ALBERT

All Library Books, journals and Electronic Records Telegrafenberg

feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 1
    Publication Date: 2008-12-17
    Description: Contact inhibition of locomotion was discovered by Abercrombie more than 50 years ago and describes the behaviour of fibroblast cells confronting each other in vitro, where they retract their protrusions and change direction on contact. Its failure was suggested to contribute to malignant invasion. However, the molecular basis of contact inhibition of locomotion and whether it also occurs in vivo are still unknown. Here we show that neural crest cells, a highly migratory and multipotent embryonic cell population, whose behaviour has been likened to malignant invasion, demonstrate contact inhibition of locomotion both in vivo and in vitro, and that this accounts for their directional migration. When two migrating neural crest cells meet, they stop, collapse their protrusions and change direction. In contrast, when a neural crest cell meets another cell type, it fails to display contact inhibition of locomotion; instead, it invades the other tissue, in the same manner as metastatic cancer cells. We show that inhibition of non-canonical Wnt signalling abolishes both contact inhibition of locomotion and the directionality of neural crest migration. Wnt-signalling members localize at the site of cell contact, leading to activation of RhoA in this region. These results provide the first example of contact inhibition of locomotion in vivo, provide an explanation for coherent directional migration of groups of cells and establish a previously unknown role for non-canonical Wnt signalling.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2635562/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2635562/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Carmona-Fontaine, Carlos -- Matthews, Helen K -- Kuriyama, Sei -- Moreno, Mauricio -- Dunn, Graham A -- Parsons, Maddy -- Stern, Claudio D -- Mayor, Roberto -- BB/D017521/1/Biotechnology and Biological Sciences Research Council/United Kingdom -- G0100152/Medical Research Council/United Kingdom -- G0100152(56891)/Medical Research Council/United Kingdom -- G0400559/Medical Research Council/United Kingdom -- G0401026/Medical Research Council/United Kingdom -- G0801145/Medical Research Council/United Kingdom -- G117/506/Medical Research Council/United Kingdom -- G117/506(63530)/Medical Research Council/United Kingdom -- England -- Nature. 2008 Dec 18;456(7224):957-61. doi: 10.1038/nature07441. Epub 2008 Dec 10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Anatomy and Developmental Biology, University College London, London WC1E 6BT, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19078960" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Communication ; *Cell Movement ; Cell Polarity ; *Contact Inhibition ; Embryo, Nonmammalian/cytology ; Neural Crest/*cytology ; Signal Transduction ; Wnt Proteins/metabolism ; Xenopus/embryology ; Zebrafish/embryology ; rhoA GTP-Binding Protein/metabolism
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 2
    Publication Date: 2013-10-25
    Description: Protein biosynthesis depends on the availability of ribosomes, which in turn relies on ribosomal RNA production. In eukaryotes, this process is carried out by RNA polymerase I (Pol I), a 14-subunit enzyme, the activity of which is a major determinant of cell growth. Here we present the crystal structure of Pol I from Saccharomyces cerevisiae at 3.0 A resolution. The Pol I structure shows a compact core with a wide DNA-binding cleft and a tightly anchored stalk. An extended loop mimics the DNA backbone in the cleft and may be involved in regulating Pol I transcription. Subunit A12.2 extends from the A190 jaw to the active site and inserts a transcription elongation factor TFIIS-like zinc ribbon into the nucleotide triphosphate entry pore, providing insight into the role of A12.2 in RNA cleavage and Pol I insensitivity to alpha-amanitin. The A49-A34.5 heterodimer embraces subunit A135 through extended arms, thereby contacting and potentially regulating subunit A12.2.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fernandez-Tornero, Carlos -- Moreno-Morcillo, Maria -- Rashid, Umar J -- Taylor, Nicholas M I -- Ruiz, Federico M -- Gruene, Tim -- Legrand, Pierre -- Steuerwald, Ulrich -- Muller, Christoph W -- England -- Nature. 2013 Oct 31;502(7473):644-9. doi: 10.1038/nature12636. Epub 2013 Oct 23.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉1] Centro de Investigaciones Biologicas, Consejo Superior de Investigaciones Cientificas, Ramiro de Maeztu 9, 28040 Madrid, Spain [2].〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/24153184" target="_blank"〉PubMed〈/a〉
    Keywords: Catalytic Domain ; Crystallography, X-Ray ; DNA/chemistry/metabolism ; Models, Molecular ; Peptide Chain Elongation, Translational ; Protein Binding ; Protein Conformation ; Protein Multimerization ; Protein Subunits/*chemistry ; RNA Polymerase I/*chemistry ; RNA Polymerase II/chemistry ; RNA Polymerase III/chemistry ; Saccharomyces cerevisiae/*enzymology ; Transcription, Genetic
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 3
    Publication Date: 2010-09-11
    Description: The magnitude-8.8 Maule (Chile) earthquake of 27 February 2010 ruptured a segment of the Andean subduction zone megathrust that has been suspected to be of high seismic potential. It is the largest earthquake to rupture a mature seismic gap in a subduction zone that has been monitored with a dense space-geodetic network before the event. This provides an image of the pre-seismically locked state of the plate interface of unprecedentedly high resolution, allowing for an assessment of the spatial correlation of interseismic locking with coseismic slip. Pre-seismic locking might be used to anticipate future ruptures in many seismic gaps, given the fundamental assumption that locking and slip are similar. This hypothesis, however, could not be tested without the occurrence of the first gap-filling earthquake. Here we show evidence that the 2010 Maule earthquake slip distribution correlates closely with the patchwork of interseismic locking distribution as derived by inversion of global positioning system (GPS) observations during the previous decade. The earthquake nucleated in a region of high locking gradient and released most of the stresses accumulated in the area since the last major event in 1835. Two regions of high seismic slip (asperities) appeared to be nearly fully locked before the earthquake. Between these asperities, the rupture bridged a zone that was creeping interseismically with consistently low coseismic slip. The rupture stopped in areas that were highly locked before the earthquake but where pre-stress had been significantly reduced by overlapping twentieth-century earthquakes. Our work suggests that coseismic slip heterogeneity at the scale of single asperities should indicate the seismic potential of future great earthquakes, which thus might be anticipated by geodetic observations.