Results 41 to 50 of about 158,042 (243)

Crystal Structure of the Herpesvirus Nuclear Egress Complex Provides Insights into Inner Nuclear Membrane Remodeling

Cell Reports, 2015
Although nucleo-cytoplasmic transport is typically mediated through nuclear pore complexes, herpesvirus capsids exit the nucleus via a unique vesicular pathway.
Tzviya Zeev-Ben-Mordehai, Marion Weberruß, Michael Lorenz, Juliana Cheleski, Teresa Hellberg, Cathy Whittle, Kamel El Omari, Daven Vasishtan, Kyle C. Dent, Karl Harlos, Kati Franzke, Christoph Hagen, Barbara G. Klupp, Wolfram Antonin, Thomas C. Mettenleiter, Kay Grünewald   +15 more
doaj   +1 more source

Methodologies to monitor protein turnover at the inner nuclear membrane. [PDF]

Methods Enzymol, 2019
Lamin B receptor (LBR) is an inner nuclear membrane protein that associates with the nuclear lamina and harbors sterol reductase activity essential for cholesterol biosynthesis. Several LBR mutations implicated in human congenital disorders give rise to C-terminal truncations which render LBR metabolically unstable, resulting in their rapid turnover in
Tsai PL, Zhao C, Schlieker C.
europepmc   +4 more sources

Secret passage to the inner nuclear membrane [PDF]

Journal of Cell Biology, 2010
Proteins enter the inner nuclear membrane through a side door in the nuclear pore complex, [Theerthagiri et al.][1] report. ![Figure][2] A swollen nucleus lacking Nup188 and Nup93 (left) dwarfs a normal nucleus (right).
openaire   +1 more source

Organizing the interface—Plasma membrane architecture and receptor dynamics in virus‐cell interactions

FEBS Letters, EarlyView.
Plasma membranes contain dynamic nanoscale domains that organize lipids and receptors. Because viruses operate at similar scales, this architecture shapes early infection steps, including attachment, receptor engagement, and entry. Using influenza A virus and HIV‐1 as examples, we highlight how receptor nanoclusters, multivalent glycan interactions ...
Jan Schlegel, Christian Sieben
wiley   +1 more source

Nucleoplasmic signals promote directed transmembrane protein import simultaneously via multiple channels of nuclear pores

Nature Communications, 2020
The contribution of central and peripheral channels of nuclear pores to transport of transmembrane proteins is unclear. Here the authors show that most inner nuclear membrane proteins use only peripheral channels, but some extend nuclear localization ...
Krishna C. Mudumbi, Rafal Czapiewski, Andrew Ruba, Samuel L. Junod, Yichen Li, Wangxi Luo, Christina Ngo, Valentina Ospina, Eric C. Schirmer, Weidong Yang   +9 more
doaj   +1 more source

Multiple routes to the inner nuclear membrane [PDF]

Journal of Cell Biology, 2011
![Figure][1] Gold particles mark the location of the INM protein NET39 in the ONM (downward arrowhead) and in the INM (upward arrowhead). At least four mechanisms can usher inner nuclear membrane (INM) proteins to their proper location, [Zuleger et al.][2] show.
openaire   +1 more source

Cell geometry and membrane protein crowding constrain Escherichia coli growth rate, overflow metabolism, respiration, and maintenance energy

FEBS Letters, EarlyView.
The physical dimensions and shape of bacterial cells define the surface area available to acquire nutrients and the volume available for synthesizing proteins and DNA. Here, we use computational systems biology to decode the importance of cell geometry as a major determinant of prokaryotic phenotype, including growth rate and metabolic efficiency. This
Ross P. Carlson, Tomáš Gedeon, Mauricio Garcia Benitez, Campbell Putnam, William R. Harcombe, Radhakrishnan Mahadevan, Ashley E. Beck   +6 more
wiley   +1 more source

Evidence for the existence of Dm0-like Lamin in Sf9 cells

浙江大学学报. 农业与生命科学版, 2015
The nuclear membrane of mammalian cells was composed of inner nuclear membrane, outer nuclear membrane and perinuclear space. The lamina was localized under the nucleoplasm face of inner nuclear membrane. It has been known that the lamina was distributed
Wei Wenqiang, Ji Shaoping, Zhang Yinyan
doaj   +1 more source

Targeting the inner nuclear membrane

The Journal of Cell Biology, 2004
![][1] A reporter (green) gets trapped (bottom) in the nucleus by binding its partner (red). Proteins destined for the inner nuclear membrane (INM) start out in the peripheral ER.
openaire   +2 more sources

Microbiome−host proteostasis crosstalk—An emerging perspective on mechanisms and interventions toward healthy longevity

FEBS Letters, EarlyView.
Proteostasis and the gut microbiota play a key role in shaping host physiology. Microbiota‐derived metabolites, vitamins, and RNA modulate host proteostasis. Findings from model systems, including C. elegans, indicate microbes can either stabilize or disrupt host proteostasis.
Abhishek Anil Dubey, Maria Ermolaeva
wiley   +1 more source