Reduction of the disulfide bond of chromogranin B (secretogranin I) in the trans-Golgi network causes its missorting to the constitutive secretory pathways. (Q34051310)

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English	Reduction of the disulfide bond of chromogranin B (secretogranin I) in the trans-Golgi network causes its missorting to the constitutive secretory pathways.	scientific article

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13 October 2019

Reduction of the disulfide bond of chromogranin B (secretogranin I) in the trans-Golgi network causes its missorting to the constitutive secretory pathways (English)

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13 October 2019

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13 October 2019

author name string

Chanat E

1

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13 October 2019

Weiss U

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13 October 2019

Huttner WB

3

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13 October 2019

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1 May 1993

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13 October 2019

The EMBO Journal

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13 October 2019

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13 October 2019

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13 October 2019

2159-2168

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13 October 2019

Membrane glycoprotein folding, oligomerization and intracellular transport: effects of dithiothreitol in living cells.

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The primary structure of human secretogranin I (chromogranin B): comparison with chromogranin A reveals homologous terminal domains and a large intervening variable region

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Constitutive and regulated secretion of proteins

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Inhibition of tyrosine sulfation in the trans-Golgi retards the transport of a constitutively secreted protein to the cell surface

1 reference

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Tyrosine sulfation is a trans-Golgi-specific protein modification

1 reference

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1 reference

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Biochemistry of the chromogranin A protein family

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Structure and function of the chromogranin A gene. Clues to evolution and tissue-specific expression.

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Chromogranin B (secretogranin I), a secretory protein of the regulated pathway, is also present in a tightly membrane-associated form in PC12 cells

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[10] Cell-free formation of immature secretory granules and constitutive secretory vesicles from trans-golgi network

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Identifiers

10.1002/J.1460-2075.1993.TB05864.X

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13 October 2019

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13 October 2019

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13 October 2019

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