| Year |
Citation |
Score |
| 2020 |
Thevarajan I, Zolkiewski M, Zolkiewska A. Human CLPB forms ATP-dependent complexes in the mitochondrial intermembrane space. The International Journal of Biochemistry & Cell Biology. 127: 105841. PMID 32866687 DOI: 10.1016/J.Biocel.2020.105841 |
0.344 |
|
| 2019 |
Romero Y, Wise R, Zolkiewska A. Proteolytic processing of PD-L1 by ADAM proteases in breast cancer cells. Cancer Immunology, Immunotherapy : Cii. PMID 31796994 DOI: 10.1007/S00262-019-02437-2 |
0.33 |
|
| 2018 |
Leutert M, Menzel S, Braren R, Rissiek B, Hopp AK, Nowak K, Bisceglie L, Gehrig P, Li H, Zolkiewska A, Koch-Nolte F, Hottiger MO. Proteomic Characterization of the Heart and Skeletal Muscle Reveals Widespread Arginine ADP-Ribosylation by the ARTC1 Ectoenzyme. Cell Reports. 24: 1916-1929.e5. PMID 30110646 DOI: 10.1016/J.Celrep.2018.07.048 |
0.346 |
|
| 2017 |
Wise R, Zolkiewska A. Metalloprotease-dependent activation of EGFR modulates CD44(+)/CD24(-) populations in triple negative breast cancer cells through the MEK/ERK pathway. Breast Cancer Research and Treatment. PMID 28791489 DOI: 10.1007/S10549-017-4440-0 |
0.333 |
|
| 2017 |
Duhachek-Muggy S, Qi Y, Wise R, Alyahya L, Li H, Hodge J, Zolkiewska A. Metalloprotease-disintegrin ADAM12 actively promotes the stem cell-like phenotype in claudin-low breast cancer. Molecular Cancer. 16: 32. PMID 28148288 DOI: 10.1186/S12943-017-0599-6 |
0.384 |
|
| 2016 |
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 Research and Treatment. PMID 27161215 DOI: 10.1007/S10549-016-3820-1 |
0.453 |
|
| 2016 |
Qi Y, Duhachek-Muggy S, Li H, Alyahya L, Wise R, Zolkiewska A. Abstract B43: ADAM12 is a novel regulator of stem-like cells in triple-negative breast cancer Cancer Research. 76. DOI: 10.1158/1538-7445.Tummet15-B43 |
0.475 |
|
| 2016 |
Wise R, Duhachek-Muggy S, Qi Y, Zolkiewski M, Zolkiewska A. Abstract A40: Protein disulfide isomerases in the endoplasmic reticulum promote anchorage-independent growth of breast cancer cells Cancer Research. 76. DOI: 10.1158/1538-7445.Tummet15-A40 |
0.453 |
|
| 2015 |
Duhachek-Muggy S, Zolkiewska A. ADAM12-L is a direct target of the miR-29 and miR-200 families in breast cancer. Bmc Cancer. 15: 93. PMID 25886595 DOI: 10.1186/S12885-015-1108-1 |
0.32 |
|
| 2014 |
Qi Y, Duhachek-Muggy S, Li H, Zolkiewska A. Phenotypic diversity of breast cancer-related mutations in metalloproteinase-disintegrin ADAM12. Plos One. 9: e92536. PMID 24651654 DOI: 10.1371/Journal.Pone.0092536 |
0.37 |
|
| 2013 |
Duhachek-Muggy S, Li H, Qi Y, Zolkiewska A. Alternative mRNA splicing generates two distinct ADAM12 prodomain variants. Plos One. 8: e75730. PMID 24116070 DOI: 10.1371/Journal.Pone.0075730 |
0.441 |
|
| 2013 |
Ngansop F, Li H, Zolkiewska A, Zolkiewski M. Biochemical characterization of the apicoplast-targeted AAA+ ATPase ClpB from Plasmodium falciparum. Biochemical and Biophysical Research Communications. 439: 191-5. PMID 23994135 DOI: 10.1016/J.Bbrc.2013.08.064 |
0.303 |
|
| 2013 |
Li H, Duhachek-Muggy S, Dubnicka S, Zolkiewska A. Metalloproteinase-disintegrin ADAM12 is associated with a breast tumor-initiating cell phenotype. Breast Cancer Research and Treatment. 139: 691-703. PMID 23771733 DOI: 10.1007/S10549-013-2602-2 |
0.412 |
|
| 2013 |
Duhachek-Muggy S, Zolkiewska A. Abstract B133: Metalloprotease-disintegrin ADAM12-L in breast cancer cells: Regulation of expression by microRNA-200b/c Molecular Cancer Research. 11. DOI: 10.1158/1557-3125.Advbc-B133 |
0.365 |
|
| 2013 |
Qi Y, Duhachek-Muggy S, Li H, Zolkiewska A. Abstract P2-08-05: Functional characterization of three novel breast cancer-related somatic mutations in metalloproteinase-disintegrin ADAM12 Cancer Research. 73. DOI: 10.1158/0008-5472.Sabcs13-P2-08-05 |
0.367 |
|
| 2012 |
