| Year |
Citation |
Score |
| 2022 |
Marano N, Holaska JM. Emerin interacts with histone methyltransferases to regulate repressive chromatin at the nuclear periphery. Frontiers in Cell and Developmental Biology. 10: 1007120. PMID 36274837 DOI: 10.3389/fcell.2022.1007120 |
0.316 |
|
| 2021 |
Liddane AG, Holaska JM. The Role of Emerin in Cancer Progression and Metastasis. International Journal of Molecular Sciences. 22. PMID 34681951 DOI: 10.3390/ijms222011289 |
0.327 |
|
| 2020 |
Gómez-Monsivais WL, Monterrubio-Ledezma F, Huerta-Cantillo J, Mondragon-Gonzalez R, Alamillo-Iniesta A, García-Aguirre I, Azuara-Medina PM, Arguello-García R, Rivera-Monroy JE, Holaska JM, Hernández-Méndez JME, Garrido E, Magaña JJ, Winder SJ, Brancaccio A, et al. The Molecular Basis and Biologic Significance of the β-Dystroglycan-Emerin Interaction. International Journal of Molecular Sciences. 21. PMID 32824881 DOI: 10.3390/Ijms21175944 |
0.335 |
|
| 2020 |
Iyer A, Holaska JM. EDMD-Causing Emerin Mutant Myogenic Progenitors Exhibit Impaired Differentiation Using Similar Mechanisms. Cells. 9. PMID 32549231 DOI: 10.3390/Cells9061463 |
0.329 |
|
| 2020 |
Bossone KA, Ellis JA, Holaska JM. Histone acetyltransferase inhibition rescues differentiation of emerin-deficient myogenic progenitors. Muscle & Nerve. PMID 32304242 DOI: 10.1002/Mus.26892 |
0.309 |
|
| 2017 |
Iyer A, Koch AJ, Holaska JM. Expression Profiling of Differentiating Emerin-Null Myogenic Progenitor Identifies Molecular Pathways Implicated in Their Impaired Differentiation. Cells. 6. PMID 29065506 DOI: 10.3390/Cells6040038 |
0.356 |
|
| 2017 |
Collins CM, Ellis J, Holaska JM. MAPK signaling pathways and HDAC3 activity are disrupted during emerin-null myogenic progenitor differentiation. Disease Models & Mechanisms. PMID 28188262 DOI: 10.1242/Dmm.028787 |
0.388 |
|
| 2016 |
Holaska JM. Diseases of the Nucleoskeleton. Comprehensive Physiology. 6: 1655-1674. PMID 27783855 DOI: 10.1002/Cphy.C150039 |
0.447 |
|
| 2015 |
Depreux FF, Puckelwartz MJ, Augustynowicz A, Wolfgeher D, Labno CM, Pierre-Louis D, Cicka D, Kron SJ, Holaska J, McNally EM. Disruption of the lamin A and matrin-3 interaction by myopathic LMNA mutations. Human Molecular Genetics. 24: 4284-95. PMID 25948554 DOI: 10.1093/Hmg/Ddv160 |
0.508 |
|
| 2015 |
Mull A, Kim G, Holaska JM. LMO7-null mice exhibit phenotypes consistent with emery-dreifuss muscular dystrophy. Muscle & Nerve. 51: 222-8. PMID 24825363 DOI: 10.1002/Mus.24286 |
0.439 |
|
| 2014 |
Koch AJ, Holaska JM. Emerin in health and disease. Seminars in Cell & Developmental Biology. 29: 95-106. PMID 24365856 DOI: 10.1016/J.Semcdb.2013.12.008 |
0.399 |
|
| 2013 |
Demmerle J, Koch AJ, Holaska JM. Emerin and histone deacetylase 3 (HDAC3) cooperatively regulate expression and nuclear positions of MyoD, Myf5, and Pax7 genes during myogenesis. Chromosome Research : An International Journal On the Molecular, Supramolecular and Evolutionary Aspects of Chromosome Biology. 21: 765-79. PMID 24062260 DOI: 10.1007/S10577-013-9381-9 |
0.431 |
|
| 2012 |
Koch AJ, Holaska JM. Loss of emerin alters myogenic signaling and miRNA expression in mouse myogenic progenitors. Plos One. 7: e37262. PMID 22606356 DOI: 10.1371/Journal.Pone.0037262 |
