ArticleThe Biochemical journal1991
Characterization of isoforms of protein 4.1 present in the nucleus.
Article in The Biochemical journal, 1991. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
21 citing papers in PubMed, 62 citations in OpenAlex.
- FERM domain-containing proteins are active components of the cell nucleus.Life science alliance · 2024Review
- Protein 4.1N is required for the formation of the lateral membrane domain in human bronchial epithelial cells.Biochimica et biophysica acta. Biomembranes · 2018Article
- Lack of protein 4.1G causes altered expression and localization of the cell adhesion molecule nectin-like 4 in testis and can cause male infertility.Molecular and cellular biology · 2011Article
- Structural protein 4.1R is integrally involved in nuclear envelope protein localization, centrosome-nucleus association and transcriptional signaling.Journal of cell science · 2011Article
- Comprehensive characterization of expression patterns of protein 4.1 family members in mouse adrenal gland: implications for functions.Histochemistry and cell biology · 2010Article
- Rolly protein (ROLP)-Epb4.1/3: a potential protein-protein interaction relevant for the maintenance of cell adhesion.International journal of molecular sciences · 2009Article
- A Golgi-associated protein 4.1B variant is required for assimilation of proteins in the membrane.Journal of cell science · 2009Article
- Inhibition of protein 4.1 R and NuMA interaction by mutagenization of their binding-sites abrogates nuclear localization of 4.1 R.Clinical and translational science · 2009Article
- Protein 4.1R self-association: identification of the binding domain.The Biochemical journal · 2006Article
- Cell cycle-dependent nucleocytoplasmic shuttling of the neurofibromatosis 2 tumour suppressor merlin.Oncogene · 2005Article
- Mutagenesis of the phosphatidylinositol 4,5-bisphosphate (PIP(2)) binding site in the NH(2)-terminal domain of ezrin correlates with its altered cellular distribution.The Journal of cell biology · 2000Article
- Protein 4.1 R-135 interacts with a novel centrosomal protein (CPAP) which is associated with the gamma-tubulin complex.Molecular and cellular biology · 2000Article
- The N-terminal 209-aa domain of high molecular-weight 4.1R isoforms abrogates 4.1R targeting to the nucleus.Proceedings of the National Academy of Sciences of the United States of America · 1999Article
- Deciphering the nuclear import pathway for the cytoskeletal red cell protein 4.1R.Molecular biology of the cell · 1999Article
- Protein 4.1R-deficient mice are viable but have erythroid membrane skeleton abnormalities.The Journal of clinical investigation · 1999Article
- Communication between the cell membrane and the nucleus: role of protein compartmentalization.Journal of cellular biochemistry. Supplement · 1998Review
- Structural protein 4.1 is located in mammalian centrosomes.Proceedings of the National Academy of Sciences of the United States of America · 1997Article
- Structural protein 4.1 in the nucleus of human cells: dynamic rearrangements during cell division.The Journal of cell biology · 1997Article
- Role of tissue specific alternative pre-mRNA splicing in the differentiation of the erythrocyte membrane.Transactions of the American Clinical and Climatological Association · 1997Review
- Protein 4.1 is a component of the nuclear matrix of mammalian cells.The Biochemical journal · 1995Article
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Although protein 4.1 was originally identified as an element of the erythrocyte membrane skeleton, its presence in most mammalian cell types is now well described. Antibodies raised against erythrocyte protein 4.1 or synthetic peptides corresponding to the spectrin-actin-binding domain of protein 4.1 react with plasma membranes and, unexpectedly, nuclei of different cell types. Nuclear staining was further confirmed in isolated nuclei prepared from rat liver and human leukaemic cell lines. Immunoblot analysis of subcellular fractions derived from these cells revealed three prominent proteins, of 80, 135 and 145 kDa. The structural relationship of the high-molecular-mass proteins with erythrocyte protein 4.1 was demonstrated by peptide mapping. These results indicate that mammalian nucleated cells contain several isoforms of erythrocyte protein 4.1 and that some high-molecular-mass forms may primarily reside in the nucleus.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.