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1

ERp57/GRP58: A protein with multiple functions

100%
Turano C., Gaucci E., Grillo C., Chichiarelli S.
Cellular and Molecular Biology Letters
|
2011
|
tom 16
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nr 4
The protein ERp57/GRP58 is a stress-responsive protein and a component of the protein disulfide isomerase family. Its functions in the endoplasmic reticulum are well known, concerning mainly the proper folding and quality control of glycoproteins, and participation in the assembly of the major histocompatibility complex class 1. However, ERp57 is present in many other subcellular locations, where it is involved in a variety of functions, primarily suggested by its participation in complexes with other proteins and even with DNA. While in some instances these roles need to be confirmed by further studies, a great number of observations support the participation of ERp57 in signal transduction from the cell surface, in regulatory processes taking place in the nucleus, and in multimeric protein complexes involved in DNA repair.
2

Nuclear matrix localization of chicken HSP108

100%
Altieri F., Eufemi M., Maras B., Turano C.
Cellular and Molecular Biology Letters
|
1997
|
tom 02
|
nr 4
A glycoprotein purified from the internal nuclear matrix of chicken liver nuclei has been identified, by partial sequencing and by Western blotting, as hsp108, which is a component of the hsp90 superfamily. This protein has been previously characterized as a protein which copurifies with the cytoplasmic progesterone receptor and as a transferrin-binding protein of the chicken oviduct cell membrane. We have found that hsp108 is present in the nuclear matrix even in the absence of a heat shock or of other noxious conditions. Some of the properties already described for its homologous proteins (endoplasmin, grp94, hsp100) might explain its function at the nuclear matrix level. Hsp108 isolated from the liver nuclear matrix has a carbohydrate composition significantly different from that of the protein of the oviduct cell membrane.
3

DNA-nuclear matrix interactions analyzed by cross-linking reactions in intact nuclei from avian liver

88%
Ferraro A., Eufemi M., Cervoni L., Altieri F., Turano C.
Acta Biochimica Polonica
|
1995
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tom 42
|
nr 2
To detect the interactions of DNA with the nuclear matrix proteins, DNA-protein cross-linkages were induced in intact nuclei from chicken liver by the use of ds-diammine dichloroplatinum. Methods have been devised for fast purification both of the proteins and of the DNA fragments involved in the cross-linked complexes. By Southern-Western blotting a number of matrix proteins isolated from the complexes have been shown to recognize specifically DNA sequences present in the cross-linked DNA fragments. This experimental approach not only allows to identify the nuclear matrix-DNA interactions existing in the nucleus before its disruption, but also provides a preparation of matrix proteins enriched in those species which are involved in such interactions and which can therefore be detected with high sensitivity.
4

Detection of novel DNA-nuclear matrix interactions

76%
Ferraro A., Altieri F., Cervoni L., Eufemi M., Coppari S., Turano C.
Cellular and Molecular Biology Letters
|
1997
|
tom 02
|
nr 2
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