A. Østvold

发表

NUCKS1 is a novel RAD51AP1 paralog important for homologous recombination and genome stability

N. Sharma, P. Sung, D. Schild, 2015, Nucleic acids research.

Cytoplasmic retention of peroxide‐activated ERK provides survival in primary cultures of rat hepatocytes

E. Skarpen, M. Oksvold, H. Huitfeldt, 2005, Hepatology.

NUCKS1 is a highly modified, chromatin-associated protein involved in a diverse set of biological and pathophysiological processes.

C. Wiese, K. Grundt, A. Østvold, 2022, The Biochemical journal.

NUCKS1 is a novel RAD51AP1 paralog important for homologous recombination and genome stability

N. Sharma, P. Sung, D. Schild, 2015, Nucleic acids research.

Nondysplastic Ulcerative Colitis Has High Levels of the Homologous Recombination Repair Protein NUCKS1 and Low Levels of the DNA Damage Marker Gamma-H2AX.

H. Huitfeldt, A. Østvold, A. Schjølberg, 2018, Inflammatory bowel diseases.

A putative DNA-binding domain in the NUCKS protein.

H. Huitfeldt, T. Skauge, H. Anthonsen, 2002, Archives of biochemistry and biophysics.

Degradation of the Type I Inositol 1,4,5‐Trisphosphate Receptor by Caspase‐3 in SH‐SY5Y Neuroblastoma Cells Undergoing Apoptosis

S. Walaas, A. Østvold, L. Haug, 2000, Journal of neurochemistry.

Analysis of Protein Phosphorylation in Intact Cells and Extracts

S. Walaas, A. Østvold, 1997 .

HMG 17 in metaphase‐arrested and interphase HeLa S3 cells

T. Kristensen, K. Sletten, S. Laland, 1981, FEBS letters.

Phosphorylation of the Inositol 1,4,5-Trisphosphate Receptor by Cyclic Nucleotide-dependent Kinases in Vitroand in Rat Cerebellar Slices in Situ *

V. Jensen, Ø. Hvalby, S. Walaas, 1999, The Journal of Biological Chemistry.

UV induces tyrosine kinase-independent internalisation and endosome arrest of the EGF receptor.

E. Skarpen, M. Oksvold, H. Huitfeldt, 2002, Journal of cell science.

NUCKS overexpression in breast cancer

C. Kittas, P. Kollia, S. Havaki, 2009, Cancer Cell International.

Nucks1 synergizes with Trp53 to promote radiation lymphomagenesis in mice

D. Schild, K. Jen, C. Wiese, 2016, Oncotarget.

Identification of kinases phosphorylating 13 sites in the nuclear, DNA-binding protein NUCKS.

B. Thiede, K. Grundt, A. Østvold, 2017, Biochimica et biophysica acta. Proteins and proteomics.

Characterisation of the NUCKS gene on human chromosome 1q32.1 and the presence of a homologous gene in different species.

K. Grundt, A. Østvold, Y. Drosos, 2004, Biochemical and biophysical research communications.

p23, a novel mammalian nucleic acid‐binding protein with homology to the yeast ribosomal protein YL43

K. Sletten, A. Østvold, I. Hullstein, 1992, FEBS letters.

Nuclear receptor and apoptosis initiator NGFI-B is a substrate for kinase ERK2.

R. Paulsen, Åsa B Fallgren, A. Østvold, 2002, Biochemical and biophysical research communications.

Intracerebroventricular administration of quinolinic acid induces a selective decrease of inositol(1,4,5)-trisphosphate receptor in rat brain

S. Walaas, A. Østvold, L. Dvořáková, 1998, Neurochemistry International.

Type I Inositol (1,4,5) Trisphosphate Receptor and Phosphate-Activated Glutaminase are Highly Enriched in Neurons as Compared to Glial Cells in Rat Neostriatum

S. Walaas, A. Østvold, I. Torgner, 1997 .

Reduced [3H]IP3 binding but unchanged IP3 receptor levels in the rat hippocampus CA1 region following transient global ischemia and tolerance induction

N. Diemer, C. Dahl, A. Østvold, 2000, Neurochemistry International.

On the presence of poly(ADP‐ribose) polymerase activity in metaphase chromosomes from HeLa S3 cells

T. Kristensen, S. Laland, A. Østvold, 1980, FEBS letters.

Molecular cloning of a mammalian nuclear phosphoprotein NUCKS, which serves as a substrate for Cdk1 in vivo.

J. Norum, K. Grundt, A. Østvold, 2001, European journal of biochemistry.

Behaviour of endogenous and newly absorbed serotonin in the platelet release reaction.

H. Holmsen, A. Østvold, A. Ostvold, 1973, Biochemical pharmacology.

A novel, highly phosphorylated protein, of the high-mobility group type, present in a variety of proliferating and non-proliferating mammalian cells.

S. Laland, A. Østvold, A. Ostvold, 1985, European journal of biochemistry.

Heterodimerization of the epidermal-growth-factor (EGF) receptor and ErbB2 and the affinity of EGF binding are regulated by different mechanisms.

L. E. Johannessen, I. Madshus, E. Stang, 2001, The Biochemical journal.