Results 31 to 40 of about 590,456 (352)

Rapid degradation of mutant SLC25A46 by the ubiquitin-proteasome system results in MFN1/2-mediated hyperfusion of mitochondria. [PDF]

, 2017
SCL25A46 is a mitochondrial carrier protein that surprisingly localizes to the outer membrane and is distantly related to Ugo1. Here we show that a subset of SLC25A46 interacts with mitochondrial dynamics components and the MICOS complex.
Claypool, Steven M, Jen, Joanna C, Koehler, Carla M, Steffen, Janos, Vashisht, Ajay A, Wan, Jijun, Wohlschlegel, James A   +6 more
core   +1 more source

Outer membrane proteins of Pseudomonas [PDF]

Molecular Microbiology, 1990
SummaryIn this review, we describe the outer membrane proteins of Pseudomonas aeruginosa and related strains from the Pseudomonas fluorescens rRNA homology group of the Pseudomonadaceae, with emphasis on the physiological function and biochemical characteristics of these proteins.
R E, Hancock, R, Siehnel, N, Martin
openaire   +2 more sources

Structural bioinformatics studies of bacterial outer membrane beta-barrel transporters and their AlphaFold2 predicted water-soluble QTY variants.

PLoS ONE, 2023
Beta-barrel outer membrane proteins (OMP) are integral components of Gram-negative bacteria, eukaryotic mitochondria, and chloroplasts. They play essential roles in various cellular processes including nutrient transport, membrane stability, host ...
Akash Sajeev-Sheeja, Eva Smorodina, Shuguang Zhang   +2 more
doaj   +1 more source

Biosynthesis of Mitochondrial Porin and Insertion into the Outer Mitochondrial Membrane of Neuruspora crassa [PDF]

, 1982
Mitochondrial porin, the major protein of the outer mitochondrial membrane is synthesized by free cytoplasmic polysomes. The apparent molecular weight of the porin synthesized in homologous or heterologous cell-free systems is the same as that of the ...
Cassady W. E., Colombini M., Conboy J. G., Cote C., Cowlesmith I., Freitag H., Glizin V., Hallermayer R., Hennig B., Korb H., Lewin A., Maccecchini M. L., Maccechini M. L., Matsuura S., Mihara K., Nabi N., Nelson N., Neupert W., Oda T., Palmiter R. D., Payvar F., Raymond Y., Scheele G., Schleyer M., Schmelzer E., Sebald W., Sherton C. C., Shore G. C., Sonderegger P., Teintze M., Ullrich A., Zelman L. S., Zimmermann R., Zimmermann R., Zimmermann R., Zimmermann R.   +35 more
core   +1 more source

Phosphoproteins and protein-kinase activity in isolated envelopes of pea (Pisum sativum L.) chloroplasts [PDF]

, 1985
A protein kinase was found in envelope membranes of purified pea (Pisum sativum L.) chloroplasts. Separation of the two envelope membranes showed that most of the enzyme activity was localized in the outer envelope.
D.G. Robinson, G. Mourioux, G.M. Hathaway, H.Y. Nakatani, J. Joyard, J. Pfisterer, J. Soll, J. Soll, K. Cline, K. Cline, M.A. Block, O.H. Lowry, R. Douce, R. Douce, T.J. Yan, U.J. Flügge, W.A. Laing, Z.F. Lin   +17 more
core   +1 more source

Regulation of Peptidoglycan Synthesis by Outer-Membrane Proteins [PDF]

Cell, 2010
Growth of the mesh-like peptidoglycan (PG) sacculus located between the bacterial inner and outer membranes (OM) is tightly regulated to ensure cellular integrity, maintain cell shape, and orchestrate division. Cytoskeletal elements direct placement and activity of PG synthases from inside the cell, but precise spatiotemporal control over this process ...
Typas, A., Banzhaf, M., van den Berg van Saparoea, B., Verheul, J., Biboy, J., Nichols, R.J., Zietek, M., Beilharz, K., Kannenberg, K., von Rechenberg, M., Breukink, E., den Blaauwen, T., Gross, C.A., Vollmer, W.   +13 more
openaire   +7 more sources

Outer envelope membranes from chloroplasts are isolated as right-side-out vesicles [PDF]

, 1992
Outer envelope membranes were isolated from purified chloroplasts of pea leaves. The sidedness of the vesicles was analyzed by (i) aqueous polymer-two phase partitioning, (ii) the effect of limited proteolysis on the outer-envelope proteins (OEP) 86 and ...
Eichacker, Susanne, Soll, Jürgen, Waegemann, Karin   +2 more
core   +1 more source

HHomp—prediction and classification of outer membrane proteins [PDF]

Nucleic Acids Research, 2009
Outer membrane proteins (OMPs) are the transmembrane proteins found in the outer membranes of Gram-negative bacteria, mitochondria and plastids. Most prediction methods have focused on analogous features, such as alternating hydrophobicity patterns. Here, we start from the observation that almost all beta-barrel OMPs are related by common ancestry.
Michael Remmert, Dirk Linke, Andrei N. Lupas, Johannes Söding   +3 more
openaire   +5 more sources

Building bigger beta-barrels

eLife, 2019
The range of barrel-shaped proteins found in the outer membrane of certain bacteria evolved through multiple pathways.
Vikas Nanda
doaj   +1 more source

BNIP3 and NIX mediate Mieap-induced accumulation of lysosomal proteins within mitochondria. [PDF]

PLoS ONE, 2012
Mieap, a p53-inducible protein, controls mitochondrial quality by repairing unhealthy mitochondria. During repair, Mieap induces the accumulation of intramitochondrial lysosomal proteins (designated MALM for Mieap-induced accumulation of lysosome-like ...
Yasuyuki Nakamura, Noriaki Kitamura, Daisuke Shinogi, Masaki Yoshida, Olga Goda, Ryuya Murai, Hiroki Kamino, Hirofumi Arakawa   +7 more
doaj   +1 more source