Search Results - "Harkiolaki, M"

Supramolecular attack particles are autonomous killing entities released from cytotoxic T cells by Bálint, Š, Müller, S, Fischer, R, Kessler, B M, Harkiolaki, M, Valitutti, S, Dustin, M L

“…Cytotoxic T lymphocytes (CTLs) kill infected and cancerous cells. We detected transfer of cytotoxic multiprotein complexes, called supramolecular attack…”
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Correlative 3D cryo X-ray imaging reveals intracellular location and effect of designed antifibrotic protein-nanomaterial hybrids by Groen, J, Palanca, A, Aires, A, Conesa, J. J, Maestro, D, Rehbein, S, Harkiolaki, M, Villar, A. V, Cortajarena, A. L, Pereiro, E

“…Revealing the intracellular location of novel therapeutic agents is paramount for the understanding of their effect at the cell ultrastructure level. Here, we…”
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Structural basis for SH3 domain-mediated high-affinity binding between Mona/Gads and SLP-76 by Feller, Stephan M, Harkiolaki, Maria, Lewitzky, Marc, Gilbert, Robert J.C, Jones, EYvonne, Bourette, Roland P, Mouchiroud, Guy, Sondermann, Holger, Moarefi, Ismail

“…SH3 domains are protein recognition modules within many adaptors and enzymes. With more than 500 SH3 domains in the human genome, binding selectivity is a key…”
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The Crystal Structure of Trypanosoma cruzi dUTPase Reveals a Novel dUTP/dUDP Binding Fold by Harkiolaki, Maria, Dodson, Eleanor J, Bernier-Villamor, Victor, Turkenburg, Johan P, González-Pacanowska, Dolores, Wilson, Keith S

“…dUTPase is an essential enzyme involved with nucleotide metabolism and replication. We report here the X-ray structure of Trypanosoma cruzi dUTPase in its…”
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Crystallization and preliminary crystallographic analysis of deoxyuridine 5′-triphosphate nucleotidohydrolase from Bacillus subtilis by Persson, Rebecca, Harkiolaki, Maria, McGeehan, John, Wilson, Keith S.

“…Single crystals of purified homotrimeric deoxyuridine 5′‐triphosphate nucleotidohydrolase (dUTPase) from Bacillus subtilis have been grown under several…”
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New crystal forms of Trypanosoma cruzi dUTPase by Harkiolaki, Maria, Brzozowski, Andrzej Marek, Gonzalez-Pacanowska, Dolores, Hidalgo-Zarco, Fernando, Wilson, Keith S.

“…The dUTPase from Trypanosoma cruzi has been crystallized in two crystal forms, both belonging to space group P6322, with unit‐cell parameters a = b = 134.67, c…”
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ARP/wARP and molecular replacement by Perrakis, Anastassis, Harkiolaki, Maria, Wilson, Keith S., Lamzin, Victor S.

“…The aim of ARP/wARP is improved automation of model building and refinement in macromolecular crystallography. Once a molecular‐replacement solution has been…”
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The Crystal Structure of a Complex of Campylobacter jejuni dUTPase with Substrate Analogue Sheds Light on the Mechanism and Suggests the “Basic Module” for Dimeric d(C/U)TPases by Moroz, Olga V., Harkiolaki, Maria, Galperin, Michael Y., Vagin, Alexei A., González-Pacanowska, Dolores, Wilson, Keith S.

“…The crystal structure of the dUTPase from the important gastric pathogen Campylobacter jejuni has been solved at 1.65 Å spacing. This essential bacterial…”
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Mona/Gads SH3C Binding to Hematopoietic Progenitor Kinase 1 (HPK1) Combines an Atypical SH3 Binding Motif, R/KXXK, with a Classical PXXP Motif Embedded in a Polyproline Type II (PPII) Helix by Lewitzky, Marc, Harkiolaki, Maria, Domart, Marie-Charlotte, Jones, E Yvonne, Feller, Stephan M

“…Hematopoietic progenitor kinase 1 (HPK1) is implicated in signaling downstream of the T cell receptor. Its non-catalytic, C-terminal half contains several…”
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Crystal Structure and DNA Repair Activities of the AP Endonuclease from Leishmania major by Vidal, Antonio E., Harkiolaki, Maria, Gallego, Claribel, Castillo-Acosta, Victor M., Ruiz-Pérez, Luis M., Wilson, Keith, González-Pacanowska, Dolores

“…Apurinic/apyrimidinic endonucleases initiate the repair of abasic sites produced either spontaneously, from attack of bases by reactive oxygen species or as…”
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Structural basis for the oncogenic signalling complex formed by Grb2 and Gab2 in Her2 (ErbB2/Neu)-driven breast cancers and CML cells by Tsirka, T, Harkiolaki, M, Lewitzky, M, Wecklein, H, Bird, L, Jones, EY, Raabe, T, OReilly, N, Feller, SM

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A procedure for setting up high-throughput nanolitre crystallization experiments. II. Crystallization results by Brown, J., Walter, T. S., Carter, L., Abrescia, N. G. A., Aricescu, A. R., Batuwangala, T. D., Bird, L. E., Brown, N., Chamberlain, P. P., Davis, S. J., Dubinina, E., Endicott, J., Fennelly, J. A., Gilbert, R. J. C., Harkiolaki, M., Hon, W.-C., Kimberley, F., Love, C. A., Mancini, E. J., Manso-Sancho, R., Nichols, C. E., Robinson, R. A., Sutton, G. C., Schueller, N., Sleeman, M. C., Stewart-Jones, G. B., Vuong, M., Welburn, J., Zhang, Z., Stammers, D. K., Owens, R. J., Jones, E. Y., Harlos, K., Stuart, D. I.

“…An initial tranche of results from day‐to‐day use of a robotic system for setting up 100 nl‐scale vapour‐diffusion sitting‐drop protein crystallizations has…”
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