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Welcome to the Pubget Medical Subject Headings (MESH) browser. Click on a topic or subtopic below to explore related papers. In the gold box is the most recent paper about the current MESH term, and below are 20 related papers.
Cryoelectron Microscopy (0):
Recent article
Cryoelectron Microscopy
Abstract
We use cryo-electron microscopy to determine the subnanometre structures of Cascade before and after binding to a target sequence. These structures reveal a sea-horse-shaped architecture in which the crRNA is displayed along a helical arrangement of protein subunits that protect the crRNA from degra...
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PMID: 21938068
PDF is available here.
PDF is available here.
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Biochimica et Biophysica Acta (1808)10 2011
Abstract
We studied the potential of monoolein (MO) as helper lipid for cellular transfection. Lipoplexes composed of pDNA and dioctadecyldimethylammonium bromide (DODAB)/1-monooleoyl-rac-glycerol (MO) at different molar ratios (4:1, 2:1 and 1:1) and at different cationic lipid/DNA ratios were investigated....
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PMID: 21787746
PDF is available here.
PDF is available here.
Abstract
We demonstrate that amelogenin undergoes stepwise hierarchical self-assembly. Furthermore, our results indicate that interactions between amelogenin hydrophilic C-terminal telopeptides are essential for oligomer formation and for subsequent steps of hierarchical self-assembly. We further show that a...
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PMID: 21825148
PDF is available here.
PDF is available here.
Abstract
We developed a directed weighted graph, the topology graph, to represent the secondary structure assignment problem. We prove that the problem of finding the valid topology with the minimum cost is NP hard. We developed an O(N(2)2(N)) dynamic programming algorithm to identify the topology with the m...
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PMID: 21714133
PDF is available here.
PDF is available here.
Abstract
The complex molecular events responsible for coordinating chromosome replication and segregation with cell division and growth are collectively known as the cell cycle. Progression through the cell cycle is orchestrated by the interplay between controlled protein synthesis and degrad...
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PMID: 21092369
PDF is available here.
PDF is available here.
Biochimica et Biophysica Acta (1808)8 2011
Abstract
We explain why this limited, all-or-none leakage could nevertheless account for the killing of virtually all fungi whereas the same extent of graded vesicle leakage may be biologically irrelevant. Then, crystallization of AS1 and micellization of plipastatins cause a cut-off in leakage at 15% that m...
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PMID: 21545788
PDF is available here.
PDF is available here.
Abstract
We derived a 22 Å-resolution three-dimensional (3D) density map of LDL using cryo-electron microscopy and image reconstruction, which showed a backbone of high-density regions that encircle the LDL particle. Additional high-density belts complemented this backbone high density to enclose the edge o...
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PMID: 21460103
PDF is available here.
PDF is available here.
Abstract
When the ribosome machinery reaches a stop codon in the mRNA, protein synthesis stops, and nascent polypeptide release is catalysed by class-I release factors (RFs); class-II RFs then promote the release of class-I RFs. Cryo electron microscopy structures of termination complexes and crystal structur...
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PMID: 21420300
PDF is available here.
PDF is available here.
Abstract
To increase our current understanding of cellular processes, such as cell signaling and division, knowledge is needed about the spatial and temporal organization of the proteome at different organizational levels. These levels cover a wide range of length and time scales: from the at...
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PMID: 21094684
PDF is available here.
PDF is available here.
Abstract
I review recent progress in obtaining structural information for virions, procapsids and the individual motor protein components, and discuss single-molecule in vitro packaging reactions, which have yielded important new information about the mechanism by which these powerful molecular machines tran...
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PMID: 21836625
PDF is available here.
PDF is available here.
Abstract
We report the crystal structures of the precursor p62-E1 heterodimer and of the mature E3-E2-E1 glycoprotein complexes. The resulting atomic models allow the synthesis of a wealth of genetic, biochemical, immunological and electron microscopy data accumulated over the years on alphaviruses in genera...
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PMID: 21124458
PDF is available here.
PDF is available here.
Abstract
We use multiparticle cryoelectron microscopy analysis to resolve two previously unseen subpopulations within Thermus thermophilus EF-G-ribosome complexes at subnanometre resolution, one of them with a partly translocated tRNA. Comparison of these substates reveals that translocation of tRNA on the 3...
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PMID: 21124459
PDF is available here.
PDF is available here.
Abstract
We report the structure of an alphavirus spike, crystallized at low pH, representing an intermediate in the fusion process and clarifying the maturation process. The trimer of E2-E1 in the crystal structure is similar to the spikes in the neutral pH virus except that the E2 middle region is disorder...
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PMID: 21124457
PDF is available here.
PDF is available here.