Li H, Duhachek-Muggy S, Qi Y, Hong Y, Behbod F, Zolkiewska A. An essential role of metalloprotease-disintegrin ADAM12 in triple-negative breast cancer. Breast Cancer Research and Treatment. 135: 759-69. PMID 22926263 DOI: 10.1007/S10549-012-2220-4 |
0.394 |
|
| 2011 |
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, et al. Hesr1 and Hesr3 are essential to generate undifferentiated quiescent satellite cells and to maintain satellite cell numbers. Development (Cambridge, England). 138: 4609-19. PMID 21989910 DOI: 10.1242/Dev.067165 |
0.386 |
|
| 2011 |
Chen J, Zolkiewska A. Force-induced unfolding simulations of the human Notch1 negative regulatory region: possible roles of the heterodimerization domain in mechanosensing. Plos One. 6: e22837. PMID 21829530 DOI: 10.1371/Journal.Pone.0022837 |
0.389 |
|
| 2011 |
Li H, Solomon E, Duhachek Muggy S, Sun D, Zolkiewska A. Metalloprotease-disintegrin ADAM12 expression is regulated by Notch signaling via microRNA-29. The Journal of Biological Chemistry. 286: 21500-10. PMID 21518768 DOI: 10.1074/Jbc.M110.207951 |
0.643 |
|
| 2010 |
Solomon E, Li H, Duhachek Muggy S, Syta E, Zolkiewska A. The role of SnoN in transforming growth factor beta1-induced expression of metalloprotease-disintegrin ADAM12. The Journal of Biological Chemistry. 285: 21969-77. PMID 20457602 DOI: 10.1074/Jbc.M110.133314 |
0.649 |
|
| 2008 |
Sun D, Li H, Zolkiewska A. The role of Delta-like 1 shedding in muscle cell self-renewal and differentiation. Journal of Cell Science. 121: 3815-23. PMID 18957511 DOI: 10.1242/Jcs.035493 |
0.68 |
|
| 2008 |
Zolkiewska A. ADAM proteases: Ligand processing and modulation of the Notch pathway Cellular and Molecular Life Sciences. 65: 2056-2068. PMID 18344021 DOI: 10.1007/S00018-008-7586-4 |
0.434 |
|
| 2008 |
Dyczynska E, Syta E, Sun D, Zolkiewska A. Breast cancer-associated mutations in metalloprotease disintegrin ADAM12 interfere with the intracellular trafficking and processing of the protein. International Journal of Cancer. 122: 2634-40. PMID 18241035 DOI: 10.1002/Ijc.23405 |
0.608 |
|
| 2007 |
Dyczynska E, Sun D, Yi H, Sehara-Fujisawa A, Blobel CP, Zolkiewska A. Proteolytic processing of delta-like 1 by ADAM proteases. The Journal of Biological Chemistry. 282: 436-44. PMID 17107962 DOI: 10.1074/Jbc.M605451200 |
0.748 |
|
| 2005 |
Zolkiewska A. Ecto-ADP-ribose transferases: cell-surface response to local tissue injury. Physiology (Bethesda, Md.). 20: 374-81. PMID 16287986 DOI: 10.1152/Physiol.00028.2005 |
0.327 |
|
| 2005 |
Yi H, Gruszczynska-Biegala J, Wood D, Zhao Z, Zolkiewska A. Cooperation of the metalloprotease, disintegrin, and cysteine-rich domains of ADAM12 during inhibition of myogenic differentiation. The Journal of Biological Chemistry. 280: 23475-83. PMID 15849365 DOI: 10.1074/Jbc.M413550200 |
0.712 |
|
| 2005 |
Zhao Z, Gruszczynska-Biegala J, Zolkiewska A. ADP-ribosylation of integrin alpha7 modulates the binding of integrin alpha7beta1 to laminin. The Biochemical Journal. 385: 309-17. PMID 15361073 DOI: 10.1042/Bj20040590 |
0.578 |
|
| 2004 |
Zhao Z, Gruszczynska-Biegala J, Cheuvront T, Yi H, von der Mark H, von der Mark K, Kaufman SJ, Zolkiewska A. Interaction of the disintegrin and cysteine-rich domains of ADAM12 with integrin alpha7beta1. Experimental Cell Research. 298: 28-37. PMID 15242759 DOI: 10.1016/J.Yexcr.2004.04.005 |
0.709 |
|
| 2003 |
Cao Y, Zhao Z, Gruszczynska-Biegala J, Zolkiewska A. Role of metalloprotease disintegrin ADAM12 in determination of quiescent reserve cells during myogenic differentiation in vitro. Molecular and Cellular Biology. 23: 6725-38. PMID 12972593 DOI: 10.1128/Mcb.23.19.6725-6738.2003 |
0.693 |
|
| 2003 |
Liu Z, Zolkiewska A, Zolkiewski M. Characterization of human torsinA and its dystonia-associated mutant form. The Biochemical Journal. 374: 117-22. PMID 12780349 DOI: 10.1042/Bj20030258 |
0.365 |
|
| 2002 |
