Schaap, Iwan A. T.

[["dc.bibliographiccitation.firstpage","282"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Journal of Structural Biology"],["dc.bibliographiccitation.lastpage","292"],["dc.bibliographiccitation.volume","158"],["dc.contributor.author","Schaap, Iwan A. T."],["dc.contributor.author","Hoffmann, Bernd"],["dc.contributor.author","Carrasco, Carolina"],["dc.contributor.author","Merkel, Rudolf"],["dc.contributor.author","Schmidt, Christoph"],["dc.date.accessioned","2017-09-07T11:49:47Z"],["dc.date.available","2017-09-07T11:49:47Z"],["dc.date.issued","2007"],["dc.description.abstract","Tau is one of the most abundant microtubule-associated proteins involved in kinetic stabilization and bundling of axonal microtubules. Although intense research has revealed much about tau function and its involvement in Alzheimer's disease during the past years, it still remains unclear how exactly tau binds on microtubules and if the kinetic stabilization of microtubules by tau is accompanied, at least in part, by a mechanical reinforcement of microtubules. In this paper, we have used atomic force microscopy to address both aspects by visualizing and mechanically analyzing microtubules in the presence of native tau isoforms. We could show that tau at saturating concentrations forms a 1 nm thick layer around the microtubule, but leaves the protofilament structure well visible. The latter observation argues for tau binding mainly along and not across the protofilaments. The radial elasticity of microtubules was almost unaffected by tau, consistent with tau binding along the tops of the protofilaments. Tau did increase the resistance of microtubules against rupture. Finite-element calculations confirmed our findings. (c) 2006 Elsevier Inc. All rights reserved."],["dc.identifier.doi","10.1016/j.jsb.2006.11.010"],["dc.identifier.gro","3143493"],["dc.identifier.isi","000246927800003"],["dc.identifier.pmid","17329123"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1014"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Academic Press Inc Elsevier Science"],["dc.relation.issn","1047-8477"],["dc.title","Tau protein binding forms a 1 nm thick layer along protofilaments without affecting the radial elasticity of microtubules"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1100"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Biophysical Journal"],["dc.bibliographiccitation.lastpage","1108"],["dc.bibliographiccitation.volume","100"],["dc.contributor.author","Carrasco, Carolina"],["dc.contributor.author","Luque, A."],["dc.contributor.author","Hernando-Perez, Mercedes"],["dc.contributor.author","Miranda, Roberto"],["dc.contributor.author","Carrascosa, Jose L."],["dc.contributor.author","Serena, P. A."],["dc.contributor.author","de Ridder, M."],["dc.contributor.author","Raman, A."],["dc.contributor.author","Gomez-Herrero, J."],["dc.contributor.author","Schaap, I. A. T."],["dc.contributor.author","Reguera, David"],["dc.contributor.author","de Pablo, Pedro J."],["dc.date.accessioned","2018-11-07T08:59:13Z"],["dc.date.available","2018-11-07T08:59:13Z"],["dc.date.issued","2011"],["dc.description.abstract","Mechanical properties of biological molecular aggregates are essential to their function. A remarkable example are double-stranded DNA viruses such as the phi 29 bacteriophage, that not only has to withstand pressures of tens of atmospheres exerted by the confined DNA, but also uses this stored elastic energy during DNA translocation into the host. Here we show that empty prolated phi 29 bacteriophage proheads exhibit an intriguing anisotropic stiffness which behaves counterintuitively different from standard continuum elasticity predictions. By using atomic force microscopy, we find that the phi 29 shells are approximately two-times stiffer along the short than along the long axis. This result can be attributed to the existence of a residual stress, a hypothesis that we confirm by coarse-grained simulations. This built-in stress of the virus prohead could be a strategy to provide extra mechanical strength to withstand the DNA compaction during and after packing and a variety of extracellular conditions, such as osmotic shocks or dehydration."],["dc.identifier.doi","10.1016/j.bpj.2011.01.008"],["dc.identifier.isi","000287624000038"],["dc.identifier.pmid","21320456"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/23836"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Cell Press"],["dc.relation.issn","0006-3495"],["dc.title","Built-In Mechanical Stress in Viral Shells"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2450"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","Biophysical Journal"],["dc.bibliographiccitation.lastpage","2456"],["dc.bibliographiccitation.volume","100"],["dc.contributor.author","Schaap, Iwan A. T."],["dc.contributor.author","Carrasco, Carolina"],["dc.contributor.author","Pablo, Pedro J. de"],["dc.contributor.author","Schmidt, Christoph"],["dc.date.accessioned","2017-09-07T11:44:16Z"],["dc.date.available","2017-09-07T11:44:16Z"],["dc.date.issued","2011"],["dc.description.abstract","Motor proteins of the kinesin family move actively along microtubules to transport cargo within cells. How exactly a single motor proceeds on the 13 narrow lanes or protofilaments of a microtubule has not been visualized directly, and there persists controversy on the relative position of the two kinesin heads in different nucleotide states. We have succeeded in imaging Kinesin-1 dimers immobilized on microtubules with single-head resolution by atomic force microscopy. Moreover, we could catch glimpses of single Kinesin-1 dimers in their motion along microtubules with nanometer resolution. We find in our experiments that frequently both heads of one dimer are microtubule-bound at submicromolar ATP concentrations. Furthermore, we could unambiguously resolve that both heads bind to the same protofilament, instead of straddling two, and remain on this track during processive movement."],["dc.identifier.doi","10.1016/j.bpj.2011.04.015"],["dc.identifier.gro","3142727"],["dc.identifier.isi","000290830900016"],["dc.identifier.pmid","21575579"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/163"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Cell Press"],["dc.relation.issn","0006-3495"],["dc.title","Kinesin Walks the Line: Single Motors Observed by Atomic Force Microscopy"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1521"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Biophysical Journal"],["dc.bibliographiccitation.lastpage","1531"],["dc.bibliographiccitation.volume","91"],["dc.contributor.author","Schaap, Iwan A. T."],["dc.contributor.author","Carrasco, Carolina"],["dc.contributor.author","Pablo, Pedro J. de"],["dc.contributor.author","MacKintosh, Frederick C."],["dc.contributor.author","Schmidt, Christoph"],["dc.date.accessioned","2017-09-07T11:52:37Z"],["dc.date.available","2017-09-07T11:52:37Z"],["dc.date.issued","2006"],["dc.description.abstract","We tested the mechanical properties of single microtubules by lateral indentation with the tip of an atomic force microscope. Indentations up to similar to 3.6 nm, i.e., 15% of the microtubule diameter, resulted in an approximately linear elastic response, and indentations were reversible without hysteresis. At an indentation force of around 0.3 nN we observed an instability corresponding to an similar to 1-nm indentation step in the taxol-stabilized microtubules, which could be due to partial or complete rupture of a relatively small number of lateral or axial tubulin-tubulin bonds. These indentations were reversible with hysteresis when the tip was retracted and no trace of damage was observed in subsequent high-resolution images. Higher forces caused substantial damage to the microtubules, which either led to depolymerization or, occasionally, to slowly reannealing holes in the microtubule wall. We modeled the experimental results using finite-element methods and find that the simple assumption of a homogeneous isotropic material, albeit structured with the characteristic proto. lament corrugations, is sufficient to explain the linear elastic response of microtubules."],["dc.identifier.doi","10.1529/biophysj.105.077826"],["dc.identifier.gro","3143644"],["dc.identifier.isi","000239242000037"],["dc.identifier.pmid","16731557"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1181"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0006-3495"],["dc.title","Elastic response, buckling, and instability of microtubules under radial indentation"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]