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Binding of the protein disulfide isomerase isoform ERp60 to the nuclear matrix-associated regions of DNA
scientific article published on 01 March 1999
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PubMed publication ID
10022612
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title
Binding of the protein disulfide isomerase isoform ERp60 to the nuclear matrix-associated regions of DNA
(English)
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PubMed publication ID
10022612
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10 November 2019
author
Fabio Altieri
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2
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PubMed publication ID
10022612
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10 November 2019
author name string
A Ferraro
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1
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PubMed publication ID
10022612
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S Coppari
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3
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10022612
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10 November 2019
M Eufemi
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4
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S Chichiarelli
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5
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10022612
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10 November 2019
C Turano
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6
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10022612
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publication date
1 March 1999
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PubMed publication ID
10022612
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10 November 2019
published in
Journal of Cellular Biochemistry
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10022612
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10 November 2019
volume
72
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PubMed publication ID
10022612
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10 November 2019
issue
4
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PubMed publication ID
10022612
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10 November 2019
page(s)
528-539
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PubMed publication ID
10022612
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10 November 2019
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The nuclear lamina is a meshwork of intermediate-type filaments
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The nuclear matrix: a heuristic model for investigating genomic organization and function in the cell nucleus
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cDNA cloning and baculovirus expression of the human liver endoplasmic reticulum P58: characterization as a protein disulfide isomerase isoform, but not as a protease or a carnitine acyltransferase
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Chromosomal loop anchorage of the kappa immunoglobulin gene occurs next to the enhancer in a region containing topoisomerase II sites
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Characterization of the active site cysteine residues of the thioredoxin-like domains of protein disulfide isomerase.
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Nucleolin is a matrix attachment region DNA-binding protein that specifically recognizes a region with high base-unpairing potential
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The thiol-dependent reductase ERp57 interacts specifically with N-glycosylated integral membrane proteins
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Crosslinking of nuclear proteins to DNA by cis-diamminedichloroplatinum in intact cells. Involvement of nuclear matrix proteins
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Comparison of DNA-protein interactions in intact nuclei from avian liver and erythrocytes: a cross-linking study
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A c-erb-A binding site in rat growth hormone gene mediates trans-activation by thyroid hormone.
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Binding specificity of a nuclear scaffold: supercoiled, single-stranded, and scaffold-attached-region DNA.
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Binding of matrix attachment regions to lamin polymers involves single-stranded regions and the minor groove
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Erp61 is GRP58, a stress-inducible luminal endoplasmic reticulum protein, but is devoid of phosphatidylinositide-specific phospholipase C activity
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Organization of the higher-order chromatin loop: specific DNA attachment sites on nuclear scaffold
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The structure of an oligo(dA).oligo(dT) tract and its biological implications
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An isoform of protein disulfide isomerase is expressed in the developing acrosome of spermatids during rat spermiogenesis and is transported into the nucleus of mature spermatids and epididymal spermatozoa
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Purification and molecular cloning of the scaffold attachment factor B (SAF-B), a novel human nuclear protein that specifically binds to S/MAR-DNA
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Nuclear localisation of calreticulin in vivo is enhanced by its interaction with glucocorticoid receptors
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21 January 2018
Regulation of transcription-factor activity during growth and differentiation: involvement of the nuclear matrix in concentration and localization of promoter binding proteins
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The nucleus: A black box being opened
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Nuclear matrix association of multiple sequence-specific DNA binding activities related to SP-1, ATF, CCAAT, C/EBP, OCT-1, and AP-1.
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Intracellular localization of heat shock proteins in Drosophila
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A matrix/scaffold attachment region binding protein: Identification, purification, and mode of binding
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Chicken MAR binding protein p120 is identical to human heterogeneous nuclear ribonucleoprotein (hnRNP) U.
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Crystal structures of reduced, oxidized, and mutated human thioredoxins: evidence for a regulatory homodimer
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Binding of matrix attachment regions to nuclear lamin is mediated by the rod domain and depends on the lamin polymerization state.
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Identifiers
DOI
10.1002/(SICI)1097-4644(19990315)72:4<528::AID-JCB8>3.0.CO;2-V
1 reference
stated in
Europe PubMed Central
PubMed publication ID
10022612
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10022612%20AND%20SRC:MED&resulttype=core&format=json
retrieved
10 November 2019
PubMed publication ID
10022612
1 reference
stated in
Europe PubMed Central
PubMed publication ID
10022612
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10022612%20AND%20SRC:MED&resulttype=core&format=json
retrieved
10 November 2019
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