0.355 |
|
| 2012 |
Demmerle J, Koch AJ, Holaska JM. The nuclear envelope protein emerin binds directly to histone deacetylase 3 (HDAC3) and activates HDAC3 activity. The Journal of Biological Chemistry. 287: 22080-8. PMID 22570481 DOI: 10.1074/Jbc.M111.325308 |
0.497 |
|
| 2011 |
Dedeic Z, Cetera M, Cohen TV, Holaska JM. Emerin inhibits Lmo7 binding to the Pax3 and MyoD promoters and expression of myoblast proliferation genes. Journal of Cell Science. 124: 1691-702. PMID 21525034 DOI: 10.1242/Dev.068981 |
0.464 |
|
| 2010 |
Puckelwartz MJ, Kessler EJ, Kim G, Dewitt MM, Zhang Y, Earley JU, Depreux FF, Holaska J, Mewborn SK, Pytel P, McNally EM. Nesprin-1 mutations in human and murine cardiomyopathy. Journal of Molecular and Cellular Cardiology. 48: 600-8. PMID 19944109 DOI: 10.1016/J.Yjmcc.2009.11.006 |
0.369 |
|
| 2010 |
Cetera M, Holaska JM. Emerin binding to Lmo7 inhibits Lmo7 binding to the Pax3 and MyoD promoters and expression of critical myoblast differentiation genes F1000research. 1. DOI: 10.7490/F1000Research.61.1 |
0.382 |
|
| 2009 |
Puckelwartz MJ, Kessler E, Zhang Y, Hodzic D, Randles KN, Morris G, Earley JU, Hadhazy M, Holaska JM, Mewborn SK, Pytel P, McNally EM. Disruption of nesprin-1 produces an Emery Dreifuss muscular dystrophy-like phenotype in mice. Human Molecular Genetics. 18: 607-20. PMID 19008300 DOI: 10.1093/Hmg/Ddn386 |
0.446 |
|
| 2008 |
Holaska JM. Emerin and the nuclear lamina in muscle and cardiac disease. Circulation Research. 103: 16-23. PMID 18596264 DOI: 10.1161/Circresaha.108.172197 |
0.449 |
|
| 2007 |
Holaska JM, Wilson KL. An emerin "proteome": purification of distinct emerin-containing complexes from HeLa cells suggests molecular basis for diverse roles including gene regulation, mRNA splicing, signaling, mechanosensing, and nuclear architecture. Biochemistry. 46: 8897-908. PMID 17620012 DOI: 10.1021/Bi602636M |
0.555 |
|
| 2006 |
Holaska JM, Rais-Bahrami S, Wilson KL. Lmo7 is an emerin-binding protein that regulates the transcription of emerin and many other muscle-relevant genes. Human Molecular Genetics. 15: 3459-72. PMID 17067998 DOI: 10.1093/Hmg/Ddl423 |
0.465 |
|
| 2006 |
Holaska JM, Wilson KL. Multiple roles for emerin: implications for Emery-Dreifuss muscular dystrophy. The Anatomical Record. Part a, Discoveries in Molecular, Cellular, and Evolutionary Biology. 288: 676-80. PMID 16761279 DOI: 10.1002/Ar.A.20334 |
0.383 |
|
| 2005 |
Wilson KL, Holaska JM, Montes de Oca R, Tifft K, Zastrow M, Segura-Totten M, Mansharamani M, Bengtsson L. Nuclear membrane protein emerin: roles in gene regulation, actin dynamics and human disease. Novartis Foundation Symposium. 264: 51-58; discussion 58. PMID 15773747 DOI: 10.1002/0470093765.Ch5 |
0.546 |
|
| 2004 |
Holaska JM, Kowalski AK, Wilson KL. Emerin caps the pointed end of actin filaments: evidence for an actin cortical network at the nuclear inner membrane. Plos Biology. 2: E231. PMID 15328537 DOI: 10.1371/Journal.Pbio.0020231 |
0.434 |
|
| 2004 |
Haraguchi T, Holaska JM, Yamane M, Koujin T, Hashiguchi N, Mori C, Wilson KL, Hiraoka Y. Emerin binding to Btf, a death-promoting transcriptional repressor, is disrupted by a missense mutation that causes Emery-Dreifuss muscular dystrophy. European Journal of Biochemistry. 271: 1035-45. PMID 15009215 DOI: 10.1111/J.1432-1033.2004.04007.X |
