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Department of Biochemistry and Molecular Biophysics

Department of Biochemistry & Molecular Biophysics
141 Chalmers Hall
1711 Claflin Rd.
Manhattan, KS 66506
785-532-7278 fax

Biotechnology Core Facility
206 Burt Hall
785-532-6297 fax

Biomolecular NMR Facility
37 Chalmers Hall

Anna Zolkiewska, Ph.D., Professor
Undergraduate Advisor

Complete Publications List

2020s | 2010s | 2000s | 1990s


Thevarajan, I., Zolkiewski, M., and Zolkiewska, A. (2020) Human CLPB forms ATP-dependent complexes in the mitochondrial intermembrane space. Int. J. Biochem. Cell Biol. 127, 105841

Romero, Y., Wise, R., and Zolkiewska, A. (2020) Proteolytic processing of PD-L1 by ADAM proteases in breast cancer cells. Cancer Immunology, Immunotherapy 69, 43-55

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Leutert, M., Menzel, S., Braren, R., Rissiek, B., Hopp, A. K., Nowak, K., Bisceglie, L., Gehrig, P., Li, H., Zolkiewska, A., Koch-Nolte, F., Hottiger, M. O. (2018) Proteomic characterization of the heart and skeletal muscle reveals widespread arginine ADP-ribosylation by the ARTC1 ectoenzyme. Cell Rep. 24, 1916-1929

Wise, R., and Zolkiewska A. (2017) Metalloprotease-dependent activation of EGFR modulates CD44+/CD24- populations in triple negative breast cancer cells through the MEK/ERK pathway. Breast Cancer Res. Treat. 166, 421-433

Duhachek-Muggy, S., Qi, Y., Wise, R., Alyahya, L., Li, H., Hodge, J., and Zolkiewska, A. (2017) Metalloprotease-disintegrin ADAM12 actively promotes the stem cell-like phenotype in claudin-low breast cancer. Molecular Cancer, 16:32

Wise R, Duhachek-Muggy S, Qi Y, Zolkiewski M, Zolkiewska A. Protein disulfide isomerases in the endoplasmic reticulum promote anchorage-independent growth of breast cancer cells. Breast Cancer Res Treat. 2016 Jun;157(2):241-252.

Duhachek-Muggy, S., and Zolkiewska, A. (2015) ADAM12-L is a direct target of the miR-29 and miR-200 families in breast cancer. BMC Cancer 15:93

Qi, Y., Duhachek-Muggy, S., Li, H., and Zolkiewska, A. (2014) Phenotypic diversity of breast cancer-related mutations in metalloproteinase-disintegrin ADAM 12. PLoS ONE. 9(3):e92536.

Ngansop, F., Li, H., Zolkiewska, A., and Zolkiewski, M. (2013) Biochemical characterization of the apicoplast-targeted AAA+ ATPase ClpB from Plasmodium falciparum. Biochem. Biophys. Res. Comm., 436(2):161-5.

Duhachek-Muggy, S., Li, H., Qi, Y., and Zolkiewska, A. (2013) Alternative mRNA splicing generates two distinct ADAM12 prodomain variants. PLoS ONE. 8(10):e75730.

Li, H., Duhachek-Muggy, S., and Zolkiewska, A. (2013) Metalloproteinase-disintegrin ADAM12 is associated with a breast tumor-initiating cell phenotype. Breast Cancer Res. Treat. 139, 691-703

Li, H., Duhachek-Muggy, S., Qi, Y., Hong, Y., Behbod, F., and Zolkiewska, A. (2012) An essential role of metalloprotease-disintegrin ADAM12 in triple-negative breast cancer. Breast Cancer Res. Treat., 135, 759-769.

Chen, J., and Zolkiewska, A. (2011) Force-induced unfolding simulations of the human Notch1 negative regulatory region: possible roles of the heterodimerization domain in mechanosensing.  PLoS One 6(7):e22837.