Nature Materials (9)12 2010
Abstract
We show that collagen functions in synergy with inhibitors of hydroxyapatite nucleation to actively control mineralization. The positive net charge close to the C-terminal end of the collagen molecules promotes the infiltration of the fibrils with amorphous calcium phosphate (ACP). Furthermore, the...
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PMID: 20972429
PDF is available here.
PDF is available here.
EMBO Journal (29)20 2010
Abstract
We studied the structure and function of the kinesin-8 motor domain. We determined the first crystal structure of a kinesin-8 and used cryo-electron microscopy to calculate the structure of the microtubule-bound motor. Microtubule-bound kinesin-8 reveals a new conformation compared with the crystal...
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PMID: 20818331
PDF is available here.
PDF is available here.
Abstract
We present a subnanometre-resolution cryo-electron microscopy reconstruction of the human Ndc80 complex bound to microtubules, sufficient for precise docking of crystal structures of the component proteins. We find that the Ndc80 complex binds the microtubule with a tubulin monomer repeat, recognizi...
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PMID: 20944740
PDF is available here.
PDF is available here.
Abstract
We found that at a charge ratio (rho) of 4.0 lipoplexes had optimum characteristics for gene delivery in vitro. To decrease the size of lipoplexes, we used a method of continuous-flow microfluidics. PEGylation of lipoplexes did not hinder internalization, but was found to hamper transfection. To dis...
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PMID: 19947825
PDF is available here.
PDF is available here.
Abstract
Our results in this study of b1b in the Escherichia coli 70S ribosome suggest that the intrinsic molecular features of the bridging proteins allow the bridge to modulate the ratchet-like motion in a controlled manner. Additionally, another large subunit protein, L31, seems to participate with S13 an...
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PMID: 20643101
PDF is available here.
PDF is available here.
Journal of Molecular Biology (401)2 2010
Abstract
We assayed the ability of bacteriophage MS2 coat protein to package large, defined fragments of its genomic, single-stranded RNA. We show that the efficiency of packaging into a T=3 capsid in vitro is inversely proportional to RNA length, implying that there is a free-energy barrier to be overcome d...
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PMID: 20684044
PDF is available here.
PDF is available here.
Abstract
We combine structural and single molecule fluorescence methods to examine how PRC1, the human MAP65, crosslinks antiparallel microtubules. We find that PRC1's microtubule binding is mediated by a structured domain with a spectrin-fold and an unstructured Lys/Arg-rich domain. These two domains, at ea...
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PMID: 20691902
PDF is available here.
PDF is available here.
Scientific American (303)2 2010
Abstract
Abstract
We provide a comprehensive analysis of the current structural knowledge on the RP, including structures of the RP subunits, physical protein-protein interactions, and cryoelectron microscopy data. These data allowed us to compute an atomic model for the CP-AAA-ATPase subcomplex. In addition to this...
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PMID: 20467039
PDF is available here.
PDF is available here.
Journal of Virology (84)16 2010
Abstract
During dengue virus replication, an incomplete cleavage of the envelope glycoprotein prM, generates a mixture of mature (prM-less) and prM-containing, immature extracellular particles. In this study, sequential immunoprecipitation and cryoelectron microscopy revealed a third type of extracellular pa...
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PMID: 20519400
PDF is available here.
PDF is available here.
Journal of General Virology (91)Pt 8 2010
Abstract
Cell entry and membrane fusion of the hepatitis C virus (HCV) depend on its envelope glycoproteins E1 and E2. HCV pseudotyped particles (HCVpps) are relevant and popular models to study the early steps of the HCV life cycle. However, no structural characterization of HCVpp has been available so far....
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PMID: 20375221
PDF is available here.
PDF is available here.
Journal of Biological Chemistry (285)30 2010
Abstract
We used cryoelectron microscopy to characterize structural changes induced in lipid vesicles by exposure to endophilin. The vesicles convert rapidly to coated tubules whose morphology reflects the local concentration of endophilin. Their diameters and curvature resemble those of synaptic vesicles in...
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PMID: 20484046
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We show that in M. gryphiswaldense MamK is not absolutely required for chain formation. Straight chains, albeit shorter, fragmented and ectopic, were still formed in a mamK deletion mutant, although magnetosome filaments were absent as shown by cryo-electron tomography. Loss of MamK also resulted in...
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PMID: 20487281
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We identify DipM, a putative LytM endopeptidase in Caulobacter crescentus, and show that it plays a critical role in maintaining cell envelope architecture during growth and division. DipM localized to the division site in an FtsZ-dependent manner via its PG-binding LysM domains. Although not essent...
