(Q39297363)

English

Caenorhabditis elegans S-adenosylmethionine decarboxylase is highly stimulated by putrescine but exhibits a low specificity for activator binding

scientific article published on January 2003

In more languages

Statements

scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

10 September 2017

Caenorhabditis elegans S-adenosylmethionine decarboxylase is highly stimulated by putrescine but exhibits a low specificity for activator binding (English)

1 reference

Europe PubMed Central

PubMed publication ID

10 September 2017

Caenorhabditis elegans

0 references

S-adenosylmethionine decarboxylase beta chain CELE_F47G4.7

1 reference

GOA release 2020-03-11

author name string

Dieudonne Ndjonka

1

1 reference

Europe PubMed Central

PubMed publication ID

10 September 2017

Akram Da'dara

2

1 reference

Europe PubMed Central

PubMed publication ID

10 September 2017

Rolf D Walter

3

1 reference

Europe PubMed Central

PubMed publication ID

10 September 2017

Kai Lüersen

4

1 reference

Europe PubMed Central

PubMed publication ID

10 September 2017

publication date

1 January 2003

1 reference

Europe PubMed Central

PubMed publication ID

10 September 2017

Biological Chemistry

1 reference

Europe PubMed Central

PubMed publication ID

10 September 2017

384

1 reference

Europe PubMed Central

PubMed publication ID

10 September 2017

1

1 reference

Europe PubMed Central

PubMed publication ID

10 September 2017

83-91

1 reference

Europe PubMed Central

PubMed publication ID

10 September 2017

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

1 reference

https://api.crossref.org/works/10.1515%2FBC.2003.009

21 January 2018

Activation of rat liver S-adenosylmethionine decarboxylase by putrescine and 2-substituted 1,4-butanediamines.

1 reference

https://api.crossref.org/works/10.1515%2FBC.2003.009

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1515%2FBC.2003.009

21 January 2018

Structure of a human S-adenosylmethionine decarboxylase self-processing ester intermediate and mechanism of putrescine stimulation of processing as revealed by the H243A mutant

1 reference

https://api.crossref.org/works/10.1515%2FBC.2003.009

21 January 2018

pha-1, a selectable marker for gene transfer in C. elegans

1 reference

https://api.crossref.org/works/10.1515%2FBC.2003.009

21 January 2018

Putrescine-activated S-adenosylmethionine decarboxylase from Acanthamoeba culbertsoni

1 reference

https://api.crossref.org/works/10.1515%2FBC.2003.009

21 January 2018

Cloning and expression of the S-adenosylmethionine decarboxylase gene of Neurospora crassa and processing of its product

1 reference

https://api.crossref.org/works/10.1515%2FBC.2003.009

21 January 2018

Reverse genetics by chemical mutagenesis in Caenorhabditis elegans

1 reference

https://api.crossref.org/works/10.1515%2FBC.2003.009

21 January 2018

Cloning and kinetic characterization of the Trypanosoma cruzi S-adenosylmethionine decarboxylase

1 reference

https://api.crossref.org/works/10.1515%2FBC.2003.009

21 January 2018

S-Adenosylmethionine

1 reference

https://api.crossref.org/works/10.1515%2FBC.2003.009

21 January 2018

DNA transformation

1 reference

https://api.crossref.org/works/10.1515%2FBC.2003.009

21 January 2018

Stimulation of the decarboxylation of S-adenosylmethionine by putrescine in mammalian tissues

1 reference

https://api.crossref.org/works/10.1515%2FBC.2003.009

21 January 2018

Purification and characterization of S-adenosyl-L-methionine decarboxylase from mouse mammary gland and liver

1 reference

https://api.crossref.org/works/10.1515%2FBC.2003.009

21 January 2018

Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa

1 reference

https://api.crossref.org/works/10.1515%2FBC.2003.009

21 January 2018

Putrescine-Sensitive (Artifactual) and Insensitive (Biosynthetic) S-Adenosyl-L-Methionine Decarboxylase Activities of Lathyrus sativus Seedlings

1 reference

https://api.crossref.org/works/10.1515%2FBC.2003.009

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2003.009

21 January 2018

Putrescine activated S-adenosylmethionine decarboxylase from Trypanosoma brucei brucei

1 reference

https://api.crossref.org/works/10.1515%2FBC.2003.009

21 January 2018

The structural basis for substrate specificity and inhibition of human S-adenosylmethionine decarboxylase

1 reference

https://api.crossref.org/works/10.1515%2FBC.2003.009

21 January 2018

The Plasmodium falciparum bifunctional ornithine decarboxylase, S-adenosyl-L-methionine decarboxylase, enables a well balanced polyamine synthesis without domain-domain interaction.

1 reference

https://api.crossref.org/works/10.1515%2FBC.2003.009

21 January 2018

Mechanistic studies of the processing of human S-adenosylmethionine decarboxylase proenzyme. Isolation of an ester intermediate

1 reference

https://api.crossref.org/works/10.1515%2FBC.2003.009

21 January 2018

Processing of mammalian and plant S-adenosylmethionine decarboxylase proenzymes

1 reference

https://api.crossref.org/works/10.1515%2FBC.2003.009

21 January 2018

Purification of S-adenosylmethionine decarboxylase from soybean

1 reference

https://api.crossref.org/works/10.1515%2FBC.2003.009

21 January 2018

Identifiers

10.1515/BC.2003.009

1 reference

Europe PubMed Central

PubMed publication ID

10 September 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

10 September 2017

Sitelinks

Wikipedia(0 entries)

Wikibooks(0 entries)

Wikinews(0 entries)

Wikiquote(0 entries)

Wikisource(0 entries)

Wikiversity(0 entries)

Wikivoyage(0 entries)

Wiktionary(0 entries)

Multilingual sites(0 entries)

Retrieved from "https://www.wikidata.org/w/index.php?title=Q39297363&oldid=1819047971"