Results 31 to 40 of about 18,763 (263)

Septin filament organization in Saccharomyces cerevisiae. [PDF]

, 2012
Septins are a family of GTP-binding, membrane-interacting cytoskeletal proteins, highly conserved and essential in all eukaryotes (with the exception of plants). Septins play important roles in a number of cellular events that involve membrane remodeling
Bertin, Aurélie, NOGALES, Eva
core   +1 more source

Diversity of opisthokont septin proteins reveals structural constraints and conserved motifs

BMC Evolutionary Biology, 2019
Background Septins are cytoskeletal proteins important in cell division and in establishing and maintaining cell polarity. Although septins are found in various eukaryotes, septin genes had the richest history of duplication and diversification in the ...
Benjamin Auxier, Jaclyn Dee, Mary L. Berbee, Michelle Momany   +3 more
doaj   +1 more source

A homozygous genome‐edited Sept2‐EGFP fibroblast cell line [PDF]

, 2019
Septins are a conserved, essential family of GTPases that interact with actin, microtubules, and membranes and form scaffolds and diffusion barriers in cells. Several of the 13 known mammalian septins assemble into nonpolar, multimeric complexes that can
Banko, Monika, Ewers, Helge, Heyd, Florian, Mucha‐Kruczynska, Iwona, Weise, Christoph   +4 more
core   +1 more source

Septins as membrane influencers: direct play or in association with other cytoskeleton partners

Frontiers in Cell and Developmental Biology, 2023
The cytoskeleton comprises three polymerizing structures that have been studied for a long time, actin microfilaments, microtubules and intermediate filaments, plus more recently investigated dynamic assemblies like septins or the endocytic-sorting ...
Béatrice Benoit, Christian Poüs, Christian Poüs, Anita Baillet   +3 more
doaj   +1 more source

Regulation of polarised growth in fungi [PDF]

, 2008
Polarised growth in fungi occurs through the delivery of secretory vesicles along tracks formed by cytoskeletal elements to specific sites on the cell surface where they dock with a multiprotein structure called the exocyst before fusing with the ...
Adamo, Adamo, Adams, Akashi, Ayad-Durieux, Bachewich, Bartnicki-Garcia, Bartnicki-Garcia, Bassilana, Bassilana, Bassilana, Behrens, Berman, Bidlingmaier, Bose, Boyce, Boyce, Boyce, Boyd, Brown, Caviston, Chant, Chapa y Lazo, Collinge, Colman-Lerner, Court, Crampin, Cvrckova, Dong, Drgonova, Dunkler, Feng, Finger, France, Gao, Girbardt, Gladfelter, Goehring, Gorovits, Gulli, Guo, Harris, Harris, Hartwell, Hergovich, Hou, Hou, Irazoqui, Jin, Karnoub, Knechtle, Kohno, Konzack, Kron, Leberer, Leberer, Leberer, Leonhard, Lew, Li, Liu, Loeb, Loeb, Longtine, Mahlert, Mata, McCollum, McCusker, Medkova, Mehta, Mendenhall, Nelson, Nonaka, Novick, Pan, Park, Pearson, Peter, Peter E. Sudbery, Philippsen, Punt, Qadota, Racki, Read, Santangelo, Schmidt, Seiler, Seiler, Sinha, Smith, Soll, Stevenson, Sudbery, Sudbery, Sudbery, Tamaskovic, Tanaka, Tcheperegine, Trinci, Verde, Versele, Virag, Virag, Walton, Walworth, Wedlich-Soldner, Wedlich-Soldner, Wendland, Wu, Yarden, Zhang, Zheng, Zheng   +112 more
core   +1 more source

The hierarchical assembly of septins revealed by high-speed AFM

Nature Communications, 2020
Septins are GTP-binding proteins involved in diverse cellular processes including division, polarity maintenance and membrane remodeling. Here authors use high-speed atomic force microscopy to show that assembly of septin filaments is a diffusion-driven ...
Fang Jiao, Kevin S. Cannon, Yi-Chih Lin, Amy S. Gladfelter, Simon Scheuring   +4 more
doaj   +1 more source

Role of Nucleotide Binding in Septin-Septin Interactions and Septin Localization in Saccharomyces cerevisiae [PDF]

Molecular and Cellular Biology, 2008
Septins are a conserved family of eukaryotic GTP-binding, filament-forming proteins. In Saccharomyces cerevisiae, five septins (Cdc3p, Cdc10p, Cdc11p, Cdc12p, and Shs1p) form a complex and colocalize to the incipient bud site and as a collar of filaments at the neck of budded cells.
Nagaraj, Satish, Rajendran, Ashok, Jackson, Charles E, Longtine, Mark S   +3 more
openaire   +3 more sources

Lipopolysaccharide (LPS)-binding protein is carried on lipoproteins and acts as a cofactor in the neutralization of LPS. [PDF]

, 1994
Lipoproteins isolated from normal human plasma can bind and neutralize bacterial lipopolysaccharide (LPS) and may represent an important mechanism in host defense against gram-negative septic shock. Recent studies have shown that experimentally elevating
Kane, JP, Kunitake, ST, Lichenstein, H, Wright, SD, Wurfel, MM   +4 more
core   +1 more source

Phosphorylation of Pnut in the Early Stages of Drosophila Embryo Development Affects Association of the Septin Complex with the Membrane and Is Important for Viability

G3: Genes, Genomes, Genetics, 2018
Septin proteins are polymerizing GTPases that are found in most eukaryotic species. Septins are important for cytokinesis and participate in many processes involving spatial modifications of the cell cortex. In Drosophila, septin proteins Pnut, Sep1, and
Katarina Akhmetova, Maxim Balasov, Anton Svitin, Elena Chesnokova, Matthew Renfrow, Igor Chesnokov   +5 more
doaj   +1 more source

MoMtg1 Acts as a Novel Transcriptional Repressor of MoSwi6 During Appressorium-Mediated Penetration in the Rice Blast Fungus. [PDF]

Adv Sci (Weinh)
Appressoria are specialized penetration structures for many plant pathogenic fungi, demanding precise cell cycle control. This study unveils MoMtg1 as a transcriptional repressor of MoSwi6, orchestrating MoCYC1 expression during turgor‐driven cell cycle progression to enable appressorium‐mediated penetration. Moreover, a small‐molecule inhibitor ZS1619
Wang X, Zhang T, Li Q, Ji CA, Huang L, Zhang M, Yang L, Liu X, Liu M, Li G, Zhang Z, Zhang H.   +11 more
europepmc   +2 more sources