Matthias Eibauer
Overview
Explore the profile of Matthias Eibauer including associated specialties, affiliations and a list of published articles.
Author names and details appear as published. Due to indexing inconsistencies, multiple individuals may share a name, and a single author may have variations. MedLuna displays this data as publicly available, without modification or verification
Snapshot
Snapshot
Articles
21
Citations
840
Followers
0
Related Specialties
Related Specialties
Top 10 Co-Authors
Top 10 Co-Authors
Published In
Published In
Affiliations
Affiliations
Soon will be listed here.
Recent Articles
11.
Turgay Y, Eibauer M, Goldman A, Shimi T, Khayat M, Ben-Harush K, et al.
Nature
. 2017 Feb;
543(7644):261-264.
PMID: 28241138
The nuclear lamina is a fundamental constituent of metazoan nuclei. It is composed mainly of lamins, which are intermediate filament proteins that assemble into a filamentous meshwork, bridging the nuclear...
12.
Zwerger M, Eibauer M, Medalia O
Nucleus
. 2016 Feb;
7(1):1-7.
PMID: 26902931
Nuclear pore complexes (NPCs) serve as the gateway of the cell nucleus. These macromolecular assemblies form selective aqueous translocation channels permitting the free diffusion of small molecules, as well as...
13.
Tamir A, Sorrentino S, Motahedeh S, Shai E, Dubrovsky A, Dahan I, et al.
J Struct Biol
. 2016 Jan;
193(3):181-187.
PMID: 26767592
Platelets are essential for hemostasis and wound healing. They are involved in fundamental processes of vascular biology such as angiogenesis, tissue regeneration, and tumor metastasis. Upon activation, platelets shed small...
14.
Eibauer M, Pellanda M, Turgay Y, Dubrovsky A, Wild A, Medalia O
Nat Commun
. 2015 Jun;
6:7532.
PMID: 26112706
Nuclear pore complexes (NPCs) perforate the nuclear envelope and allow the exchange of macromolecules between the nucleus and the cytoplasm. To acquire a deeper understanding of this transport mechanism, we...
15.
Harapin J, Eibauer M, Medalia O
Structure
. 2013 Sep;
21(9):1522-30.
PMID: 24010711
Structural analysis of macromolecular assemblies in their physiological environment is a challenging task that is instrumental in answering fundamental questions in cellular and molecular structural biology. The continuous development of...
16.
Eibauer M, Hoffmann C, Plitzko J, Baumeister W, Nickell S, Engelhardt H
J Struct Biol
. 2012 Sep;
180(3):488-96.
PMID: 23000705
Cryo-electron tomography in combination with subtomogram averaging allows to investigate the structure of protein assemblies in their natural environment in a close to live state. To make full use of...
17.
Pfeffer S, Brandt F, Hrabe T, Lang S, Eibauer M, Zimmermann R, et al.
Structure
. 2012 Jul;
20(9):1508-18.
PMID: 22819217
In eukaryotic cells, cotranslational protein translocation across the endoplasmic reticulum (ER) membrane requires an elaborate macromolecular machinery. While structural details of ribosomes bound to purified and solubilized constituents of the...
18.
Rigort A, Bauerlein F, Villa E, Eibauer M, Laugks T, Baumeister W, et al.
Proc Natl Acad Sci U S A
. 2012 Mar;
109(12):4449-54.
PMID: 22392984
Cryoelectron tomography provides unprecedented insights into the macromolecular and supramolecular organization of cells in a close-to-living state. However because of the limited thickness range (< 0.5-1 μm) that is accessible...
19.
Ortiz J, Brandt F, Matias V, Sennels L, Rappsilber J, Scheres S, et al.
J Cell Biol
. 2010 Aug;
190(4):613-21.
PMID: 20733057
Ribosomes arranged in pairs (100S) have been related with nutritional stress response and are believed to represent a "hibernation state." Several proteins have been identified that are associated with 100S...
20.
Rigort A, Bauerlein F, Leis A, Gruska M, Hoffmann C, Laugks T, et al.
J Struct Biol
. 2010 Feb;
172(2):169-79.
PMID: 20178848
A principal limitation of cryo-transmission electron microscopy performed on cells or tissues is the accessible specimen thickness. This is exacerbated in tomography applications, where the aspect ratio (and thus the...