scholarly journals Size-dependent protein segregation at membrane interfaces

2016 ◽  
Vol 12 (7) ◽  
pp. 704-711 ◽  
Author(s):  
Eva M. Schmid ◽  
Matthew H. Bakalar ◽  
Kaushik Choudhuri ◽  
Julian Weichsel ◽  
Hyoung Sook Ann ◽  
...  
Keyword(s):  
Size Dependent ◽  
Membrane Interfaces ◽  
Dependent Protein

scholarly journals Microscopic Investigation of Reversible Nanoscale Surface Size Dependent Protein Conjugation

2009 ◽  
Vol 10 (5) ◽  
pp. 2348-2366 ◽  
Author(s):  
Kazushige Yokoyama ◽  
Hyunah Cho ◽  
Sean Cullen ◽  
Matthew Kowalik ◽  
Nicole Briglio ◽  
...  
Keyword(s):  
Microscopic Investigation ◽  
Protein Conjugation ◽  
Size Dependent ◽  
Dependent Protein

scholarly journals Mechanisms for Size-Dependent Protein Segregation at Immune Synapses Assessed with Molecular Rulers

2011 ◽  
Vol 100 (12) ◽  
pp. 2865-2874 ◽  
Author(s):  
Juha-Matti Alakoskela ◽  
Apurba L. Koner ◽  
Dominika Rudnicka ◽  
Karsten Köhler ◽  
Mark Howarth ◽  
...  
Keyword(s):  
Size Dependent ◽  
Molecular Rulers ◽  
Immune Synapses ◽  
Dependent Protein

Crystal Plane- and Size-Dependent Protein Adsorption on Nanozeolite

2009 ◽  
Vol 113 (42) ◽  
pp. 18040-18046 ◽  
Author(s):  
Yuan-Yuan Hu ◽  
Ya-Hong Zhang ◽  
Nan Ren ◽  
Yi Tang
Keyword(s):  
Protein Adsorption ◽  
Crystal Plane ◽  
Size Dependent ◽  
Dependent Protein

scholarly journals Size-dependent protein segregation creates a spatial switch for Notch and APP signaling

2020 ◽  
Author(s):  
Minsuk Kwak ◽  
Kaden M. Southard ◽  
Nam Hyeong Kim ◽  
Ramu Gopalappa ◽  
Woon Ryoung Kim ◽  
...  
Keyword(s):  
Cell Surface ◽  
Amyloid Precursor Proteins ◽  
High Cell ◽  
Downstream Signaling ◽  
Size Dependent ◽  
Enzyme Substrate ◽  
Secretase Activity ◽  
Precursor Proteins ◽  
Dependent Protein ◽  
Dependent Mechanism

Aberrant cleavage of Notch and amyloid precursor proteins (APPs) by γ-secretase is implicated in numerous diseases, but how cleavage is regulated in space and time is unclear. Here, we report that cadherin-based adherens junctions (cadAJs) are sites of high cell-surface γ-secretase activity, while simultaneously excluding these γ-secretase substrates by a size-dependent mechanism, prohibiting enzyme-substrate interactions. Upon activation, Notch and APP undergo drastic spatial rearrangements to cadAJs, concentrating them with γ-secretase, wherein they are further processed for downstream signaling. Spatial mutation by decreasing (or increasing) the size of Notch extracellular domain promotes (or inhibits) signaling, respectively. Dysregulation of this spatial switch also promotes formation of more amyloidogenic Aβ. Therefore, cadAJs creates distinct biochemical compartments regulating signaling events involving γ-secretase and prevent pathogenic activation of its substrates.

scholarly journals A Method for Investigation of Size-Dependent Protein Binding to Nanoholes Using Intrinsic Fluorescence of Proteins

ACS Omega ◽  
2017 ◽  
Vol 2 (8) ◽  
pp. 4772-4778 ◽  
Author(s):  
Bita Malekian ◽  
Ivan Maximov ◽  
Rainer Timm ◽  
Tommy Cedervall ◽  
Dan Hessman
Keyword(s):  
Protein Binding ◽  
Intrinsic Fluorescence ◽  
Size Dependent ◽  
Dependent Protein

Production and STEM examination of controlled-size silver clusters

1983 ◽  
Vol 41 ◽  
pp. 338-339
Author(s):  
M. A. Listvan ◽  
R. P. Andres
Keyword(s):  
Cluster Size ◽  
Metal Clusters ◽  
Experimental Parameter ◽  
Carbon Films ◽  
Metal Species ◽  
Silver Clusters ◽  
Free Jet ◽  
Size Dependent ◽  
Cluster Properties ◽  
Controllable Size

Knowledge of the function and structure of small metal clusters is one goal of research in catalysis. One important experimental parameter is cluster size. Ideally, one would like to produce metal clusters of regulated size in order to characterize size-dependent cluster properties.A source has been developed which is capable of producing microscopic metal clusters of controllable size (in the range 5-500 atoms) This source, the Multiple Expansion Cluster Source, with a Free Jet Deceleration Filter (MECS/FJDF) operates as follows. The bulk metal is heated in an oven to give controlled concentrations of monomer and dimer which were expanded sonically. These metal species were quenched and condensed in He and filtered to produce areosol particles of a controlled size as verified by mass spectrometer measurements. The clusters were caught on pre-mounted, clean carbon films. The grids were then transferred in air for microscopic examination. MECS/FJDF was used to produce two different sizes of silver clusters for this study: nominally Ag6 and Ag50.

Transfer Technique for Electron Microscopy of Membrance Filter Samples

1974 ◽  
Vol 32 ◽  
pp. 554-555
Author(s):  
Lawrence W. Ortiz ◽  
Bonnie L. Isom
Keyword(s):  
Electron Microscopy ◽  
Electron Microscope ◽  
Pore Size ◽  
Membrane Filters ◽  
Size Dependent

A procedure is described for the quantitative transfer of fibers and particulates collected on membrane filters to electron microscope (EM) grids. Various Millipore MF filters (Millipore AA, HA, GS, and VM; 0.8, 0.45, 0.22 and 0.05 μm mean pore size) have been used with success. Observed particle losses have not been size dependent and have not exceeded 10%. With fibers (glass or asbestos) as the collected media this observed loss is approximately 3%.

Spindle scaling mechanisms

2020 ◽  
Vol 64 (2) ◽  
pp. 383-396
Author(s):  
Lara K. Krüger ◽  
Phong T. Tran
Keyword(s):  
Cell Size ◽  
Spindle Assembly ◽  
Dependent Manner ◽  
Post Translational Modification ◽  
Size Dependent ◽  
A Cell ◽  
Chromosome Separation ◽  
Spindle Elongation ◽  
Protein Gradients ◽  
Spindle Structure

Abstract The mitotic spindle robustly scales with cell size in a plethora of different organisms. During development and throughout evolution, the spindle adjusts to cell size in metazoans and yeast in order to ensure faithful chromosome separation. Spindle adjustment to cell size occurs by the scaling of spindle length, spindle shape and the velocity of spindle assembly and elongation. Different mechanisms, depending on spindle structure and organism, account for these scaling relationships. The limited availability of critical spindle components, protein gradients, sequestration of spindle components, or post-translational modification and differential expression levels have been implicated in the regulation of spindle length and the spindle assembly/elongation velocity in a cell size-dependent manner. In this review, we will discuss the phenomenon and mechanisms of spindle length, spindle shape and spindle elongation velocity scaling with cell size.

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