@article{BapolisiKielbBekiretal.2022,
  author    = {Bapolisi, Alain Murhimalika and Kielb, Patrycja and Bekir, Marek and Lehnen, Anne-Catherine and Radon, Christin and Laroque, Sophie and Wendler, Petra and M{\"u}ller-Werkmeister, Henrike and Hartlieb, Matthias},
  title     = {Antimicrobial polymers of linear and bottlebrush architecture},
  series = {Macromolecular rapid communications : publishing the newsletters of the European Polymer Federation},
  volume    = {43},
  journal   = {Macromolecular rapid communications : publishing the newsletters of the European Polymer Federation},
  number    = {19},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  issn      = {1521-3927},
  doi       = {10.1002/marc.202200288},
  pages     = {14},
  year      = {2022},
  abstract  = {Polymeric antimicrobial peptide mimics are a promising alternative for the future management of the daunting problems associated with antimicrobial resistance. However, the development of successful antimicrobial polymers (APs) requires careful control of factors such as amphiphilic balance, molecular weight, dispersity, sequence, and architecture. While most of the earlier developed APs focus on random linear copolymers, the development of APs with advanced architectures proves to be more potent. It is recently developed multivalent bottlebrush APs with improved antibacterial and hemocompatibility profiles, outperforming their linear counterparts. Understanding the rationale behind the outstanding biological activity of these newly developed antimicrobials is vital to further improving their performance. This work investigates the physicochemical properties governing the differences in activity between linear and bottlebrush architectures using various spectroscopic and microscopic techniques. Linear copolymers are more solvated, thermo-responsive, and possess facial amphiphilicity resulting in random aggregations when interacting with liposomes mimicking Escheria coli membranes. The bottlebrush copolymers adopt a more stable secondary conformation in aqueous solution in comparison to linear copolymers, conferring rapid and more specific binding mechanism to membranes. The advantageous physicochemical properties of the bottlebrush topology seem to be a determinant factor in the activity of these promising APs.},
  language  = {en}
}
@article{QiuZhangBicketal.2021,
  author    = {Qiu, Liang and Zhang, Haoran and Bick, Thomas and Martin, Johannes and Wendler, Petra and B{\"o}ker, Alexander and Glebe, Ulrich and Xing, Chengfen},
  title     = {Construction of highly ordered glyco-inside nano-assemblies through RAFT dispersion polymerization of galactose-decorated monomer},
  series = {Angewandte Chemie : a journal of the Gesellschaft Deutscher Chemiker ; International edition},
  volume    = {60},
  journal   = {Angewandte Chemie : a journal of the Gesellschaft Deutscher Chemiker ; International edition},
  number    = {20},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  issn      = {1433-7851},
  doi       = {10.1002/anie.202015692},
  pages     = {11098 -- 11103},
  year      = {2021},
  abstract  = {Glyco-assemblies derived from amphiphilic sugar-decorated block copolymers (ASBCs) have emerged prominently due to their wide application, for example, in biomedicine and as drug carriers. However, to efficiently construct these glyco-assemblies is still a challenge. Herein, we report an efficient technology for the synthesis of glyco-inside nano-assemblies by utilizing RAFT polymerization of a galactose-decorated methacrylate for polymerization-induced self-assembly (PISA). Using this approach, a series of highly ordered glyco-inside nano-assemblies containing intermediate morphologies were fabricated by adjusting the length of the hydrophobic glycoblock and the polymerization solids content. A specific morphology of complex vesicles was captured during the PISA process and the formation mechanism is explained by the morphology of its precursor and intermediate. Thus, this method establishes a powerful route to fabricate glyco-assemblies with tunable morphologies and variable sizes, which is significant to enable the large-scale fabrication and wide application of glyco-assemblies.},
  language  = {en}
}
@article{PetrovićWendler2021,
  author    = {Petrović, Saša and Wendler, Petra},
  title     = {A RADD approach to probing AAA plus protein function},
  series = {Nature structural \& molecular biology},
  volume    = {28},
  journal   = {Nature structural \& molecular biology},
  number    = {4},
  publisher = {Nature Publishing Group},
  address   = {Berlin},
  issn      = {1545-9993},
  doi       = {10.1038/s41594-021-00579-5},
  pages     = {329 -- 330},
  year      = {2021},
  abstract  = {AAA+ proteins (ATPases associated with various cellular activities) catalyze the energy-dependent movement or rearrangement of macromolecules. A new study addresses the important question of how to design a selective chemical inhibitor for specific proteins in this diverse superfamily. The powerful chemical genetics approach adds to a growing toolbox of applications that allow dissection of the functions of distinct AAA+ proteins in vivo, facilitating the first steps toward effective drug development.},
  language  = {en}
}
@article{BhatMilicicThieulinPardoetal.2017,
  author    = {Bhat, Javaid Y. and Milicic, Goran and Thieulin-Pardo, Gabriel and Bracher, Andreas and Maxwell, Andrew and Ciniawsky, Susanne and M{\"u}ller-Cajar, Oliver and Engen, John R. and Hartl, F. Ulrich and Wendler, Petra and Hayer-Hartl, Manajit},
  title     = {Mechanism of Enzyme Repair by the AAA(+) Chaperone Rubisco Activase},
  series = {Molecular cell},
  volume    = {67},
  journal   = {Molecular cell},
  publisher = {Cell Press},
  address   = {Cambridge},
  issn      = {1097-2765},
  doi       = {10.1016/j.molcel.2017.07.004},
  pages     = {744 -- 756},
  year      = {2017},
