Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Catherine Korsgren"'
Autor:
Catherine Korsgren, Samuel E. Lux
Publikováno v:
Blood. 116:2600-2607
Spectrin and protein 4.1R crosslink F-actin, forming the membrane skeleton. Actin and 4.1R bind to one end of β-spectrin. The adjacent end of α-spectrin, called the EF domain, is calmodulin-like, with calcium-dependent and calcium-independent EF ha
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::63725ef2ab4fb7f3b3d71133ab2e2e6a
https://doi.org/10.1182/blood-2009-12-260612
https://doi.org/10.1182/blood-2009-12-260612
Autor:
William T. Tse, Babette Gwynn, Kathryn M. John, Ou Jin, Samuel E. Lux, Ju Tang, Catherine Korsgren, Luanne L. Peters, Andrew L. Kung
Publikováno v:
Journal of Biological Chemistry. 276:23974-23985
We isolated cDNAs that encode a 77-kDa peptide similar to repeats 10-16 of beta-spectrins. Its gene localizes to human chromosome 19q13.13-q13.2 and mouse chromosome 7, at 7.5 centimorgans. A 289-kDa isoform, similar to full-length beta-spectrins, wa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e0afd272adfc19dcb835f019471bf148
https://doi.org/10.1074/jbc.m009307200
https://doi.org/10.1074/jbc.m009307200
Publikováno v:
Experimental Cell Research. 229:421-431
Band 4.2 (pallidin) is a major erythrocyte membrane protein which has been detected in a number of nonerythroid cell types. Increasing evidence suggests that band 4.2 is involved in maintaining membrane stability in the erythrocyte. For example, band
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5bbdb8e407e9f805a946f902ce0465ce
https://doi.org/10.1006/excr.1996.0387
https://doi.org/10.1006/excr.1996.0387
Autor:
Elizabeth Dotimas, Anser C. Azim, Athar H. Chishti, Catherine Korsgren, Carl M. Cohen, Shirin M. Marfatia
Publikováno v:
Biochemistry. 35:3001-3006
Dematin and protein 4.2 are peripheral membrane proteins associated with the cytoplasmic surface of the human erythrocyte plasma membrane. Isoforms of dematin and protein 4.2 exist in many nonerythroid cells. In solution, dematin is a trimeric protei
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::62a16d2aba9038f7b49a0c97e61142cb
https://doi.org/10.1021/bi951745y
https://doi.org/10.1021/bi951745y
Autor:
Catherine Korsgren, Cafl M. Cohen
Publikováno v:
Genomics. 21:478-485
Band 4.2, which plays an important but poorly understood role in erythrocyte function and survival, is a major component of erythrocyte membranes. Recently, it has been shown that the gene for murine protein band 4.2 colocalizes on chromosome 2 with
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a9a36a38664df829e4ff0e5e4e2049a2
https://doi.org/10.1006/geno.1994.1304
https://doi.org/10.1006/geno.1994.1304
Publikováno v:
The Journal of biological chemistry. 285(7)
Spectrin and protein 4.1 cross-link F-actin protofilaments into a network called the membrane skeleton. Actin and 4.1 bind to one end of beta-spectrin. The adjacent end of alpha-spectrin, called the EF-domain, is calmodulin-like, with calcium-depende
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::daa1bb9df8e88bbc96a191d6a7ccff9e
https://pubmed.ncbi.nlm.nih.gov/20007969
https://pubmed.ncbi.nlm.nih.gov/20007969
Autor:
Catherine Korsgren, Carl M. Cohen
Publikováno v:
Proceedings of the National Academy of Sciences. 88:4840-4844
Human erythrocyte band 4.2 is a major membrane-associated protein with an important, but still undefined, role in erythrocyte survival. We previously sequenced the complete cDNA for band 4.2 and showed that the protein has a strong sequence identity
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::283b302287e80e82258b5498a25c361a
https://doi.org/10.1073/pnas.88.11.4840
https://doi.org/10.1073/pnas.88.11.4840
Publikováno v:
Proceedings of the National Academy of Sciences. 87:613-617
The complete amino acid sequence for human erythrocyte band 4.2 has been derived from the nucleotide sequence of a full-length 2.35-kilobase (kb) cDNA. The 2.35-kb cDNA was isolated from a human reticulocyte cDNA library made in the expression vector
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::75de453cb2142a07e72d0cec81a02920
https://doi.org/10.1073/pnas.87.2.613
https://doi.org/10.1073/pnas.87.2.613
Autor:
Carl M. Cohen, Catherine Korsgren, Luanne L. Peters, Linda R. Adkison, Samuel E. Lux, Robert A. White
Publikováno v:
Nature genetics. 2(1)
Pallid is one of 12 independent murine mutations with a prolonged bleeding time that are models for human platelet storage pool deficiencies in which several intracellular organelles are abnormal. We have mapped the murine gene for protein 4.2 (Epb4.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::175907144f9f46bf878cd6920f01f06c
https://pubmed.ncbi.nlm.nih.gov/1284644
https://pubmed.ncbi.nlm.nih.gov/1284644
Publikováno v:
Blood. 106:810-810
The red blood cell (RBC) membrane skeleton is composed principally of short F-actin filaments crosslinked by α2β2-spectrin tetramers with the assistance of protein 4.1R. Actin and 4.1R bind to the actin-binding domain (βABD) at the N-terminus of t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2ebfb248e902444b5b3172ceb5b0d634
https://doi.org/10.1182/blood.v106.11.810.810
https://doi.org/10.1182/blood.v106.11.810.810