0.484 |
|
| 2003 |
Wilkinson FL, Holaska JM, Zhang Z, Sharma A, Manilal S, Holt I, Stamm S, Wilson KL, Morris GE. Emerin interacts in vitro with the splicing-associated factor, YT521-B. European Journal of Biochemistry. 270: 2459-66. PMID 12755701 DOI: 10.1046/J.1432-1033.2003.03617.X |
0.489 |
|
| 2003 |
Holaska JM, Lee KK, Kowalski AK, Wilson KL. Transcriptional repressor germ cell-less (GCL) and barrier to autointegration factor (BAF) compete for binding to emerin in vitro. The Journal of Biological Chemistry. 278: 6969-75. PMID 12493765 DOI: 10.1074/Jbc.M208811200 |
0.547 |
|
| 2002 |
Holaska JM, Black BE, Rastinejad F, Paschal BM. Ca2+-dependent nuclear export mediated by calreticulin. Molecular and Cellular Biology. 22: 6286-97. PMID 12167720 DOI: 10.1128/Mcb.22.17.6286-6297.2002 |
0.695 |
|
| 2002 |
Mislow JM, Holaska JM, Kim MS, Lee KK, Segura-Totten M, Wilson KL, McNally EM. Nesprin-1alpha self-associates and binds directly to emerin and lamin A in vitro. Febs Letters. 525: 135-40. PMID 12163176 DOI: 10.1016/S0014-5793(02)03105-8 |
0.377 |
|
| 2002 |
Brownawell AM, Holaska JM, Macara IG, Paschal BM. The use of permeabilized cell systems to study nuclear transport. Methods in Molecular Biology (Clifton, N.J.). 189: 209-29. PMID 12094589 DOI: 10.1385/1-59259-281-3:209 |
0.597 |
|
| 2002 |
Holaska JM, Wilson KL, Mansharamani M. The nuclear envelope, lamins and nuclear assembly. Current Opinion in Cell Biology. 14: 357-64. PMID 12067659 DOI: 10.1016/S0955-0674(02)00329-0 |
0.528 |
|
| 2001 |
Black BE, Holaska JM, Rastinejad F, Paschal BM. DNA binding domains in diverse nuclear receptors function as nuclear export signals. Current Biology : Cb. 11: 1749-58. PMID 11719216 DOI: 10.1016/S0960-9822(01)00537-1 |
0.735 |
|
| 2001 |
Lindsay ME, Holaska JM, Welch K, Paschal BM, Macara IG. Ran-binding protein 3 is a cofactor for Crm1-mediated nuclear protein export. The Journal of Cell Biology. 153: 1391-402. PMID 11425870 DOI: 10.1083/Jcb.153.7.1391 |
0.72 |
|
| 2001 |
Black BE, Holaska JM, Lévesque L, Ossareh-Nazari B, Gwizdek C, Dargemont C, Paschal BM. NXT1 is necessary for the terminal step of Crm1-mediated nuclear export. The Journal of Cell Biology. 152: 141-55. PMID 11149927 DOI: 10.1083/Jcb.152.1.141 |
0.75 |
|
| 2001 |
Holaska JM, Black BE, Love DC, Hanover JA, Leszyk J, Paschal BM. Calreticulin Is a receptor for nuclear export. The Journal of Cell Biology. 152: 127-40. PMID 11149926 DOI: 10.1083/Jcb.152.1.127 |
0.747 |
|
| 1999 |
Black BE, Lévesque L, Holaska JM, Wood TC, Paschal BM. Identification of an NTF2-related factor that binds Ran-GTP and regulates nuclear protein export. Molecular and Cellular Biology. 19: 8616-24. PMID 10567585 DOI: 10.1128/Mcb.19.12.8616 |
0.757 |
|
| 1998 |
Holaska JM, Paschal BM. A cytosolic activity distinct from crm1 mediates nuclear export of protein kinase inhibitor in permeabilized cells. Proceedings of the National Academy of Sciences of the United States of America. 95: 14739-44. PMID 9843959 DOI: 10.1073/Pnas.95.25.14739 |
0.706 |
|
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