S-adenosylmethionine decarboxylase degradation by the 26 S proteasome is accelerated by substrate-mediated transamination. (Q44725318)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:14718534%20AND%20SRC:MED&resulttype=core&format=json

17 November 2019

title

S-adenosylmethionine decarboxylase degradation by the 26 S proteasome is accelerated by substrate-mediated transamination (English)

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17 November 2019

2

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17 November 2019

author name string

Azmi Yerlikaya

series ordinal

1

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17 November 2019

language of work or name

English

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publication date

12 January 2004

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Journal of Biological Chemistry

17 November 2019

published in

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17 November 2019

volume

279

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17 November 2019

issue

13

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17 November 2019

page(s)

12469-12478

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17 November 2019

1 reference

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Regulation of S-adenosylmethionine decarboxylase activity by alterations in the intracellular polyamine content

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Ornithine decarboxylase is degraded by the 26S proteasome without ubiquitination

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The crystal structure of human S-adenosylmethionine decarboxylase at 2.25 A resolution reveals a novel fold

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Identifiers

DOI

10.1074/JBC.M312625200

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:14718534%20AND%20SRC:MED&resulttype=core&format=json

17 November 2019

1 reference