Jens Milbradt

发表

Transmembrane Protein pUL50 of Human Cytomegalovirus Inhibits ISGylation by Downregulating UBE1L

Myoung Kyu Lee, Jin-Hyun Ahn, Ye ji Kim, 2018, Journal of Virology.

Regulatory roles of protein kinases in cytomegalovirus replication.

Jens Milbradt, M. Marschall, Sabine Feichtinger, 2011, Advances in virus research.

Cytomegalovirus pUL50 is the multi-interacting determinant of the core nuclear egress complex (NEC) that recruits cellular accessory NEC components.

S. Jonjić, Jens Milbradt, M. Marschall, 2016, The Journal of general virology.

New insight into the phosphorylation-regulated intranuclear localization of human cytomegalovirus pUL69 mediated by cyclin-dependent kinases (CDKs) and viral CDK orthologue pUL97.

Jens Milbradt, M. Marschall, Sabine Feichtinger, 2016, The Journal of general virology.

Human Cytomegalovirus Replication Is Strictly Inhibited by siRNAs Targeting UL54, UL97 or UL122/123 Gene Transcripts

Jens Milbradt, M. Marschall, W. Rawlinson, 2014, PLoS ONE.

Cytomegaloviral protein kinase pUL97 interacts with the nuclear mRNA export factor pUL69 to modulate its intranuclear localization and activity.

Jens Milbradt, M. Marschall, T. Stamminger, 2009, The Journal of general virology.

Proteomic Analysis of the Multimeric Nuclear Egress Complex of Human Cytomegalovirus*

S. Pinkert, H. Sticht, Y. Couté, 2014, Molecular & Cellular Proteomics.

complex of human cytomegalovirus

S. Pinkert, H. Sticht, Y. Couté, 2014 .

Phenotypical Characterization of the Nuclear Egress of Recombinant Cytomegaloviruses Reveals Defective Replication upon ORF-UL50 Deletion but Not pUL50 Phosphosite Mutation

U. Schlötzer-Schrehardt, Jens Milbradt, M. Marschall, 2021, Viruses.

Phosphosite Analysis of the Cytomegaloviral mRNA Export Factor pUL69 Reveals Serines with Critical Importance for Recruitment of Cellular Proteins Pin1 and UAP56/URH49

Koshi Imami, Jens Milbradt, M. Marschall, 2020, Journal of Virology.

Human cytomegalovirus overcomes SAMHD1 restriction in macrophages via pUL97

M. Schindler, Jens Milbradt, T. Gramberg, 2019, Nature Microbiology.

The Prolyl Isomerase Pin1 Promotes the Herpesvirus-Induced Phosphorylation-Dependent Disassembly of the Nuclear Lamina Required for Nucleocytoplasmic Egress

Anselm H. C. Horn, H. Sticht, Jens Milbradt, 2016, PLoS pathogens.

Novel Mode of Phosphorylation-triggered Reorganization of the Nuclear Lamina during Nuclear Egress of Human Cytomegalovirus*

H. Sticht, Jens Milbradt, M. Marschall, 2010, The Journal of Biological Chemistry.

The broad-spectrum antiinfective drug artesunate interferes with the canonical nuclear factor kappa B (NF-κB) pathway by targeting RelA/p65.

T. Efferth, O. Kadioglu, S. Wandinger, 2015, Antiviral research.

Human cytomegalovirus utilises cellular dual-specificity tyrosine phosphorylation-regulated kinases during placental replication.

Jens Milbradt, M. Marschall, W. Rawlinson, 2018, Placenta.

A viral kinase counteracts in vivo restriction of murine cytomegalovirus by SAMHD1

N. Ferreirós, T. Winkler, M. Schindler, 2019, Nature Microbiology.

Inhibitors of dual‐specificity tyrosine phosphorylation‐regulated kinases (DYRK) exert a strong anti‐herpesviral activity

Jens Milbradt, M. Marschall, T. Stamminger, 2017, Antiviral research.

The unique antiviral activity of artesunate is broadly effective against human cytomegaloviruses including therapy-resistant mutants.

