Ocular proteomics: cataloging photoreceptor proteins by two-dimensional gel electrophoresis and mass spectrometry (Q30868643)

27 June 2017

Ocular proteomics: cataloging photoreceptor proteins by two-dimensional gel electrophoresis and mass spectrometry (English)

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27 June 2017

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photoreceptor protein

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author name string

Matsumoto H

series ordinal

1

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PubMed ID

10800697

27 June 2017

Komori N

series ordinal

2

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PubMed ID

10800697

27 June 2017

language of work or name

English

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publication date

1 January 2000

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27 June 2017

Methods in Enzymology

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27 June 2017

316

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27 June 2017

492-511

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Isoelectric focusing and gradient gel electrophoresis: A two-dimensional technique

27 June 2017

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Posttranslational Covalent Modification of Proteins

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In vivo chemical modification of proteins (post-translational modification).

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Phosrestin I undergoes the earliest light-induced phosphorylation by a calcium/calmodulin-dependent protein kinase in Drosophila photoreceptors.

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In-gel digestion of proteins for internal sequence analysis after one- or two-dimensional gel electrophoresis

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Initiating ocular proteomics for cataloging bovine retinal proteins: microanalytical techniques permit the identification of proteins derived from a novel photoreceptor preparation.

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Protein identification in DNA databases by peptide mass fingerprinting

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Rhodopsin kinase autophosphorylation. Characterization of site-specific mutations

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Prenylation and carboxylmethylation of G-protein gamma subunit.

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Identifiers

DOI

1 reference

27 June 2017

1 reference

PubMed ID

10800697