Priv.-Doz. Dr. rer. nat.
Marcus Nalaskowski
  • Scientist
Working area


N45 Rothe-Geussenhainer-Haus, 3rd Floor, Room number 306d
German (Mother tongue)



Tubulin Tyrosine Ligase Like 4 (TTLL4) overexpression in breast cancer cells is associated with brain metastasis and alters exosome biogenesis
Arnold J, Schattschneider J, Blechner C, Krisp C, Schlüter H, Schweizer M, Nalaskowski M, Oliveira-Ferrer L, Windhorst S
J EXP CLIN CANC RES. 2020;39(1):205.


Analysis of the FLVR motif of SHIP1 and its importance for the protein stability of SH2 containing signaling proteins
Ehm P, Lange F, Hentschel C, Jepsen A, Glück M, Nelson N, Bettin B, de Bruyn Kops C, Kirchmair J, Nalaskowski M, Jücker M
CELL SIGNAL. 2019;63:109380.

A novel 6-pyrophosphorylating IP6 kinase (IP6-6K) discovered in the protozoon Trichomonas vaginalis
Wundenberg T, Nalaskowski M, Löser B, Fanick W, Hackl T, Fürnkranz U, Rehbach C, Lin H, Mayr G
MOL BIOCHEM PARASIT. 2019;227:53-63.

A toolkit for expression of Strep-tagged enhanced green fluorescent protein concatemers in mammalian cells
Zweifel A, Giehler S, Nalaskowski M
ANAL BIOCHEM. 2019;586:113430.


Effect of the actin- and calcium-regulating activities of ITPKB on the metastatic potential of lung cancer cells
Bäder S, Glaubke E, Grüb S, Muhs S, Wellbrock J, Nalaskowski M, Lange T, Windhorst S
BIOCHEM J. 2018;475(12):2057-2071.

Nuclear accumulation of SHIP1 mutants derived from AML patients leads to increased proliferation of leukemic cells
Nalaskowski M, Ehm P, Rehbach C, Nelson N, Täger M, Modest K, Jücker M
CELL SIGNAL. 2018;49:87-94.


A set of enhanced green fluorescent protein concatemers for quantitative determination of nuclear localization signal strength.
Böhm J, Thavaraja R, Giehler S, Nalaskowski M
ANAL BIOCHEM. 2017;533:48-55.

Strong fascin expression promotes metastasis independent of its F-actin bundling activity
Heinz L, Muhs S, Schiewek J, Grüb S, Nalaskowski M, Lin Y, Wikman H, Oliveira-Ferrer L, Lange T, Wellbrock J, Konietzny A, Mikhaylova M, Windhorst S
ONCOTARGET. 2017;8(66):110077-110091.

SHIP1, but not an AML-derived SHIP1 mutant, suppresses myeloid leukemia growth in a xenotransplantation mouse model
Täger M, Horn S, Latuske E, Ehm P, Schaks M, Nalaskowski M, Fehse B, Fiedler W, Stocking C, Wellbrock J, Jücker M
GENE THER. 2017;24(11):749-753.


The tumor suppressor SHIP1 colocalizes in nucleolar cavities with p53 and components of PML nuclear bodies
Ehm P, Nalaskowski M, Wundenberg T, Jücker M
NUCLEUS-PHILA. 2015;6(2):154-64.


Efficacious inhibition of Importin α/β-mediated nuclear import of human inositol phosphate multikinase
Kublun I, Ehm P, Brehm M, Nalaskowski M
BIOCHIMIE. 2014;102:117-23.


Dissection of cell cycle-dependent dynamics of Dnmt1 by FRAP and diffusion-coupled modeling
Schneider K, Fuchs C, Dobay A, Rottach A, Qin W, Wolf P, Álvarez-Castro J, Nalaskowski M, Kremmer E, Schmid V, Leonhardt H, Schermelleh L
NUCLEIC ACIDS RES. 2013;41(9):4860-76.