S. Chou, Jens Milbradt, M. Marschall, 2011, Antiviral research.

A Novel CDK7 Inhibitor of the Pyrazolotriazine Class Exerts Broad-Spectrum Antiviral Activity at Nanomolar Concentrations

K. Korn, B. Klebl, Jens Milbradt, 2015, Antimicrobial Agents and Chemotherapy.

Human Cytomegalovirus Nuclear Egress Proteins Ectopically Expressed in the Heterologous Environment of Plant Cells are Strictly Targeted to the Nuclear Envelope

U. Sonnewald, Jens Milbradt, M. Marschall, 2016, Viruses.

Human Cytomegalovirus Nuclear Capsids Associate with the Core Nuclear Egress Complex and the Viral Protein Kinase pUL97

S. Jonjić, U. Schlötzer-Schrehardt, W. Britt, 2018, Viruses.

Cytomegaloviral proteins that associate with the nuclear lamina: components of a postulated nuclear egress complex.

H. Sticht, Jens Milbradt, M. Marschall, 2009, The Journal of general virology.

The human cytomegalovirus nuclear egress complex unites multiple functions: Recruitment of effectors, nuclear envelope rearrangement, and docking to nuclear capsids

Y. Muller, H. Sticht, Jens Milbradt, 2017, Reviews in medical virology.

Crystal Structure of the Human Cytomegalovirus pUL50-pUL53 Core Nuclear Egress Complex Provides Insight into a Unique Assembly Scaffold for Virus-Host Protein Interactions*♦

Y. Muller, H. Sticht, Jens Milbradt, 2015, The Journal of Biological Chemistry.

Cytomegaloviral proteins pUL50 and pUL53 are associated with the nuclear lamina and interact with cellular protein kinase C.

Jens Milbradt, M. Marschall, S. Auerochs, 2007, The Journal of general virology.

Specific Residues of a Conserved Domain in the N Terminus of the Human Cytomegalovirus pUL50 Protein Determine Its Intranuclear Interaction with pUL53*

Y. Muller, H. Sticht, Jens Milbradt, 2012, The Journal of Biological Chemistry.

Cytomegaloviral proteins pUL 50 and pUL 53 are associated with the nuclear lamina and interact with cellular protein kinase C

Jens Milbradt, M. Marschall, S. Auerochs, 2007 .

The cytomegalovirus egress proteins pUL50 and pUL53 are translocated to the nuclear envelope through two distinct modes of nuclear import.

H. Sticht, Jens Milbradt, M. Marschall, 2013, The Journal of general virology.

Protein kinases responsible for the phosphorylation of the nuclear egress core complex of human cytomegalovirus.

U. Sonnewald, Y. Couté, Jens Milbradt, 2017, The Journal of general virology.

Differential upregulation of host cell protein kinases by the replication of α-, β- and γ-herpesviruses provides a signature of virus-specific signalling.

R. Wagner, C. Thirion, Jens Milbradt, 2020, The Journal of general virology.

Sensitivity of human herpesvirus 6 and other human herpesviruses to the broad-spectrum antiinfective drug artesunate.

K. Korn, Jens Milbradt, M. Marschall, 2009, Journal of clinical virology : the official publication of the Pan American Society for Clinical Virology.

Nuclear import of isoforms of the cytomegalovirus kinase pUL97 is mediated by differential activity of NLS1 and NLS2 both acting through classical importin-α binding.

T. Wittenberg, H. Sticht, Jens Milbradt, 2012, The Journal of general virology.

Two isoforms of the protein kinase pUL97 of human cytomegalovirus are differentially regulated in their nuclear translocation.

Heinrich Sticht, Thomas Wittenberg, Jens Milbradt, 2011, The Journal of general virology.

The peptidyl-prolyl cis-trans isomerase Pin1 interacts with three early regulatory proteins of human cytomegalovirus.

H. Sticht, Jens Milbradt, M. Marschall, 2020, Virus research.

Sensitivity of human herpesvirus 6 and other human herpesviruses to the broad-spectrum antiinfective drug artesunate.

K. Korn, Jens Milbradt, M. Marschall, 2009, Journal of clinical virology : the official publication of the Pan American Society for Clinical Virology.

Cytomegaloviral protein kinase pUL97 interacts with the nuclear mRNA export factor pUL69 to modulate its intranuclear localization and activity.

Jens Milbradt, M. Marschall, T. Stamminger, 2009, The Journal of general virology.