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PMID: 20497504
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We identify DipM, a putative LytM endopeptidase in Caulobacter crescentus, and show that it plays a critical role in maintaining cell envelope architecture during growth and division. DipM localized to the division site in an FtsZ-dependent manner via its PG-binding LysM domains. Although not essent...
|
PMID: 20497504
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We show that in M. gryphiswaldense MamK is not absolutely required for chain formation. Straight chains, albeit shorter, fragmented and ectopic, were still formed in a mamK deletion mutant, although magnetosome filaments were absent as shown by cryo-electron tomography. Loss of MamK also resulted in...
|
PMID: 20487281
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We identify DipM, a putative LytM endopeptidase in Caulobacter crescentus, and show that it plays a critical role in maintaining cell envelope architecture during growth and division. DipM localized to the division site in an FtsZ-dependent manner via its PG-binding LysM domains. Although not essent...
|
PMID: 20497504
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We show that in M. gryphiswaldense MamK is not absolutely required for chain formation. Straight chains, albeit shorter, fragmented and ectopic, were still formed in a mamK deletion mutant, although magnetosome filaments were absent as shown by cryo-electron tomography. Loss of MamK also resulted in...
|
PMID: 20487281
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We identify DipM, a putative LytM endopeptidase in Caulobacter crescentus, and show that it plays a critical role in maintaining cell envelope architecture during growth and division. DipM localized to the division site in an FtsZ-dependent manner via its PG-binding LysM domains. Although not essent...
|
PMID: 20497504
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We show that in M. gryphiswaldense MamK is not absolutely required for chain formation. Straight chains, albeit shorter, fragmented and ectopic, were still formed in a mamK deletion mutant, although magnetosome filaments were absent as shown by cryo-electron tomography. Loss of MamK also resulted in...
|
PMID: 20487281
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We identify DipM, a putative LytM endopeptidase in Caulobacter crescentus, and show that it plays a critical role in maintaining cell envelope architecture during growth and division. DipM localized to the division site in an FtsZ-dependent manner via its PG-binding LysM domains. Although not essent...
|
PMID: 20497504
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We show that in M. gryphiswaldense MamK is not absolutely required for chain formation. Straight chains, albeit shorter, fragmented and ectopic, were still formed in a mamK deletion mutant, although magnetosome filaments were absent as shown by cryo-electron tomography. Loss of MamK also resulted in...
|
PMID: 20487281
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We identify DipM, a putative LytM endopeptidase in Caulobacter crescentus, and show that it plays a critical role in maintaining cell envelope architecture during growth and division. DipM localized to the division site in an FtsZ-dependent manner via its PG-binding LysM domains. Although not essent...
|
PMID: 20497504
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We show that in M. gryphiswaldense MamK is not absolutely required for chain formation. Straight chains, albeit shorter, fragmented and ectopic, were still formed in a mamK deletion mutant, although magnetosome filaments were absent as shown by cryo-electron tomography. Loss of MamK also resulted in...
|
PMID: 20487281
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We identify DipM, a putative LytM endopeptidase in Caulobacter crescentus, and show that it plays a critical role in maintaining cell envelope architecture during growth and division. DipM localized to the division site in an FtsZ-dependent manner via its PG-binding LysM domains. Although not essent...
|
PMID: 20497504
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We show that in M. gryphiswaldense MamK is not absolutely required for chain formation. Straight chains, albeit shorter, fragmented and ectopic, were still formed in a mamK deletion mutant, although magnetosome filaments were absent as shown by cryo-electron tomography. Loss of MamK also resulted in...
|
PMID: 20487281
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We identify DipM, a putative LytM endopeptidase in Caulobacter crescentus, and show that it plays a critical role in maintaining cell envelope architecture during growth and division. DipM localized to the division site in an FtsZ-dependent manner via its PG-binding LysM domains. Although not essent...
|
PMID: 20497504
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We identify DipM, a putative LytM endopeptidase in Caulobacter crescentus, and show that it plays a critical role in maintaining cell envelope architecture during growth and division. DipM localized to the division site in an FtsZ-dependent manner via its PG-binding LysM domains. Although not essent...
|
PMID: 20497504
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We identify DipM, a putative LytM endopeptidase in Caulobacter crescentus, and show that it plays a critical role in maintaining cell envelope architecture during growth and division. DipM localized to the division site in an FtsZ-dependent manner via its PG-binding LysM domains. Although not essent...
|
PMID: 20497504
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We show that in M. gryphiswaldense MamK is not absolutely required for chain formation. Straight chains, albeit shorter, fragmented and ectopic, were still formed in a mamK deletion mutant, although magnetosome filaments were absent as shown by cryo-electron tomography. Loss of MamK also resulted in...
|
PMID: 20487281
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We show that in M. gryphiswaldense MamK is not absolutely required for chain formation. Straight chains, albeit shorter, fragmented and ectopic, were still formed in a mamK deletion mutant, although magnetosome filaments were absent as shown by cryo-electron tomography. Loss of MamK also resulted in...
