Publikationer av Philip Köck
Refereegranskade
Artiklar
[1]
P. J. B. Koeck, "Alternative Forward Models for Imaging Thick Specimens in Transmission Electron Microscopy," Microscopy and Microanalysis, vol. 29, no. 3, s. 1071-1076, 2023.
[2]
G. Chen et al., "Short hydrophobic loop motifs in BRICHOS domains determine chaperone activity against amorphous protein aggregation but not against amyloid formation," Communications Biology, vol. 6, no. 1, 2023.
[3]
M. Kaldmae et al., "A "spindle and thread"mechanism unblocks p53 translation N-terminal disorder," Structure, vol. 30, no. 5, s. 733-742.e7, 2022.
[4]
G. Chen et al., "Abilities of the BRICHOS domain to prevent neurotoxicity and fibril formation are dependent on a highly conserved Asp residue," RSC Chemical Biology, vol. 3, no. 11, s. 1342-1358, 2022.
[5]
X. Zhong et al., "Amyloid Fibril Formation of Arctic Amyloid-β 1-42 Peptide is Efficiently Inhibited by the BRICHOS Domain," ACS Chemical Biology, vol. 17, no. 8, s. 2201-2211, 2022.
[6]
P. J. B. Koeck och L. T. Barrett, "Particle dynamics simulations of a proposed charged particle phase plate for transmission electron microscopy," Ultramicroscopy, vol. 222, 2021.
[7]
P. J. B. Koeck, "Design of a Charged Particle Beam Phase Plate for Transmission Electron Microscopy," Ultramicroscopy, vol. 205, s. 62-69, 2019.
[8]
P. J. B. Koeck, "Design of an Electrostatic Phase Shifting Device for Biological Transmission Electron Microscopy," Ultramicroscopy, vol. 187, s. 107-112, 2018.
[9]
S. Trillo-Muyo et al., "Granule-stored MUC5B mucins are packed by the non-covalent formation of N-terminal head-to-head tetramers," Journal of Biological Chemistry, vol. 293, no. 15, s. 5746-5754, 2018.
[10]
P. J. B. Koeck, "An aperture design for single side band imaging in the transmission electron microscope," Ultramicroscopy, vol. 182, s. 81-84, 2017.
[11]
G. Chen et al., "Bri2 BRICHOS client specificity and chaperone activity are governed by assembly state," Nature Communications, vol. 8, 2017.
[12]
G. Rutsdottir et al., "Structural model of dodecameric heat-shock protein Hsp21 : Flexible N-terminal arms interact with client proteins while C-terminal tails maintain the dodecamer and chaperone activity," Journal of Biological Chemistry, vol. 292, no. 19, s. 8103-8121, 2017.
[13]
P. J. B. Koeck, "Annular dark field transmission electron microscopy for protein structure determination," Ultramicroscopy, vol. 161, s. 98-104, 2016.
[14]
J. Härmark, H. Hebert och P. J. B. Koeck, "Shell thickness determination of polymer-shelled microbubbles using transmission electron microscopy," Micron, vol. 85, s. 39-43, 2016.
[15]
Q. Kuang et al., "A Refined Single-Particle Reconstruction Procedure to Process Two-Dimensional Crystal Images from Transmission Electron Microscopy," Microscopy and Microanalysis, vol. 21, no. 4, s. 876-85, 2015.
[16]
Q. Kuang et al., "Free RCK Arrangement in Kch, a Putative Escherichia coli Potassium Channel, as Suggested by Electron Crystallography," Structure, vol. 23, no. 1, s. 199-205, 2015.
[17]
P. . J. B. Koeck, "Improved Hilbert phase contrast for transmission electron microscopy," Ultramicroscopy, vol. 154, s. 37-41, 2015.
[18]
P. J. B. Koeck, "Improved Zernike-type phase contrast for transmission electron microscopy," Journal of Microscopy, vol. 259, no. 1, s. 74-78, 2015.
[19]
J. Härmark et al., "Investigation of the elimination process of a multimodal polymer-shelled contrast agent in rats using ultrasound and transmission electron microscopy," Biomedical Spectroscopy and Imaging, vol. 4, no. 1, s. 81-93, 2015.
