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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Vitellogenin B1

vitellogenin B1
Top mentioned proteins: fibrillin-1, ACID, pS2, HAD, Estrogen Receptor
Papers on vitellogenin B1
Degradation of M(r) 25,000 protein by cathepsin L-like protease in Xenopus laevis oocytes.
Hashimoto et al., Yonago, Japan. In Protein J, 2014
A phosphorylated protein with a molecular mass of 25,000 (pp25) is involved in Xenopus laevis vitellogenin B1 and partially overlaps with phosvitin and lipovitellin 2. The protease responsible for pp25 degradation was studied in vitro since this occurs during embryogenesis.
Cellular distribution of Mr 25,000 protein, a protein partially overlapping phosvitin and lipovitellin 2 in vitellogenin B1, and yolk proteins in Xenopus laevis oocytes and embryos.
Hashimoto et al., Yonago, Japan. In Comp Biochem Physiol A Mol Integr Physiol, 2007
A phosphorylated protein with molecular mass of 25,000 (pp25) can be derived from Xenopus laevis vitellogenin B1.
Different modulation of ER-mediated transactivation by xenobiotic nuclear receptors depending on the estrogen response elements and estrogen target cell types.
Min, Chinju, South Korea. In Ann N Y Acad Sci, 2006
Accordingly, this article further examined the effects of the endogenous vitellogenin B1 estrogen responsive promotor on the SXR- and PPAR-gamma-modulated ER transactivation in Hep G2, and either dose-dependent or single dose effects of SXR, PPAR-gamma, and CAR in two different breast cancer cell lines and the ovarian-derived cell line respectively, on the ER-mediated transactivation of the synthetic (4ERE)-tk-luciferase reporter.
Modulation of protein phosphorylation by Mr 25,000 protein partially overlapping phosvitin and lipovitellin 2 in Xenopus laevis vitellogenin B1 protein.
GeneRIF
Hashimoto et al., Yonago, Japan. In Protein J, 2006
results suggest that pp25 may have a role as an inhibitory modulator of some protein phosphorylation in Xenopus oocytes and embryos
Mass-spectrometric identification of binding proteins of Mr 25,000 protein, a part of vitellogenin B1, detected in particulate fraction of Xenopus laevis oocytes.
Hashimoto et al., Yonago, Japan. In Protein J, 2004
A phosphorylated protein with molecular mass of 25,000 (pp25) is a component of Xenopus laevis vitellogenin B1.
Purification and characterization of Mr 43,000 protein similar to Mr 25,000 protein, a substrate for protein Ser/Thr kinases, identified as a part of Xenopus laevis vitellogenin B1.
Hashimoto et al., Yonago, Japan. In J Protein Chem, 2003
Mr 25,000 protein (pp25), a substrate for protein Ser/Thr kinases, was recently shown to consist of a portion of the Xenopus laevis vitellogenin B1 protein.
Mr 25 000 protein, a substrate for protein serine/threonine kinases, is identified as a part of Xenopus laevis vitellogenin B1.
Hashimoto et al., Yonago, Japan. In Dev Growth Differ, 2003
A phosphorylated protein with a molecular mass of 25 000 (pp25) previously purified from the cytosolic fraction of Xenopus laevis oocytes is an effective phosphate acceptor for casein kinases and protein kinase C. In this study, based on the partial amino acid sequence of pp25, a cDNA was isolated that encodes a new yolk precursor protein, Xenopus vitellogenin B1, which contained the sequence encoding pp25.
Inhibitory cross-talk between estrogen receptor (ER) and constitutively activated androstane receptor (CAR). CAR inhibits ER-mediated signaling pathway by squelching p160 coactivators.
Kemper et al., Urbana, United States. In J Biol Chem, 2002
Of these receptors, CAR substantially inhibited ER-mediated transcriptional activity of the vitellogenin B1 promoter as well as a synthetic estrogen responsive element (ERE)-containing promoter.
Estrogen response elements alter coactivator recruitment through allosteric modulation of estrogen receptor beta conformation.
Nardulli et al., Urbana, United States. In J Biol Chem, 2001
Although the imperfect vitellogenin B1, pS2, and oxytocin (OT) EREs each differ from the consensus vitellogenin A2 ERE sequence by a single base pair, ERbeta activates transcription of reporter plasmids containing A2, pS2, B1, and OT EREs to different extents.
Interaction of estrogen receptors alpha and beta with estrogen response elements.
Nardulli et al., Urbana, United States. In Mol Cell Endocrinol, 2001
To understand how estrogen-responsive genes are regulated, we compared the abilities of estrogen receptors (ERs) alpha and beta to bind to and activate transcription through the consensus vitellogenin A2 ERE and the imperfect pS2, vitellogenin B1, and oxytocin (OT) EREs.
Allosteric modulation of estrogen receptor conformation by different estrogen response elements.
Nardulli et al., Urbana, United States. In Mol Endocrinol, 2001
We assessed the ability of the ER to activate transcription of reporter plasmids containing either the consensus vitellogenin A2 ERE or the imperfect pS2, vitellogenin B1, or oxytocin (OT) ERE.
Vigilin binding selectively inhibits cleavage of the vitellogenin mRNA 3'-untranslated region by the mRNA endonuclease polysomal ribonuclease 1.
Schoenberg et al., Columbus, United States. In Proc Natl Acad Sci U S A, 2000
The vigilin-binding site in the vitellogenin B1 mRNA 3'-UTR contains two consensus PMR-1 cleavage sites.
Determinants of vitellogenin B1 promoter architecture. HNF3 and estrogen responsive transcription within chromatin.
Wahli et al., Lausanne, Switzerland. In J Biol Chem, 2000
The liver-specific vitellogenin B1 promoter is efficiently activated by estrogen within a nucleosomal environment after microinjection into Xenopus laevis oocytes, consistent with the hypothesis that significant nucleosome remodeling over this promoter is not a prerequisite for the activation by the estrogen receptor (ERalpha).
Functional interaction between the estrogen receptor and CTF1: analysis of the vitellogenin gene B1 promoter in yeast.
Wahli et al., Lausanne, Switzerland. In Mol Endocrinol, 1998
When the natural estrogen-dependent vitellogenin B1 promoter is tested in yeast, CTF1 and CTF1-fusion proteins are unable to activate transcription, and no synergy is observed between hER, which activates the B1 promoter, and these factors.
Hormone induction of progesterone receptor (PR) messenger ribonucleic acid and activation of PR promoter regions in ovarian granulosa cells: evidence for a role of cyclic adenosine 3',5'-monophosphate but not estradiol.
Richards et al., Houston, United States. In Mol Endocrinol, 1998
Likewise, when a vector containing the consensus vitellogenin B1 gene estrogen response element (ERE) was transfected into differentiated granulosa cells, forskolin, but not E, induced activity.
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