|
PMID: 20487281
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We show that in M. gryphiswaldense MamK is not absolutely required for chain formation. Straight chains, albeit shorter, fragmented and ectopic, were still formed in a mamK deletion mutant, although magnetosome filaments were absent as shown by cryo-electron tomography. Loss of MamK also resulted in...
|
PMID: 20487281
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We identify DipM, a putative LytM endopeptidase in Caulobacter crescentus, and show that it plays a critical role in maintaining cell envelope architecture during growth and division. DipM localized to the division site in an FtsZ-dependent manner via its PG-binding LysM domains. Although not essent...
|
PMID: 20497504
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We show that in M. gryphiswaldense MamK is not absolutely required for chain formation. Straight chains, albeit shorter, fragmented and ectopic, were still formed in a mamK deletion mutant, although magnetosome filaments were absent as shown by cryo-electron tomography. Loss of MamK also resulted in...
|
PMID: 20487281
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We identify DipM, a putative LytM endopeptidase in Caulobacter crescentus, and show that it plays a critical role in maintaining cell envelope architecture during growth and division. DipM localized to the division site in an FtsZ-dependent manner via its PG-binding LysM domains. Although not essent...
|
PMID: 20497504
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We show that in M. gryphiswaldense MamK is not absolutely required for chain formation. Straight chains, albeit shorter, fragmented and ectopic, were still formed in a mamK deletion mutant, although magnetosome filaments were absent as shown by cryo-electron tomography. Loss of MamK also resulted in...
|
PMID: 20487281
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We identify DipM, a putative LytM endopeptidase in Caulobacter crescentus, and show that it plays a critical role in maintaining cell envelope architecture during growth and division. DipM localized to the division site in an FtsZ-dependent manner via its PG-binding LysM domains. Although not essent...
|
PMID: 20497504
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We show that in M. gryphiswaldense MamK is not absolutely required for chain formation. Straight chains, albeit shorter, fragmented and ectopic, were still formed in a mamK deletion mutant, although magnetosome filaments were absent as shown by cryo-electron tomography. Loss of MamK also resulted in...
|
PMID: 20487281
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We identify DipM, a putative LytM endopeptidase in Caulobacter crescentus, and show that it plays a critical role in maintaining cell envelope architecture during growth and division. DipM localized to the division site in an FtsZ-dependent manner via its PG-binding LysM domains. Although not essent...
|
PMID: 20497504
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We show that in M. gryphiswaldense MamK is not absolutely required for chain formation. Straight chains, albeit shorter, fragmented and ectopic, were still formed in a mamK deletion mutant, although magnetosome filaments were absent as shown by cryo-electron tomography. Loss of MamK also resulted in...
|
PMID: 20487281
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We identify DipM, a putative LytM endopeptidase in Caulobacter crescentus, and show that it plays a critical role in maintaining cell envelope architecture during growth and division. DipM localized to the division site in an FtsZ-dependent manner via its PG-binding LysM domains. Although not essent...
|
PMID: 20497504
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We show that in M. gryphiswaldense MamK is not absolutely required for chain formation. Straight chains, albeit shorter, fragmented and ectopic, were still formed in a mamK deletion mutant, although magnetosome filaments were absent as shown by cryo-electron tomography. Loss of MamK also resulted in...
|
PMID: 20487281
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We identify DipM, a putative LytM endopeptidase in Caulobacter crescentus, and show that it plays a critical role in maintaining cell envelope architecture during growth and division. DipM localized to the division site in an FtsZ-dependent manner via its PG-binding LysM domains. Although not essent...
|
PMID: 20497504
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We show that in M. gryphiswaldense MamK is not absolutely required for chain formation. Straight chains, albeit shorter, fragmented and ectopic, were still formed in a mamK deletion mutant, although magnetosome filaments were absent as shown by cryo-electron tomography. Loss of MamK also resulted in...
|
PMID: 20487281
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We identify DipM, a putative LytM endopeptidase in Caulobacter crescentus, and show that it plays a critical role in maintaining cell envelope architecture during growth and division. DipM localized to the division site in an FtsZ-dependent manner via its PG-binding LysM domains. Although not essent...
|
PMID: 20497504
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We identify DipM, a putative LytM endopeptidase in Caulobacter crescentus, and show that it plays a critical role in maintaining cell envelope architecture during growth and division. DipM localized to the division site in an FtsZ-dependent manner via its PG-binding LysM domains. Although not essent...
|
PMID: 20497504
PDF is available here.
PDF is available here.
Molecular Microbiology (77)1 2010
Abstract
We identify DipM, a putative LytM endopeptidase in Caulobacter crescentus, and show that it plays a critical role in maintaining cell envelope architecture during growth and division. DipM localized to the division site in an FtsZ-dependent manner via its PG-binding LysM domains. Although not essent...
|
PMID: 20497504
PDF is available here.
PDF is available here.