| http://purl.uniprot.org/citations/8402648 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/8402648 | http://www.w3.org/2000/01/rdf-schema#comment | "A multidisciplinary approach was taken to investigate the intracellular locations of the 26-kDa integral membrane protein encoded by the bcl-2 gene. Subcellular fractionation analysis of a t(14;18)-containing lymphoma cell line revealed the presence of Bcl-2 protein in nuclear, heavy-membrane, and light-membrane fractions but not in cytosol. Sedimentation of heavy-membrane fractions in Nycodenz and Percoll continuous gradients demonstrated comigration of p26-Bcl-2 with mitochondrial but not other organelle-associated proteins. Fractionation of light-membrane fractions using discontinuous sucrose-gradients revealed association of Bcl-2 protein primarily with lighter-density microsomes (smooth endoplasmic reticulum) as opposed to heavy-density microsomes (rough endoplasmic reticulum). Immune microscopy studies using laser-scanning microscopy, pre- and postembedding electron microscopic methods, and six different anti-Bcl-2 antibodies demonstrated Bcl-2 immunoreactivity in the nuclear envelope and outer mitochondrial membrane in a patchy distribution. Furthermore, anti-Bcl-2 antibody immunoreactivity generally appeared to directly overlie the nuclear envelope in high magnification electron microscopic studies, reminiscent of nuclear pore complexes. Addition of in vitro translated p26-Bcl-2 to isolated translocation-competent mitochondria revealed transmembrane domain-dependent association of Bcl-2 protein with mitochondria but provided no evidence for import into a protease-resistant compartment, consistent with immunomicroscopic localization to the outer mitochondrial membrane. Taken together, the findings demonstrate that p26-Bcl-2 resides primarily in the nuclear envelope, endoplasmic reticulum, and outer mitochondrial membrane in a nonuniform distribution suggestive of participation in protein complexes perhaps involved in some aspect of transport."xsd:string |
| http://purl.uniprot.org/citations/8402648 | http://purl.uniprot.org/core/author | "Tanaka S."xsd:string |
| http://purl.uniprot.org/citations/8402648 | http://purl.uniprot.org/core/author | "Krajewski S."xsd:string |
| http://purl.uniprot.org/citations/8402648 | http://purl.uniprot.org/core/author | "Reed J.C."xsd:string |
| http://purl.uniprot.org/citations/8402648 | http://purl.uniprot.org/core/author | "Takayama S."xsd:string |
| http://purl.uniprot.org/citations/8402648 | http://purl.uniprot.org/core/author | "Schibler M.J."xsd:string |
| http://purl.uniprot.org/citations/8402648 | http://purl.uniprot.org/core/author | "Fenton W."xsd:string |
| http://purl.uniprot.org/citations/8402648 | http://purl.uniprot.org/core/date | "1993"xsd:gYear |
| http://purl.uniprot.org/citations/8402648 | http://purl.uniprot.org/core/name | "Cancer Res"xsd:string |
| http://purl.uniprot.org/citations/8402648 | http://purl.uniprot.org/core/pages | "4701-4714"xsd:string |
| http://purl.uniprot.org/citations/8402648 | http://purl.uniprot.org/core/title | "Investigation of the subcellular distribution of the bcl-2 oncoprotein: residence in the nuclear envelope, endoplasmic reticulum, and outer mitochondrial membranes."xsd:string |
| http://purl.uniprot.org/citations/8402648 | http://purl.uniprot.org/core/volume | "53"xsd:string |
| http://purl.uniprot.org/citations/8402648 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/8402648 |
| http://purl.uniprot.org/citations/8402648 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/8402648 |
| http://purl.uniprot.org/uniprot/P10415#attribution-1D416970D0365E74E251A4652F5F460F | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/8402648 |