Výsledky vyhledávání - "K H Scheidtmann"

Simian virus 40 large T antigen induces or activates a protein kinase which phosphorylates the transformation-associated protein p53

Autor: A Haber, K H Scheidtmann

Publikováno v: Journal of Virology. 64:672-679

The cellular phosphoprotein p53 is presumably involved in simian virus 40 (SV40)-induced transformation. We have monitored changes in the state of phosphorylation of p53 from normal versus SV40-infected or -transformed cells. In normal cells, p 53 wa

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9b2148a3f849c3cec7f592a301b0ca80
https://doi.org/10.1128/jvi.64.2.672-679.1990

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Novel phosphorylation of histone H3 at threonine 11 that temporally correlates with condensation of mitotic and meiotic chromosomes in plant cells

Autor: Twan Rutten, K H Scheidtmann, Dmitri Demidov, Andreas Houben

Publikováno v: Cytogenetic and genome research. 109(1-3)

A novel mitosis-specific phosphorylation site in histone H3 at threonine 11 has been described for mammalian cells. This modification is restricted to the centromeric region while phosphorylation at the classical H3 sites, Ser10 and Ser28 occurs alon

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f81037df5b8cf5f46a6dad30b494d1c6
https://pubmed.ncbi.nlm.nih.gov/15753571

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AATF, a novel transcription factor that interacts with Dlk/ZIP kinase and interferes with apoptosis

Autor: G, Page, I, Lödige, D, Kögel, K H, Scheidtmann

Publikováno v: FEBS letters. 462(1-2)

Dlk, also known as ZIP kinase, is a serine/threonine kinase that is tightly associated with nuclear structures. Under certain conditions, which require cytoplasmic localization, Dlk can induce apoptosis. In search for interaction partners that might

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::45040f0b3f33bbcb4b58e7c74249acd5
https://pubmed.ncbi.nlm.nih.gov/10580117

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Increased oncogenicity of subclones of SV40 large T-induced neuroectodermal tumor cell lines after loss of large T expression and concomitant mutation in p53

Autor: H, Salewski, T A, Bayer, U, Eidhoff, U, Preuss, S, Weggen, K H, Scheidtmann

Publikováno v: Cancer research. 59(8)

A model for medulloblastoma-like primitive neuroectodermal tumors was established in rat using retrovirally transduced SV40 large T antigen (LT) as an inducing agent (O. D. Wiestler et al., Brain Pathol., 2: 47-59, 1992). A cell line isolated from su

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::d7259a472a3461657dc4a3bae0f13d33
https://pubmed.ncbi.nlm.nih.gov/10213510

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Differential effects of phosphorylation of rat p53 on transactivation of promoters derived from different p53 responsive genes

Autor: M, Lohrum, K H, Scheidtmann

Publikováno v: Oncogene. 13(12)

The tumor suppressor protein p53 is phosphorylated at multiple sites in the amino-terminal transactivation domain and at several sites in the carboxy-terminal region. Phosphorylation appears to modulate its DNA binding activity. Here we demonstrate t

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::4479c9e65da503182f284a7050802b6a
https://pubmed.ncbi.nlm.nih.gov/9000127

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Complex regulation of the DNA-binding activity of p53 by phosphorylation: differential effects of individual phosphorylation sites on the interaction with different binding motifs

Autor: D, Hecker, G, Page, M, Lohrum, S, Weiland, K H, Scheidtmann

Publikováno v: Oncogene. 12(5)

The tumor suppressor protein p53 exists in different phosphorylation states depending on the cellular environment and perhaps the stage of the cell cycle. These different phosphorylation states can be mimicked in the baculovirus expression system by

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::c5dd652e0151d32d2bd5b22567555eaf
https://pubmed.ncbi.nlm.nih.gov/8649812

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Purification and characterization of a protein kinase which is activated by SV40 large T-antigen and phosphorylates the tumor suppressor protein p53

Autor: E, Müller, K H, Scheidtmann

Publikováno v: Oncogene. 10(6)

In SV40-transformed or infected rat cells phosphorylation of the tumor suppressor protein p53 is enhanced due to activation of kinases. At least three different kinases can be co-precipitated with p53-large T (LT) immune complexes, casein kinase II r

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::9e333430431631d428b03c01afafd8bc
https://pubmed.ncbi.nlm.nih.gov/7700642

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Characterization of protein kinase activities associated with p53-large-T immune complexes from SV40-transformed rat cells

Autor: E, Müller, B, Boldyreff, K H, Scheidtmann

Publikováno v: Oncogene. 8(8)

Interaction of viral oncoproteins, such as SV40 large T, with cellular growth suppressor proteins Rb and p53 is presumed to inactive or modulate their growth suppression functions, thereby leading to transformation. An additional transformation-relat

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::9e46fbcde1c0179b3c1bf65276b7a56e
https://pubmed.ncbi.nlm.nih.gov/8393163

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Phosphorylation of threonine in the proline-rich carboxy-terminal region of simian virus 40 large T antigen

Autor: Gernot Walter, A Carbone, K H Scheidtmann, A Kaiser

Publikováno v: Journal of Virology. 38:59-69

The position of phosphothreonine in the predicted primary structure of simian virus 40 large T antigen was determined by different methods. After digestion of large T antigen with trypsin and subsequent two-dimensional peptide mapping, a single pepti

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::070c55de530f4d0d3bff7472d374e96e
https://doi.org/10.1128/jvi.38.1.59-69.1981

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DNA-binding activity of simian virus 40 large T antigen correlates with a distinct phosphorylation state

Autor: Gernot Walter, B Echle, K H Scheidtmann, M Hardung

Publikováno v: Journal of Virology. 50:1-12

The state of phosphorylation and the relationship of various subclasses of simian virus 40 large T antigen (large T) differing in DNA-binding activity, degree of oligomerization, age, and subcellular distribution were investigated. Young large T (con

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e3efe888bcf837da3159be4ebf2a2a3e
https://doi.org/10.1128/jvi.50.1.1-12.1984

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