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Moreno, Marcos -- Rosenau, Matthias -- Oncken, Onno -- England -- Nature. 2010 Sep 9;467(7312):198-202. doi: 10.1038/nature09349.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Helmholtz Centre Potsdam, GFZ German Research Centre for Geosciences, Telegrafenberg, Potsdam 14473, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20829792" target="_blank"〉PubMed〈/a〉
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 4
    Publication Date: 2014-08-15
    Description: On 1 April 2014, Northern Chile was struck by a magnitude 8.1 earthquake following a protracted series of foreshocks. The Integrated Plate Boundary Observatory Chile monitored the entire sequence of events, providing unprecedented resolution of the build-up to the main event and its rupture evolution. Here we show that the Iquique earthquake broke a central fraction of the so-called northern Chile seismic gap, the last major segment of the South American plate boundary that had not ruptured in the past century. Since July 2013 three seismic clusters, each lasting a few weeks, hit this part of the plate boundary with earthquakes of increasing peak magnitudes. Starting with the second cluster, geodetic observations show surface displacements that can be associated with slip on the plate interface. These seismic clusters and their slip transients occupied a part of the plate interface that was transitional between a fully locked and a creeping portion. Leading up to this earthquake, the b value of the foreshocks gradually decreased during the years before the earthquake, reversing its trend a few days before the Iquique earthquake. The mainshock finally nucleated at the northern end of the foreshock area, which skirted a locked patch, and ruptured mainly downdip towards higher locking. Peak slip was attained immediately downdip of the foreshock region and at the margin of the locked patch. We conclude that gradual weakening of the central part of the seismic gap accentuated by the foreshock activity in a zone of intermediate seismic coupling was instrumental in causing final failure, distinguishing the Iquique earthquake from most great earthquakes. Finally, only one-third of the gap was broken and the remaining locked segments now pose a significant, increased seismic hazard with the potential to host an earthquake with a magnitude of 〉8.5.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schurr, Bernd -- Asch, Gunter -- Hainzl, Sebastian -- Bedford, Jonathan -- Hoechner, Andreas -- Palo, Mauro -- Wang, Rongjiang -- Moreno, Marcos -- Bartsch, Mitja -- Zhang, Yong -- Oncken, Onno -- Tilmann, Frederik -- Dahm, Torsten -- Victor, Pia -- Barrientos, Sergio -- Vilotte, Jean-Pierre -- England -- Nature. 2014 Aug 21;512(7514):299-302. doi: 10.1038/nature13681. Epub 2014 Aug 13.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉GFZ Helmholtz Centre Potsdam, German Research Centre for Geosciences, Telegrafenberg, 14473 Potsdam, Germany. ; School of Earth and Space Sciences, Peking University, Beijing 100871, China. ; Centro Sismologico National, Universidad de Chile, Facultad de Ciencias Fisicas y Matematicas, Blanco Encalada 2002, Santiago, Chile. ; Institut de Physique du Globe de Paris, 1, rue Jussieu, 75238 Paris cedex 05, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/25119049" target="_blank"〉PubMed〈/a〉
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 5
    Publication Date: 2015-11-26
    Description: Transcription of genes encoding small structured RNAs such as transfer RNAs, spliceosomal U6 small nuclear RNA and ribosomal 5S RNA is carried out by RNA polymerase III (Pol III), the largest yet structurally least characterized eukaryotic RNA polymerase. Here we present the cryo-electron microscopy structures of the Saccharomyces cerevisiae Pol III elongating complex at 3.9 A resolution and the apo Pol III enzyme in two different conformations at 4.6 and 4.7 A resolution, respectively, which allow the building of a 17-subunit atomic model of Pol III. The reconstructions reveal the precise orientation of the C82-C34-C31 heterotrimer in close proximity to the stalk. The C53-C37 heterodimer positions residues involved in transcription termination close to the non-template DNA strand. In the apo Pol III structures, the stalk adopts different orientations coupled with closed and open conformations of the clamp. Our results provide novel insights into Pol III-specific transcription and the adaptation of Pol III towards its small transcriptional targets.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4681132/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4681132/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hoffmann, Niklas A -- Jakobi, Arjen J -- Moreno-Morcillo, Maria -- Glatt, Sebastian -- Kosinski, Jan -- Hagen, Wim J H -- Sachse, Carsten -- Muller, Christoph W -- England -- Nature. 2015 Dec 10;528(7581):231-6. doi: 10.1038/nature16143. Epub 2015 Nov 25.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉European Molecular Biology Laboratory (EMBL), Structural and Computational Biology Unit, Meyerhofstrasse 1, 69117 Heidelberg, Germany. ; European Molecular Biology Laboratory (EMBL), Hamburg Unit, Notkestrasse 85, 22607 Hamburg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/26605533" target="_blank"〉PubMed〈/a〉
    Keywords: Cryoelectron Microscopy ; *Models, Molecular ; Protein Binding ; Protein Structure, Tertiary ; RNA Polymerase III/*chemistry ; Saccharomyces cerevisiae/*enzymology ; Saccharomyces cerevisiae Proteins/*chemistry
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...