41 |
Photon-Echo-Spektroskopie zur Dynamik der Solvatation in Wasser und an Lipidmembran-Wasser-Grenzschichten / Photon-echo spectroscopy in water and at lipidmembrane-water-interfaces: a solvation dynamic studyBürsing, Helge 24 April 2002 (has links)
No description available.
|
42 |
Permeability improvement of Norway spruce wood with the white rot fungus Physisporinus vitreus / Verbesserung der Permeabilität von Fichtenholz mit dem Weißfäulepilz Physisporinus vitreusLehringer, Christian 28 January 2011 (has links)
No description available.
|
43 |
Myelin Membrane Growth and Organization in a Cellular Model System (EN) / Wachstum und Organisation von Myelinmembranen im zellulären Modellsystem (DE)Yurlova, Larisa 16 July 2010 (has links)
No description available.
|
44 |
Regulation of recycling endosomal membrane traffic by a γ-BAR/ kinesin KIF5 complex / Regulation des recycling endosomalen Membrantransports durch einen Komplex aus γ-BAR und Kinesin KIF5Schmidt, Michael 22 November 2007 (has links)
No description available.
|
45 |
Mechanisms of Neuroligin Function in Inhibitory Postsynaptic Differentiation / Mechanismen der Neuroligin- Funktion in inhibitorischer postsynaptischer DifferenzierungPoulopoulos, Alexandros 28 April 2008 (has links)
No description available.
|
46 |
Probing modes of vesicle docking in neurosecretory cells with evanescent wave microscopy / Untersuchung zur Vesikel-Andockmodi in neurosecretorischen Zellen mit TotalreflektionsmikroskopieKochubey, Olexiy 18 January 2006 (has links)
No description available.
|
47 |
Der Zellwandbau von Nadelholztracheiden: Die submikroskopische Struktur des Holzes vor dem Hintergrund holztechnologischer FragestellungenRosenthal, Michael, Bäucker, Ernst January 2012 (has links)
Die Anatomie des Holzes stellt eine entscheidende Einflussgröße bei einer Vielzahl holztechnologischer Prozesse dar. Der folgende Beitrag behandelt den Bau der verholzten Zellwand am Beispiel der Tracheiden des Nadelholzes.
|
48 |
Microcompartmentation of cell wall integrity sensors in Saccharomyces cerevisiae / Mikrokompartimentierung von Zellwandintegritätssensoren in Saccharomyces cerevisiaeKock, Christian 05 August 2016 (has links)
The ability to adapt to changing environments is a key feature of living cells which is usually mediated by signal transduction pathways. One of these pathways in Saccharomyces cerevisiae maintains the proper cell wall composition under cell wall remodeling and stress conditions which ensures cell shape and integrity. The pathway is hence commonly referred to as cell wall integrity (CWI) pathway. Five plasma membrane sensors detect surface stress and activate a conserved MAPK cascade through Rom2, Rho1 and Pkc1. Downstream of the cascade, Slt2 activates the transcription factors Rlm1 and SBF. These regulate the expression of genes which are involved in cell wall synthesis and cell cycle control, respectively. The sensors can be grouped into two protein families with Wsc1, Wsc2 and Wsc3 on the one hand and Mid2 and Mtl1 on the other hand. They all contain a highly mannosylated extracellular serine/threonine-rich region (STR), a single transmembrane domain and a cytoplasmic tail. Whereas Wsc-family sensors carry an additional cysteine-rich domain (CRD) headgroup, Mid2 and Mtl1 are N-glycosylated at an asparagine (Kock et al., 2015).
A strain deleted in all five sensor genes is not viable and WSC1, WSC2 and MID2 are the main sensor genes to mediate the stress response. Wsc1 and Mid2 show non-overlapping spot-like and network-like localization patterns in the plasma membrane, respectively, whose formation is not governed by their transmembrane domains. Colocalization studies with marker proteins of the known yeast plasma membrane domains “membrane compartment occupied by Can1” (MCC), “membrane compartment occupied by Pma1” (MCP) and the “membrane compartment of the TOR2 complex” (MCT) revealed that Wsc1 forms a distinct plasma membrane domain which is here introduced as “membrane compartment occupied by Wsc1“ (MCW). This microcompartment depends on the cysteine-rich domain (CRD) as sensors mutated in this headgroup accumulate in the vacuole. Blocking endocytosis either by an end3 deletion or by mutation of the NPFDD endocytosis signal in the cytoplasmic tail of Wsc1 restores its signaling function but displays an altered pattern of membrane distribution, changing from spot-like in wild-type to network-like in the mutants. This indicated that clustering may protect the sensor from endocytosis. In addition, Wsc1 has amyloid-like properties suggesting a role in clustering. Accordingly, protein aggregation (clustering) is lost in a mutant of a predicted amyloid motif within the CRD, which also impairs Wsc1 signaling.
|
49 |
Solvatationsdynamik an biologischen Grenzschichten / Solvation dynamics at biological interfacesSeidel, Marco Thomas 05 November 2003 (has links)
No description available.
|
Page generated in 0.0326 seconds