Silke Wiesner

ORCID: 0000-0003-0015-0167
Publications
Citations
Views
---
Saved
---
About
Contact & Profiles
Research Areas
  • X-ray Diffraction in Crystallography
  • Crystallization and Solubility Studies
  • Ubiquitin and proteasome pathways
  • RNA and protein synthesis mechanisms
  • RNA Research and Splicing
  • Peptidase Inhibition and Analysis
  • Protein Structure and Dynamics
  • Glycosylation and Glycoproteins Research
  • Chronic Myeloid Leukemia Treatments
  • Protein Degradation and Inhibitors
  • Enzyme Structure and Function
  • Crystallography and molecular interactions
  • Hippo pathway signaling and YAP/TAZ
  • Quinazolinone synthesis and applications
  • Endoplasmic Reticulum Stress and Disease
  • TGF-β signaling in diseases
  • RNA modifications and cancer
  • Cancer, Hypoxia, and Metabolism
  • Eosinophilic Disorders and Syndromes
  • Cellular transport and secretion
  • Cancer-related gene regulation
  • Zebrafish Biomedical Research Applications
  • Galectins and Cancer Biology
  • Heat shock proteins research
  • Fungal Plant Pathogen Control

University of Regensburg
2018-2024

Max Planck Institute for Developmental Biology
2009-2019

Hospital for Sick Children
2006-2009

University of Toronto
2007-2008

Canada Research Chairs
2008

SickKids Foundation
2008

National University of Singapore
2007

Center for Cancer Research
2007

European Molecular Biology Organization
2005

European Molecular Biology Laboratory
2005

Computational design has been very successful in recent years: multiple novel ligand binding proteins as well enzymes have reported. We wanted to know molecular detail how precise the predictions of interactions protein and ligands are. Therefore, we performed a structural analysis number published receptors designed onto periplasmic scaffold that were reported bind new with nano- micromolar affinities. It turned out most these are not suitable for studies due instability aggregation....

10.1073/pnas.0907950106 article EN Proceedings of the National Academy of Sciences 2009-10-16

A series of experiments are presented that provide an exchange-free measure dipole−dipole 15N transverse relaxation, Rdd, can then be substituted for R1ρ or R2 rates in the study internal protein dynamics. The method is predicated on measurement a relaxation involving 1H−15N longitudinal order, anti-phase 1H and single-quantum coherences, multiple quantum coherences; all coherences measured under conditions spin-locking. Results from detailed simulations number systems establish Rdd values...

10.1021/ja072717t article EN Journal of the American Chemical Society 2007-08-28

Abstract FAT10 is a ubiquitin-like modifier that directly targets proteins for proteasomal degradation. Here, we report the high-resolution structures of two individual domains (UBD) are joined by flexible linker. While UBDs show typical ubiquitin-fold, their surfaces entirely different from each other and ubiquitin explaining unique binding specificities. Deletion linker abrogates FAT10-conjugation while its mutation blocks auto-FAT10ylation FAT10-conjugating enzyme USE1 but not bulk...

10.1038/s41467-018-05776-3 article EN cc-by Nature Communications 2018-08-14

<h2>Summary</h2> Methyl NMR spectroscopy is a powerful tool for studying protein structure, dynamics, and interactions. Yet difficulties with resonance assignment the low abundance of methyl groups can preclude detailed studies, particularly determination continuous interaction surfaces. Here we present straightforward strategy that overcomes these problems. We systematically substituted solvent-exposed residues reporter methionines in expected binding site performed chemical shift...

10.1016/j.str.2012.02.012 article EN publisher-specific-oa Structure 2012-04-01

The association between the polarity proteins Par6 and Par3 requires a motif in that binds to two of PDZ domains Par3.

10.1126/scisignal.aam9899 article EN Science Signaling 2018-02-13

The yeast splicing factor Prp40 (pre-mRNA processing protein 40) consists of a pair WW domains followed by several FF domains. region comprising the has been shown to associate with 5' end U1 small nuclear RNA and interact directly two proteins, Clf1 (Crooked neck-like 1) phosphorylated repeats C-terminal domain polymerase II (CTD-RNAPII). In this work we reported solution structure first identification novel ligand-binding site in By using chemical shift assays, found binding for N-terminal...

10.1074/jbc.m508047200 article EN cc-by Journal of Biological Chemistry 2005-10-28

CIN85 is an adaptor protein linking the ubiquitin ligase Cbl and clathrin-binding proteins in clathrin-mediated receptor endocytosis. The SH3 domains of bind to a proline-rich region Cbl. Here we show that all three ubiquitin. We also present data-based structural model SH3-C domain complex with In this complex, binds canonical interaction surface for ligands mimics PPII helix, provide evidence competes these binding. demonstrate disruption binding results constitutive ubiquitination...

10.1021/bi800439t article EN Biochemistry 2008-08-01

In epithelia, cells adhere to each other in a dynamic fashion, allowing the change their shape and move along during morphogenesis. The regulation of adhesion occurs at belt-shaped adherens junction, zonula (ZA). Formation ZA depends on components Par-atypical PKC (Par-aPKC) complex polarity regulators. We have identified Lin11, Isl-1, Mec-3 (LIM) protein Smallish (Smash), orthologue vertebrate LMO7, as binding partner Bazooka/Par-3 (Baz), core component Par-aPKC complex. Smash also binds...

10.1083/jcb.201610098 article EN cc-by-nc-sa The Journal of Cell Biology 2018-01-22

The chlamydial deubiquitinase Cdu1 of the obligate intracellular human pathogenic bacterium Chlamydia trachomatis plays important roles in maintenance infection. Despite structural similarities shared with its homologue Cdu2, both DUBs display remarkable differences their enzymatic activity towards poly-UB chain substrates. Whereas is highly active K48- and K63- chains, Cdu2 restricted mostly to mono-UB Here, we shed light on molecular mechanisms differential substrate specificity better...

10.1371/journal.ppat.1012630 article EN cc-by PLoS Pathogens 2024-10-21
Coming Soon ...