Li, H., Solomon, E., Duhachek-Muggy, S., Sun, D., and Zolkiewska, A. (2011) Metalloprotease-disintegrin ADAM12 expression is regulated by Notch signaling via microRNA-29.  J. Biol. Chem. 286, 21500-21510.

Fukada, S., Yamaguchi, M., Kokubo, H., Ogawa, R., Uezumi, A., Yoneda, T., Matev, MM., Motohashi, N., Ito, T., Zolkiewska, A., Johnson, RL., Saga, Y., Miyagoe-Suzuki, Y., Tsujikawa, K., Takeda, S., and Yamamoto, H. (2011) Hesr1 and Hesr3 are essential to generate undifferentiated quiescent satellite cells and to maintain satellite cell numbers.  Development 138, 4609-4619.

Solomon, E., Li, H., Duhachek-Muggy, S., Syta, E., and Zolkiewska, A. (2010) The role of SnoN in transforming growth factor beta1-induced expression of metalloprotease-disintegrin ADAM12.  J. Biol. Chem. 16, 285, 21969-21977.

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Sun, D., Li, H., and Zolkiewska, A. (2008) The role of Delta-like 1 shedding in muscle cell self-renewal and differentiation.  J. Cell Sci.121, 3815-3823.

Dyczynska, E., Syta, E., Sun, D., and Zolkiewska, A. (2008) Breast cancer-associated mutations in metalloprotease disintegrin ADAM12 interfere with the intracellular trafficking and processing of the protein.  Int. J. Cancer 122, 2634-2640.

Zolkiewska, A. (2008) ADAM proteases: ligand processing and modulation of the Notch pathway.  Cell. Mol. Life Sci. 65, 2056-2068.

Dyczynska, E., Sun, D., Yi, H., Sehara-Fujisawa, A., Blobel, CP., and Zolkiewska, A. (2007) Proteolytic processing of Delta-like 1 by ADAM proteases.  J. Biol. Chem. 282, 436-444.

Yi, H., Gruszczynska-Biegala, J., Wood, D., Zhao, Z., and Zolkiewska, A. (2005) Cooperation of the metalloprotease, disintegrin and cysteine-rich domains of ADAM12 during inhibition of myogenic differentiation.  J. Biol. Chem., 280, 23475-23483.

Zhao, Z., Gruszczynska-Biegala, J., and Zolkiewska, A. (2005) ADP-ribosylation of integrin a7 modulates the binding of integrin a7b1 to laminin.  Biochem. J. 385, 309-317.

Zolkiewska, A. (2005) Ecto-ADP-ribose transferases: cell-surface response to local tissue injury.  Physiology 20, 374-381.

Zhao, Z., Gruszczynska-Biegala, J., Cheuvront, T., Yi, H., Von Der Mark, H., Von Der Mark, K., Kaufman, SJ., and Zolkiewska, A. (2004) Interaction of the disintegrin and cysteine-rich domains of ADAM12 with integrin a7b1.  Exp Cell Res. 298, 28-37.

Cao, Y., Zhao, Z., Gruszczynska-Biegala, J., and Zolkiewska, A. (2003) Role of metalloprotease disintegrin ADAM12 in determination of quiescent reserve cells during myogenic differentiation in vitro.  Mol. Cell. Biol. 23, 6725-6738 .

Liu, Z., Zolkiewska, A., and Zolkiewski, M. (2003) Characterization of human torsinA and its dystonia-associated mutant form.  Biochem. J., 374, 117-122 .

Cao, Y., Kang, Q., Zhao, Z., and Zolkiewska, A. (2002) Intracellular Processing of Metalloprotease Disintegrin ADAM12.  J. Biol. Chem. 277, 26403-26411.

