Search Results - "KURZ, Mareike"

Properties of the Thioredoxin Fold Superfamily Are Modulated by a Single Amino Acid Residue by Ren, Guoping, Stephan, Daniel, Xu, Zhaohui, Zheng, Ying, Tang, Danming, Harrison, Rosemary S., Kurz, Mareike, Jarrott, Russell, Shouldice, Stephen R., Hiniker, Annie, Martin, Jennifer L., Heras, Begonña, Bardwell, James C.A.

“…The ubiquitous thioredoxin fold proteins catalyze oxidation, reduction, or disulfide exchange reactions depending on their redox properties. They also play…”
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Structure and Substrate-Induced Conformational Changes of the Secondary Citrate/Sodium Symporter CitS Revealed by Electron Crystallography by Kebbel, Fabian, Kurz, Mareike, Arheit, Marcel, Grütter, Markus G., Stahlberg, Henning

“…The secondary Na+/citrate symporter CitS of Klebsiella pneumoniae is the best-characterized member of the 2-hydroxycarboxylate transporter family. The recent…”
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Interaction of the Sliding Clamp β-Subunit and Hda, a DnaA-Related Protein by KURZ, Mareike, DALRYMPLE, Brian, WIJFFELS, Gene, KONGSUWAN, Kritaya

“…Article Usage Stats Services JB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley…”
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Staphylococcus aureus DsbA Does Not Have a Destabilizing Disulfide by Heras, Begoña, Kurz, Mareike, Jarrott, Russell, Shouldice, Stephen R., Frei, Patrick, Robin, Gautier, Čemažar, Maša, Thöny-Meyer, Linda, Glockshuber, Rudi, Martin, Jennifer L.

“…In Gram-negative bacteria, the introduction of disulfide bonds into folding proteins occurs in the periplasm and is catalyzed by donation of an energetically…”
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The Structure of Bradyrhizobium japonicum Transcription Factor FixK2 Unveils Sites of DNA Binding and Oxidation by Bonnet, Mariette, Kurz, Mareike, Mesa, Socorro, Briand, Christophe, Hennecke, Hauke, Grütter, Markus G.

“…FixK2 is a regulatory protein that activates a large number of genes for the anoxic and microoxic, endosymbiotic, and nitrogen-fixing life styles of the…”
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Projection Structure of the Secondary Citrate/Sodium Symporter CitS at 6 Å Resolution by Electron Crystallography by Kebbel, Fabian, Kurz, Mareike, Grütter, Markus G., Stahlberg, Henning

“…CitS from Klebsiella pneumoniae acts as a secondary symporter of citrate and sodium ions across the inner membrane of the host. The protein is the best…”
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The name's bond......disulfide bond by Heras, Begoña, Kurz, Mareike, Shouldice, Stephen R, Martin, Jennifer L

“…A repeating theme in the structural biology of disulfide oxidants and isomerases is the extraordinary architectural similarity between functionally related…”
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High-throughput counter-diffusion capillary crystallization and in situ diffraction using high-pressure freezing in protein crystallography by Kurz, Mareike, Blattmann, Beat, Kaech, Andres, Briand, Christophe, Reardon, Paul, Ziegler, Urs, Gruetter, Markus G.

“…Post‐crystallization treatments such as manual fishing of crystals and soaking in cryoprotectant solutions, especially of large macromolecular complexes and…”
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Staphylococcus aureus DsbA Does Not Have a Destabilizing Disulfide: A NEW PARADIGM FOR BACTERIAL OXIDATIVE FOLDING by Heras, Begoña, Kurz, Mareike, Jarrott, Russell, Shouldice, Stephen R, Frei, Patrick, Robin, Gautier, Čemažar, Maša, Thöny-Meyer, Linda, Glockshuber, Rudi, Martin, Jennifer L

“…In Gram-negative bacteria, the introduction of disulfide bonds into folding proteins occurs in the periplasm and is catalyzed by donation of an energetically…”
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Structural and functional characterization of the oxidoreductase alpha-DsbA1 from Wolbachia pipientis by Kurz, Mareike, Iturbe-Ormaetxe, Iñaki, Jarrott, Russell, Shouldice, Stephen R, Wouters, Merridee A, Frei, Patrick, Glockshuber, Rudi, O'Neill, Scott L, Heras, Begoña, Martin, Jennifer L

“…The alpha-proteobacterium Wolbachia pipientis is a highly successful intracellular endosymbiont of invertebrates that manipulates its host's reproductive…”
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The name's bond……disulfide bond by Heras, Begoña, Kurz, Mareike, Shouldice, Stephen R, Martin, Jennifer L

“…A repeating theme in the structural biology of disulfide oxidants and isomerases is the extraordinary architectural similarity between functionally related…”
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Properties of the Thioredoxin Fold Superfamily Are Modulated by a Single Amino Acid ResidueS by Ren, Guoping, Stephan, Daniel, Xu, Zhaohui, Zheng, Ying, Tang, Danming, Harrison, Rosemary S., Kurz, Mareike, Jarrott, Russell, Shouldice, Stephen R., Hiniker, Annie, Martin, Jennifer L., Heras, Begoña, Bardwell, James C. A.

“…The ubiquitous thioredoxin fold proteins catalyze oxidation, reduction, or disulfide exchange reactions depending on their redox properties. They also play…”
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Incorporating a TEV cleavage site reduces the solubility of nine recombinant mouse proteins by Kurz, Mareike, Cowieson, Nathan P., Robin, Gautier, Hume, David A., Martin, Jennifer L., Kobe, Bostjan, Listwan, Pawel

“…Failure to express soluble proteins in bacteria is mainly attributed to the properties of the target protein itself, as well as the choice of the vector, the…”
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Cloning, expression, purification and characterization of a DsbA-like protein from Wolbachia pipientis by Kurz, Mareike, Iturbe-Ormaetxe, Iñaki, Jarrott, Russell, Cowieson, Nathan, Robin, Gautier, Jones, Alun, King, Gordon J., Frei, Patrick, Glockshuber, Rudi, O’Neill, Scott L., Heras, Begoña, Martin, Jennifer L.

“…Wolbachia pipientis are obligate endosymbionts that infect a wide range of insect and other arthropod species. They act as reproductive parasites by…”
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Modification of recombinatorial cloning for small affinity tag fusion protein construct generation by Listwan, Pawel, Cowieson, Nathan, Kurz, Mareike, Hume, David A., Martin, Jennifer L., Kobe, Bostjan

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Pilot studies on the parallel production of soluble mouse proteins in a bacterial expression system by Cowieson, Nathan P, Listwan, Pawel, Kurz, Mareike, Aagaard, Anna, Ravasi, Timothy, Wells, Christine, Huber, Thomas, Hume, David A, Kobe, Bostjan, Martin, Jennifer L

“…We investigated the parallel production in medium throughput of mouse proteins, using protocols that involved recombinatorial cloning, protein expression…”
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