(Q47905653)

6 February 2018

title

Structural changes in alpha-crystallin and whole eye lens during heating, observed by low-angle X-ray diffraction. (English)

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6 February 2018

main subject

X-ray diffraction

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X-ray crystallography

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author name string

Regini JW

1

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6 February 2018

Grossmann JG

2

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6 February 2018

Burgio MR

3

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6 February 2018

Malik NS

4

1 reference

6 February 2018

Koretz JF

5

1 reference

6 February 2018

Hodson SA

6

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6 February 2018

Elliott GF

7

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6 February 2018

language of work or name

English

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publication date

1 March 2004

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6 February 2018

Journal of Molecular Biology

number of pages

10

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based on heuristic

inferred from page(s)

published in

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6 February 2018

volume

336

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6 February 2018

issue

5

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6 February 2018

page(s)

1185-1194

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6 February 2018

alpha B subunit of lens-specific protein alpha-crystallin is present in other ocular and non-ocular tissues

cites work

1 reference

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Tissue distribution and developmental profiles of immunoreactive alpha B crystallin in the rat determined with a sensitive immunoassay system.

7 January 2021

1 reference

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A possible structure for alpha-crystallin

7 January 2021

1 reference

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Image restrained modeling of alphaB-crystallin

7 January 2021

1 reference

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Short-range order of crystallin proteins accounts for eye lens transparency

7 January 2021

1 reference

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Alpha-crystallin can function as a molecular chaperone

7 January 2021

1 reference

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Protection of enzymes by alpha-crystallin acting as a molecular chaperone.

7 January 2021

1 reference

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Characterization of the alpha-gamma and alpha-beta complex: evidence for an in vivo functional role of alpha-crystallin as a molecular chaperone.

7 January 2021

1 reference

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Evidence that alpha-crystallin prevents non-specific protein aggregation in the intact eye lens

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900814-3

Eye lens alphaA- and alphaB-crystallin: complex stability versus chaperone-like activity

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900814-3

Heat-induced conformational change and increased chaperone activity of lens alpha-crystallin

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900814-3

Correlation between the chaperone-like activity and aggregate size of alpha-crystallin with increasing temperature

7 January 2021

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The effect of temperature on the Donnan potentials in biological polyelectrolyte gels: cornea and striated muscle

7 January 2021

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Protein denaturation: a small-angle X-ray scattering study of the ensemble of unfolded states of cytochrome c.

7 January 2021

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Molecular basis of eye lens transparency. Osmotic pressure and X-ray analysis of alpha-crystallin solutions

7 January 2021

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A small-angle X-ray solution scattering study of bovine alpha-crystallin

7 January 2021

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Native quaternary structure of bovine alpha-crystallin

7 January 2021

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Polydispersity of a mammalian chaperone: mass spectrometry reveals the population of oligomers in alphaB-crystallin

7 January 2021

1 reference

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alpha m-Crystallin: the native form of the protein?

7 January 2021

1 reference

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Multiwire Gas Proportional Counters: Decrepit Antiques or ClassicPerformers?

7 January 2021

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Type I collagen packing, conformation of the triclinic unit cell

7 January 2021

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10.1016/S0022-2836(03)00814-3

7 January 2021

Identifiers

DOI

1 reference

6 February 2018

PubMed ID

15037078

1 reference

6 February 2018