fibrillation

21 January 2018

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Characterization of the oligomeric states of insulin in self-assembly and amyloid fibril formation by mass spectrometry

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Rapid induction of Alzheimer A beta amyloid formation by zinc.

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Molecular understanding of copper and iron interaction with alpha-synuclein by fluorescence analysis

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Zn(II)- and Cu(II)-induced non-fibrillar aggregates of amyloid-beta (1-42) peptide are transformed to amyloid fibrils, both spontaneously and under the influence of metal chelators.

21 January 2018

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Probing the mechanism of insulin fibril formation with insulin mutants

21 January 2018

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Early events in the fibrillation of monomeric insulin.

21 January 2018

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21 January 2018

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Insulin is a kinetic but not a thermodynamic inhibitor of amylin aggregation

21 January 2018

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Proinsulin C-peptide elicits disaggregation of insulin resulting in enhanced physiological insulin effects

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Oligomerization and insulin interactions of proinsulin C-peptide: Threefold relationships to properties of insulin

21 January 2018

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Polymerization pattern of insulin at pH 7.0

21 January 2018

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The influence of ionic strength and pH on the aggregation properties of zinc-free insulin studied by static and dynamic laser light scattering

21 January 2018

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X-ray crystallographic studies on zinc insulin crystals

21 January 2018

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Structure of human insulin monomer in water/acetonitrile solution

21 January 2018

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Molecular basis for insulin fibril assembly

21 January 2018

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Time-dependent insulin oligomer reaction pathway prior to fibril formation: cooling and seeding

21 January 2018

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A universal pathway for amyloid nucleus and precursor formation for insulin

21 January 2018

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Insulin fibril nucleation: the role of prefibrillar aggregates.

21 January 2018

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A beta oligomers - a decade of discovery

21 January 2018

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Natural course of preclinical type 1 diabetes

21 January 2018

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Copper- and iron-induced differential fibril formation in α-synuclein: TEM study

21 January 2018

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21 January 2018

Identifiers

DOI

10.1042/BJ20100627

1 reference

9 April 2018

release_3rtpgpyp6zesfiz6k4sn3sypui

Fatcat ID

1 reference

Fatcat

https://api.fatcat.wiki/v0/release/3rtpgpyp6zesfiz6k4sn3sypui

mapped directly with Wikidata item

24 November 2022

based on heuristic

1 reference

9 April 2018