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The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.

Molecular Cloning and Characterization of Bif-1

Open access
Cuddeback, Sandy M., Yamaguchi, Hirohito, Komatsu, Kiyoshi, Miyashita, Toshiyuki, Yamada, Masao, Wu, Chun, Singh, Sujay, Wang, Hong-Gang·2001·Journal of Biological Chemistry

Abstract

Bax is a proapoptotic member of the Bcl-2 protein family that commits the cell to undergo programmed cell death in response to apoptotic stimuli. To gain further insights into Bax mechanisms, we have identified a novel Bax-binding protein, termed Bif-1, by using a yeast two-hybrid cloning technique. Bif-1 is an evolutionarily conserved cytoplasmic protein that contains a predicted Src homology 3 (SH3) domain located near its C terminus but shares no significant homology with members of the Bcl-2 family. A Northern blot analysis indicates that Bif-1 is expressed in most tissues with abundant expression in heart and skeletal muscle. Bif-1 is capable of interacting with Bax as demonstrated by yeast two-hybrid, coimmunoprecipitation, and immunofluorescence studies. Induction of apoptosis in murine pre-B hematopoietic cells FL5.12 by interleukin-3 withdrawal results in increased association of Bax with Bif-1, which is accompanied by a conformational change in the Bax protein. Overexpression of Bif-1 promotes Bax conformational change, caspase activation, and apoptotic cell death in FL5.12 cells following interleukin-3 deprivation. Bif-1 thus represents a new type of regulator of Bax-mediated signaling pathways for apoptosis.

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Metadata

Authors
Cuddeback, S. M., Yamaguchi, H., Komatsu, K., Miyashita, T., Yamada, M., Wu, C., Singh, S., & Wang, H.-G.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
2001-01
Volume
276
Issue
23
Pages
20559-20565
ISSN
0021-9258 (ISSN-L)
OpenAlex
W2049180642
Cited by
635
References
3
FWCI
11.29
Type
journal article
Language
en
Open access
hybrid

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