Search Results - "Hol, Wim G.J."

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  1. 1

    Calcium Is Essential for the Major Pseudopilin in the Type 2 Secretion System by Korotkov, Konstantin V., Gray, Miranda D., Kreger, Allison, Turley, Stewart, Sandkvist, Maria, Hol, Wim G.J.

    Published in The Journal of biological chemistry (18-09-2009)
    “…The pseudopilus is a key feature of the type 2 secretion system (T2SS) and is made up of multiple pseudopilins that are similar in fold to the type 4 pilins…”
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  2. 2

    The type II secretion system: biogenesis, molecular architecture and mechanism by Korotkov, Konstantin V., Sandkvist, Maria, Hol, Wim G. J.

    Published in Nature reviews. Microbiology (01-05-2012)
    “…Key Points The type II secretion system (T2SS) is a double-membrane-spanning protein secretion system composed of 12–15 different general secretory pathway…”
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  3. 3

    The Crystal Structure of Human Tyrosyl-DNA Phosphodiesterase, Tdp1 by Davies, Douglas R, Interthal, Heidrun, Champoux, James J, Hol, Wim G.J

    Published in Structure (London) (01-02-2002)
    “…Tyrosyl-DNA phosphodiesterase (Tdp1) catalyzes the hydrolysis of a phosphodiester bond between a tyrosine residue and a DNA 3′ phosphate. The enzyme appears to…”
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  4. 4

    A general protocol for the generation of Nanobodies for structural biology by Pardon, Els, Laeremans, Toon, Triest, Sarah, Rasmussen, Søren G F, Wohlkönig, Alexandre, Ruf, Armin, Muyldermans, Serge, Hol, Wim G J, Kobilka, Brian K, Steyaert, Jan

    Published in Nature protocols (01-03-2014)
    “…There is growing interest in using antibodies as auxiliary tools to crystallize proteins. Here we describe a general protocol for the generation of Nanobodies…”
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  5. 5

    Secretins: dynamic channels for protein transport across membranes by Korotkov, Konstantin V., Gonen, Tamir, Hol, Wim G.J.

    “…Secretins form megadalton bacterial-membrane channels in at least four sophisticated multiprotein systems that are crucial for translocation of proteins and…”
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  6. 6

    The Crystal Structure of the Periplasmic Domain of the Type II Secretion System Protein EpsM From Vibrio cholerae: The Simplest Version of the Ferredoxin Fold by Abendroth, Jan, Rice, Adrian E, McLuskey, Karen, Bagdasarian, Michael, Hol, Wim G.J

    Published in Journal of molecular biology (30-04-2004)
    “…The terminal branch of the general secretion pathway (Gsp or type II secretion system) is used by several pathogenic bacteria for the secretion of their…”
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  7. 7

    The 1.25 Å resolution refinement of the cholera toxin B-pentamer: evidence of peptide backbone strain at the receptor-binding site by Merritt, Ethan A, Kuhn, Peter, Sarfaty, Steve, Erbe, Jarrod L, Holmes, Randall K, Hol, Wim G.J

    Published in Journal of molecular biology (09-10-1998)
    “…Crystals of the 61 kDa complex of the cholera toxin B-pentamer with the ganglioside G M1receptor pentasaccharide diffract to near-atomic resolution. We have…”
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  8. 8

    Structure of the cholera toxin secretion channel in its closed state by Hol, Wim G J, Gonen, Tamir, Reichow, Steve L, Korotkov, Konstantin V

    Published in Nature structural & molecular biology (01-10-2010)
    “…Secretins are bacterial outer membrane proteins involved in different pathways for protein secretion or macromolecular complex assembly. Secretin can form a…”
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  9. 9

    Structure of the GspK-GspI-GspJ complex from the enterotoxigenic Escherichia coli type 2 secretion system by Korotkov, Konstantin V, Hol, Wim G J

    Published in Nature structural & molecular biology (01-05-2008)
    “…Gram-negative bacteria translocate various proteins including virulence factors across their outer membrane via type 2 secretion systems (T2SSs). T2SSs are…”
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  10. 10
  11. 11

    Hexamers of the Type II Secretion ATPase GspE from Vibrio cholerae with Increased ATPase Activity by Lu, Connie, Turley, Stewart, Marionni, Samuel T., Park, Young-Jun, Lee, Kelly K., Patrick, Marcella, Shah, Ripal, Sandkvist, Maria, Bush, Matthew F., Hol, Wim G.J.