  abstract  = {How AAA(+) chaperones conformationally remodel specific target proteins in an ATP-dependent manner is not well understood. Here, we investigated the mechanism of the AAA(+) protein Rubisco activase (Rca) in metabolic repair of the photosynthetic enzyme Rubisco, a complex of eight large (RbcL) and eight small (RbcS) subunits containing eight catalytic sites. Rubisco is prone to inhibition by tight-binding sugar phosphates, whose removal is catalyzed by Rca. We engineered a stable Rca hexamer ring and analyzed its functional interaction with Rubisco. Hydrogen/deuterium exchange and chemical crosslinking showed that Rca structurally destabilizes elements of the Rubisco active site with remarkable selectivity. Cryo-electron microscopy revealed that Rca docks onto Rubisco over one active site at a time, positioning the C-terminal strand of RbcL, which stabilizes the catalytic center, for access to the Rca hexamer pore. The pulling force of Rca is fine-tuned to avoid global destabilization and allow for precise enzyme repair.},
  language  = {en}
}
@article{WendlerEnenkel2019,
  author    = {Wendler, Petra and Enenkel, Cordula},
  title     = {Nuclear Transport of Yeast Proteasomes},
  series = {Frontiers in molecular biosciences},
  volume    = {6},
  journal   = {Frontiers in molecular biosciences},
  publisher = {Frontiers Research Foundation},
  address   = {Lausanne},
  issn      = {2296-889X},
  doi       = {10.3389/fmolb.2019.00034},
  pages     = {12},
  year      = {2019},
  abstract  = {Proteasomes are key proteases in regulating protein homeostasis. Their holo-enzymes are composed of 40 different subunits which are arranged in a proteolytic core (CP) flanked by one to two regulatory particles (RP). Proteasomal proteolysis is essential for the degradation of proteins which control time-sensitive processes like cell cycle progression and stress response. In dividing yeast and human cells, proteasomes are primarily nuclear suggesting that proteasomal proteolysis is mainly required in the nucleus during cell proliferation. In yeast, which have a closed mitosis, proteasomes are imported into the nucleus as immature precursors via the classical import pathway. During quiescence, the reversible absence of proliferation induced by nutrient depletion or growth factor deprivation, proteasomes move from the nucleus into the cytoplasm. In the cytoplasm of quiescent yeast, proteasomes are dissociated into CP and RP and stored in membrane-less cytoplasmic foci, named proteasome storage granules (PSGs). With the resumption of growth, PSGs clear and mature proteasomes are transported into the nucleus by Blm10, a conserved 240 kDa protein and proteasome-intrinsic import receptor. How proteasomes are exported from the nucleus into the cytoplasm is unknown.},
  language  = {en}
}
@misc{SchieferdeckerWendler2019,
  author    = {Schieferdecker, Anne and Wendler, Petra},
  title     = {Structural mapping of missense mutations in the Pex1/Pex6 complex},
  series = {Postprints der Universit{\"a}t Potsdam : Mathematisch-Naturwissenschaftliche Reihe},
  journal   = {Postprints der Universit{\"a}t Potsdam : Mathematisch-Naturwissenschaftliche Reihe},
  number    = {1072},
  issn      = {1866-8372},
  doi       = {10.25932/publishup-47284},
  url       = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus4-472843},
  pages     = {27},
  year      = {2019},
  abstract  = {Peroxisome biogenesis disorders (PBDs) are nontreatable hereditary diseases with a broad range of severity. Approximately 65\% of patients are affected by mutations in the peroxins Pex1 and Pex6. The proteins form the heteromeric Pex1/Pex6 complex, which is important for protein import into peroxisomes. To date, no structural data are available for this AAA+ ATPase complex. However, a wealth of information can be transferred from low-resolution structures of the yeast scPex1/scPex6 complex and homologous, well-characterized AAA+ ATPases. We review the abundant records of missense mutations described in PBD patients with the aim to classify and rationalize them by mapping them onto a homology model of the human Pex1/Pex6 complex. Several mutations concern functionally conserved residues that are implied in ATP hydrolysis and substrate processing. Contrary to fold destabilizing mutations, patients suffering from function-impairing mutations may not benefit from stabilizing agents, which have been reported as potential therapeutics for PBD patients.},
  language  = {en}
}
@article{SchieferdeckerWendler2019,
  author    = {Schieferdecker, Anne and Wendler, Petra},
  title     = {Structural Mapping of Missense Mutations in the Pex1/Pex6 Complex},
  series = {International journal of molecular sciences},
  volume    = {20},
  journal   = {International journal of molecular sciences},
  number    = {15},
  publisher = {MDPI},
  address   = {Basel},
  issn      = {1422-0067},
  doi       = {10.3390/ijms20153756},
  pages     = {25},
  year      = {2019},
  abstract  = {Peroxisome biogenesis disorders (PBDs) are nontreatable hereditary diseases with a broad range of severity. Approximately 65\% of patients are affected by mutations in the peroxins Pex1 and Pex6. The proteins form the heteromeric Pex1/Pex6 complex, which is important for protein import into peroxisomes. To date, no structural data are available for this AAA+ ATPase complex. However, a wealth of information can be transferred from low-resolution structures of the yeast scPex1/scPex6 complex and homologous, well-characterized AAA+ ATPases. We review the abundant records of missense mutations described in PBD patients with the aim to classify and rationalize them by mapping them onto a homology model of the human Pex1/Pex6 complex. Several mutations concern functionally conserved residues that are implied in ATP hydrolysis and substrate processing. Contrary to fold destabilizing mutations, patients suffering from function-impairing mutations may not benefit from stabilizing agents, which have been reported as potential therapeutics for PBD patients.},
  language  = {en}
}