[20]
P. J. B. Koeck och A. Karshikoff, "Limitations of the linear and the projection approximations in three-dimensional transmission electron microscopy of fully hydrated proteins," Journal of Microscopy, vol. 259, no. 3, s. 197-209, 2015.
[21]
H. E. Nilsson et al., "Intestinal MUC2 Mucin Supramolecular Topology by Packing and Release Resting on D3 Domain Assembly," Journal of Molecular Biology, vol. 426, no. 14, s. 2567-2579, 2014.
[22]
D. Ambort et al., "Calcium and pH-dependent packing and release of the gel-forming MUC2 mucin," Proceedings of the National Academy of Sciences of the United States of America, vol. 109, no. 15, s. 5645-5650, 2012.
[23]
W. Lambert et al., "Subunit arrangement in the dodecameric chloroplast small heat shock protein Hsp21," Protein Science, vol. 20, no. 2, s. 291-301, 2011.
[24]
S. Wu et al., "Single-particle cryoelectron microscopy analysis reveals the HIV-1 spike as a tripod structure," Proceedings of the National Academy of Sciences of the United States of America, vol. 107, no. 44, s. 18844-18849, 2010.
[25]
S. Wu et al., "Turning of the receptor binding domains opens up the murine leukaemia virus Env for membrane fusion," EMBO Journal, vol. 27, no. 20, s. 2799-2808, 2008.
[26]
P. J. B. Koeck et al., "Single particle refinement in electron crystallography : A pilot study," Journal of Structural Biology, vol. 160, no. 3, s. 344-352, 2007.
[27]
K. Cheng et al., "Rapana thomasiana hemocyanin (RtH) : Comparison of the two isoforms, RtH1 and RtH2, at 19 Å and 16 Å resolution," Micron, vol. 37, no. 6, s. 566-576, 2006.
[28]
H. Elmlund et al., "The cyclin-dependent kinase 8 module sterically blocks Mediator interactions with RNA polymerase II," Proceedings of the National Academy of Sciences of the United States of America, vol. 103, no. 43, s. 15788-15793, 2006.
[29]
P. J. B. Koeck, "Missing Data in Image and Signal Processing: The case of binary objects," Optik (Stuttgart), vol. 115, no. 10, s. 459-472, 2004.
Konferensbidrag
[30]
P. J. B. Koeck et al., "3D-correlation-averaging for membrane-protein-crystals," i EMC 2008 14th European Microscopy Congress, 2008, s. 55-56.
[31]
P. Purhonen et al., "Cryo-EM studies of renal Na,K-ATPase in native membranes," i Proc of the 12th International ATPase Conference. Na,K-ATPase and related transport ATPases of P-type, 2008.
[32]
P. J. B. Koeck et al., "Single-particle refinement in electron crystallography of membrane-proteins," i Scandem 2007, Annual Meeting of the Nordic Microscopy Society. Espoo, Finland. June 18-20th 2007, 2007.
[33]
P. Purhonen et al., "Three-dimensional structure of renal Na,K-ATPase as determined by cryo-electron microscopy," i Scandem 2007, Annual Meeting of the Nordic Microscopy Society. Espoo, Finland. June 18-20th 2007, 2007.
[34]
K. Cheng et al., "Comparison of the two Rapana thomasiana Hemocyanin isoforms : RtH1 and RtH2," i Proc 16. International Microscopy Conference, 2006.
[35]
P. Purhonen et al., "Renal Na, K-ATPase Structure from Cryo-Electron Microscopy with 2-D Crystals Showing Structural Variability," i Proc. of the 13th European Congress on Electron Microscopy, 2004.
[36]
K. Cheng et al., "Stainless Models of Rapana Thomasiana Hemocyanin," i Proc. of the 13th European Congress on Electron Microscopy, 2004, s. 22-27.
Icke refereegranskade
Övriga
[37]
K. Cheng et al., "Low resolution structure and apparent melting temperature of the chaperonin from Pyrococcus furiosus," (Manuskript).
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2024-04-28 02:32:21