Kang, Q., Cao, Y., and Zolkiewska, A. (2001) Direct interaction between the cytoplasmic tail of ADAM 12 and the SH3 domain of p85a activates phosphatidylinositol 3-kinase in C2C12 cells.  J. Biol. Chem. 276, 24466-24472.

Cao, Y., Kang, Q., and Zolkiewska A. (2001) Metalloprotease-disintegrin ADAM12 interacts with a-actinin-1.  Biochem. J. 357, 353-361.

Kang, Q., Cao, Y., and Zolkiewska, A. (2000) Metalloprotease-disintegrin ADAM12 binds to the SH3 domain of Src and activates Src tyrosine kinase in C2C12 cells.  Biochem. J. 352, 883-892.

Barnett, ME., Zolkiewska, A., and Zolkiewski, M. (2000) Structure and activity of ClpB from Escherichia coli: role of the amino- and carboxy-terminal domains.  J. Biol. Chem. 275, 37565-37571.

Iba, K., Albrechtsen, R., Gilpin, B., Fröhlich, C., Loechel, F., Zolkiewska, A., Ishiguro, K., Kojima, T., Liu, W., Langford, JK., Sanderson, RD., Brakebusch, C., Fässler, R., and Wewer, UM. (2000) The cysteine-rich domain of human ADAM12 supports cell adhesion through syndecans and triggers signaling events that leads to integrin b1-dependent cell spreading.  J. Cell Biol., 149, 1143-1156.

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Zolkiewska, A. (1999) Disintegrin-like/cysteine-rich region of ADAM12 is an active cell adhesion domain.  Exp. Cell Res. 252, 423-431 .

Moss, J., Balducci, E., Cavanaugh, E., Kim, HJ., Konczalik, P., Lesma, EA., Okazaki, IJ., Park, M., Schoemaker, M., Stevens, LA., and Zolkiewska, A. (1999) Characterization of NAD:arginine ADP-ribosyltransferases.  Mol. Cell. Biochem. 193, 109-113.

Zolkiewska, A., Thompson, WC., and Moss, J. (1998) Interaction of integrin a7b1 in C2C12 myotubes and in solution with laminin.  Exp. Cell Res. 240, 86‑94 .

Moss, J., Zolkiewska, A., and Okazaki, IJ. (1997) ADP-ribosylarginine hydrolases and ADP-ribosyltransferases. Partners in ADP-ribosylation cycles.  Adv.Exp. Med. Biol. 419, 25-33.

Zolkiewska, A., and Moss, J. (1997) The a7 integrin as a target protein for cell surface mono-ADP-ribosylation in muscle cellsAdv.Exp. Med. Biol. 419, 297-303.

Zolkiewska, A., and Moss, J. (1995) Processing of ADP-ribosylated integrin a7 in skeletal muscle myotubes.  J. Biol. Chem. 270, 9227-9233.

Okazaki, IJ., Zolkiewska, A., Takada, T., and Moss, J. (1995) Characterization of mammalian ADP-ribosylation cycles.  Biochimie 77, 319-325.

Zolkiewska, A., Okazaki,  IJ., and Moss, J. (1994) Vertebrate ADP-ribosyltransferases.  Mol. Cell. Biochem. 138, 107-112.

Okazaki, IJ., Zolkiewska, A., Nightingale, MS., and Moss, J. (1994) Immunological and structural conservation of mammalian skeletal muscle glycosylphosphatidylinositol-linked ADP-ribosyltransferases.  Biochemistry 33, 12828-12836.

Zolkiewska, A., and Moss, J. (1993) Integrin a7 as substrate for a glycosylphosphatidyl-inositol-anchored ADP-ribosyltransferase on the surface of skeletal muscle cells.  J. Biol. Chem. 268, 25273-25276.

Zolkiewska, A., Nightingale, MS., and Moss, J. (1992) Molecular characterization of NAD:arginine ADP-ribosyltransferase from rabbit skeletal muscle.  Proc. Natl. Acad. Sci. USA 89, 11352-21356.

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