A novel Entamoeba histolytica inositol phosphate kinase catalyzes the formation of 5PP-Ins(1,2,3,4,6)P(5)
Löser B, Nalaskowski M, Fanick W, Lin H, Tannich E, Mayr G
MOL BIOCHEM PARASIT. 2012;181(1):49-52.

Nucleocytoplasmic shuttling of human inositol phosphate multikinase is influenced by CK2 phosphorylation.
Meyer R, Nalaskowski M, Ehm P, Schröder C, Naj X, Brehm M, Mayr G
BIOL CHEM. 2012;393(3):149-160.

A toolkit for graded expression of green fluorescent protein fusion proteins in mammalian cells.
Nalaskowski M, Ehm P, Giehler S, Mayr G
ANAL BIOCHEM. 2012;428(1):24-27.

The inositol 5-phosphatase SHIP1 is a nucleo-cytoplasmic shuttling protein and enzymatically active in cell nuclei.
Nalaskowski M, Metzner A, Brehm M, Labiadh S, Brauer H, Grabinski N, Mayr G, Jücker M
CELL SIGNAL. 2012;24(3):621-628.

A Plasmodium multi-domain protein possesses multiple inositol phosphate kinase activities.
Stritzke C, Nalaskowski M, Fanick W, Lin H, Mayr G
MOL BIOCHEM PARASIT. 2012;186(2):134-138.


Human inositol 1,4,5-trisphosphate 3-kinase isoform B (IP3KB) is a nucleocytoplasmic shuttling protein specifically enriched at cortical actin filaments and at invaginations of the nuclear envelope.
Nalaskowski M, Fliegert R, Ernst O, Brehm M, Fanick W, Windhorst S, Lin H, Giehler S, Hein J, Lin Y, Mayr G
J BIOL CHEM. 2011;286(6):4500-4510.


Ins(1,4,5)P3 3-kinase-A overexpression induces cytoskeletal reorganization via a kinase-independent mechanism.
Windhorst S, Blechner C, Lin H, Elling C, Nalaskowski M, Kirchberger T, Guse A, Mayr G
BIOCHEM J. 2008;414(3):407-417.


Intracellular localization of human Ins(1,3,4,5,6)P5 2-kinase.
Brehm M, Schenk T, Zhou X, Fanick W, Lin H, Windhorst S, Nalaskowski M, Kobras M, Shears S, Mayr G
BIOCHEM J. 2007;408(3):335-345.

Nuclear localization of enhanced green fluorescent protein homomultimers.
Seibel N, Eljouni J, Nalaskowski M, Hampe W
ANAL BIOCHEM. 2007;368(1):95-99.


Subcellular localisation of human inositol 1,4,5-trisphosphate 3-kinase C: species-specific use of alternative export sites for nucleo-cytoplasmic shuttling indicates divergent roles of the catalytic and N-terminal domains.
Nalaskowski M, Windhorst S, Stockebrand M, Mayr G
BIOL CHEM. 2006;387(5):583-593.


The families of kinases removing the Ca2+ releasing second messenger Ins(1,4,5)P3.
Nalaskowski M, Mayr G
CURR MOL MED. 2004;4(3):277-290.


Rat inositol 1,4,5-trisphosphate 3-kinase C is enzymatically specialized for basal cellular inositol trisphosphate phosphorylation and shuttles actively between nucleus and cytoplasm.
Nalaskowski M, Bertsch U, Fanick W, Stockebrand M, Schmale H, Mayr G
J BIOL CHEM. 2003;278(22):19765-19776.


The human homologue of yeast ArgRIII protein is an inositol phosphate multikinase with predominantly nuclear localization.
Nalaskowski M, Deschermeier C, Fanick W, Mayr G
BIOCHEM J. 2002;366(2):549-556.

Letzte Aktualisierung aus dem FIS: 15.04.2024 - 06:36 Uhr