    Published in Structure (London) (03-09-2013)
    “…The type II secretion system (T2SS), a multiprotein machinery spanning two membranes in Gram-negative bacteria, is responsible for the secretion of folded…”
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  12. 12

    Distinct States of Methionyl-tRNA Synthetase Indicate Inhibitor Binding by Conformational Selection by Koh, Cho Yeow, Kim, Jessica E., Shibata, Sayaka, Ranade, Ranae M., Yu, Mingyan, Liu, Jiyun, Gillespie, J. Robert, Buckner, Frederick S., Verlinde, Christophe L.M.J., Fan, Erkang, Hol, Wim G.J.

    Published in Structure (London) (10-10-2012)
    “…To guide development of new drugs targeting methionyl-tRNA synthetase (MetRS) for treatment of human African trypanosomiasis, crystal structure determinations…”
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  13. 13

    Functional and Structural Characterization of Vibrio cholerae Extracellular Serine Protease B, VesB by Gadwal, Shilpa, Korotkov, Konstantin V., Delarosa, Jaclyn R., Hol, Wim G.J., Sandkvist, Maria

    Published in The Journal of biological chemistry (21-03-2014)
    “…The chymotrypsin subfamily A of serine proteases consists primarily of eukaryotic proteases, including only a few proteases of bacterial origin. VesB, a newly…”
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  14. 14

    In vivo cross-linking of EpsG to EpsL suggests a role for EpsL as an ATPase-pseudopilin coupling protein in the Type II secretion system of Vibrio cholerae by Gray, Miranda D, Bagdasarian, Michael, Hol, Wim G.J, Sandkvist, Maria

    Published in Molecular microbiology (01-02-2011)
    “…The type II secretion system is a multi-protein complex that spans the cell envelope of Gram-negative bacteria and promotes the secretion of proteins,…”
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  15. 15

    Structural and functional studies on the interaction of GspC and GspD in the type II secretion system by Korotkov, Konstantin V, Johnson, Tanya L, Jobling, Michael G, Pruneda, Jonathan, Pardon, Els, Héroux, Annie, Turley, Stewart, Steyaert, Jan, Holmes, Randall K, Sandkvist, Maria, Hol, Wim G J

    Published in PLoS pathogens (01-09-2011)
    “…Type II secretion systems (T2SSs) are critical for secretion of many proteins from Gram-negative bacteria. In the T2SS, the outer membrane secretin GspD forms…”
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  16. 16

    An unexpected extended conformation for the third TPR motif of the peroxin PEX5 from Trypanosoma brucei by Kumar, Abhinav, Roach, Claudia, Hirsh, Irwin S, Turley, Stewart, deWalque, Stéphane, Michels, Paul A.M, Hol, Wim G.J

    Published in Journal of molecular biology (16-03-2001)
    “…A number of helix-rich protein motifs are involved in a variety of critical protein-protein interactions in living cells. One of these is the tetratrico…”
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  17. 17

    Two Sensor Kinases Contribute to the Hypoxic Response of Mycobacterium tuberculosis by Roberts, David M., Liao, Reiling P., Wisedchaisri, Goragot, Hol, Wim G.J., Sherman, David R.

    Published in The Journal of biological chemistry (28-05-2004)
    “…Current estimates indicate that nearly a third of the world's population is latently infected with Mycobacterium tuberculosis. Reduced oxygen tension and…”
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  18. 18

    The dimer formed by the periplasmic domain of EpsL from the Type 2 Secretion System of Vibrio parahaemolyticus by Abendroth, Jan, Kreger, Allison C., Hol, Wim G.J.

    Published in Journal of structural biology (01-11-2009)
    “…The Type 2 Secretion System (T2SS), occurring in many Gram-negative bacteria, is responsible for the transport of a diversity of proteins from the periplasm…”
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  19. 19

    A Protein-Protein Interaction Map of Trypanosome ∼20S Editosomes by Schnaufer, Achim, Wu, Meiting, Park, Young-jun, Nakai, Tadashi, Deng, Junpeng, Proff, Rose, Hol, Wim G.J., Stuart, Kenneth D.

    Published in The Journal of biological chemistry (19-02-2010)
    “…Mitochondrial mRNA editing in trypanosomatid parasites involves several multiprotein assemblies, including three very similar complexes that contain the key…”
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  20. 20

    Structural Basis for the Activation of Cholera Toxin by Human ARF6-GTP by O'Neal, Claire J, Jobling, Michael G, Holmes, Randall K, Hol, Wim G. J

    “…The Vibrio cholerae bacterium causes devastating diarrhea when it infects the human intestine. The key event is adenosine diphosphate (ADP)-ribosylation of the…”
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