(Q24297115)

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The MYND domain-containing protein BRAM1 inhibits lymphotoxin beta receptor-mediated signaling through affecting receptor oligomerization

scientific article published on August 21, 2010

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title

The MYND domain-containing protein BRAM1 inhibits lymphotoxin beta receptor-mediated signaling through affecting receptor oligomerization (English)

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main subject

Zinc finger MYND-type containing 11

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stated in

GOA release 2020-03-11

Lymphotoxin beta receptor

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stated in

GOA release 2020-03-11

negative regulation of extrinsic apoptotic signaling pathway

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stated in

GOA release 2020-03-11

1

Hao-Ping Liu

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Europe PubMed Central

PubMed publication ID

20732415

reference URL

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A20732415

21 June 2024

4

Yu-Sun Chang

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Europe PubMed Central

PubMed publication ID

20732415

reference URL

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A20732415

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21 June 2024

author name string

Pei-Jung Chung

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2

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Chih-Lung Liang

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3

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language of work or name

English

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publication date

January 2011

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21 August 2010

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Europe PubMed Central

PubMed publication ID

20732415

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A20732415

retrieved

21 June 2024

full work available at URL

https://api.elsevier.com/content/article/PII:S0898656810002330?httpAccept=text/xml

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DOI

10.1016/J.CELLSIG.2010.08.006

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https://api.crossref.org/works/10.1016/J.CELLSIG.2010.08.006

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21 June 2024

https://api.elsevier.com/content/article/PII:S0898656810002330?httpAccept=text/plain

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DOI

10.1016/J.CELLSIG.2010.08.006

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https://api.crossref.org/works/10.1016/J.CELLSIG.2010.08.006

21 June 2024

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23

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issue

1

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page(s)

80-8

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Identifiers

DOI

10.1016/J.CELLSIG.2010.08.006

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PubMed publication ID

20732415

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(Q24297115)

The MYND domain-containing protein BRAM1 inhibits lymphotoxin beta receptor-mediated signaling through affecting receptor oligomerization

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