Cao Y, Kang Q, Zhao Z, Zolkiewska A. Intracellular processing of metalloprotease disintegrin ADAM12. The Journal of Biological Chemistry. 277: 26403-11. PMID 12000744 DOI: 10.1074/Jbc.M110814200 |
0.716 |
|
| 2001 |
Cao Y, Kang Q, Zolkiewska A. Metalloprotease-disintegrin ADAM 12 interacts with alpha-actinin-1. The Biochemical Journal. 357: 353-61. PMID 11439084 DOI: 10.1042/0264-6021:3570353 |
0.624 |
|
| 2001 |
Kang Q, Cao Y, Zolkiewska A. Direct interaction between the cytoplasmic tail of ADAM 12 and the Src homology 3 domain of p85alpha activates phosphatidylinositol 3-kinase in C2C12 cells. The Journal of Biological Chemistry. 276: 24466-72. PMID 11313349 DOI: 10.1074/Jbc.M101162200 |
0.61 |
|
| 2000 |
Kang Q, Cao Y, Zolkiewska A. Metalloprotease-disintegrin ADAM 12 binds to the SH3 domain of Src and activates Src tyrosine kinase in C2C12 cells. The Biochemical Journal. 352: 883-92. PMID 11104699 DOI: 10.1042/Bj3520883 |
0.685 |
|
| 2000 |
Barnett ME, Zolkiewska A, Zolkiewski M. Structure and activity of ClpB from Escherichia coli. Role of the amino-and -carboxyl-terminal domains. The Journal of Biological Chemistry. 275: 37565-71. PMID 10982797 DOI: 10.1074/Jbc.M005211200 |
0.359 |
|
| 2000 |
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, Wewer UM. The cysteine-rich domain of human ADAM 12 supports cell adhesion through syndecans and triggers signaling events that lead to β1 integrin-dependent cell spreading Journal of Cell Biology. 149: 1143-1155. PMID 10831617 DOI: 10.1083/Jcb.149.5.1143 |
0.466 |
|
| 1999 |
Zolkiewska A. Disintegrin-like/cysteine-rich region of ADAM 12 is an active cell adhesion domain Experimental Cell Research. 252: 423-431. PMID 10527632 DOI: 10.1006/Excr.1999.4632 |
0.458 |
|
| 1999 |
Moss J, Balducci E, Cavanaugh E, Kim HJ, Konczalik P, Lesma EA, Okazaki IJ, Park M, Shoemaker M, Stevens LA, Zolkiewska A. Characterization of NAD:arginine ADP-ribosyltransferases. Molecular and Cellular Biochemistry. 193: 109-13. PMID 10331646 DOI: 10.1023/A:1006924514074 |
0.428 |
|
| 1998 |
Zolkiewska A, Thompson WC, Moss J. Interaction of integrin α7β1 in C2C12 myotubes and in solution with laminin Experimental Cell Research. 240: 86-94. PMID 9570924 DOI: 10.1006/Excr.1998.4002 |
0.343 |
|
| 1997 |
Zolkiewska A, Moss J. The α7 integrin as a target protein for cell surface mono-ADP- ribosylation in muscle cells Advances in Experimental Medicine and Biology. 419: 297-303. PMID 9193669 DOI: 10.1007/978-1-4419-8632-0_39 |
0.344 |
|
| 1997 |
Moss J, Zolkiewska A, Okazaki I. ADP-ribosylarginine hydrolases and ADP-ribosyltransferases: Partners in aDP-ribosylation cycles Advances in Experimental Medicine and Biology. 419: 25-33. PMID 9193633 DOI: 10.1007/978-1-4419-8632-0_3 |
0.357 |
|
| 1995 |
Okazaki IJ, Zolkiewska A, Takada T, Moss J. Characterization of mammalian ADP-ribosylation cycles Biochimie. 77: 319-325. PMID 8527484 DOI: 10.1016/0300-9084(96)88141-7 |
0.352 |
|
| 1995 |
Zolkiewska A, Moss J. Processing of ADP-ribosylated integrin α7 in skeletal muscle myotubes Journal of Biological Chemistry. 270: 9227-9233. PMID 7721841 DOI: 10.1074/Jbc.270.16.9227 |
0.307 |
|
| 1994 |
Zolkiewska A, Okazaki IJ, Moss J. Vertebrate mono-ADP-ribosyltransferases Molecular and Cellular Biochemistry. 138: 107-112. PMID 7898451 DOI: 10.1007/Bf00928450 |
0.377 |
|
| 1993 |
Zolkiewska A, Moss J. Integrin α7 as substrate for a glycosylphosphatidylinositol-anchored ADP- ribosyltransferase on the surface of skeletal muscle cells Journal of Biological Chemistry. 268: 25273-25276. PMID 8244957 |
0.302 |
|
| 1992 |
Zolkiewska A, Nightingale MS, Moss J. Molecular characterization of NAD:arginine ADP-ribosyltransferase from rabbit skeletal muscle Proceedings of the National Academy of Sciences of the United States of America. 89: 11352-11356. PMID 1454819 DOI: 10.1073/Pnas.89.23.11352 |
0.332 |
|
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