Results 51 to 60 of about 3,184,320 (288)

Organoids in pediatric cancer research

FEBS Letters, EarlyView.
Organoid technology has revolutionized cancer research, yet its application in pediatric oncology remains limited. Recent advances have enabled the development of pediatric tumor organoids, offering new insights into disease biology, treatment response, and interactions with the tumor microenvironment.
Carla Ríos Arceo, Jarno Drost
wiley   +1 more source

BAR Domain Scaffolds in Dynamin-Mediated Membrane Fission [PDF]

Cell, 2014
Biological membranes undergo constant remodeling by membrane fission and fusion to change their shape and to exchange material between subcellular compartments. During clathrin-mediated endocytosis, the dynamic assembly and disassembly of protein scaffolds comprising members of the bin-amphiphysin-rvs (BAR) domain protein superfamily constrain the ...
Daumke, Oliver, Roux, Aurélien, Haucke, Volker   +2 more
openaire   +3 more sources

Salmonella lipopolysaccharide‐containing supported lipid bilayers as platforms to study bacteriophage interactions

FEBS Letters, EarlyView.
We present robust protocols for the preparation of supported lipid bilayers (SLBs) incorporating either Salmonella smooth LPS or outer membrane vesicles (OMVs). We use a combination of quartz crystal microbalance with dissipation (QCM‐D) and fluorescence microscopy to both characterize the SLBs of various compositions and to probe their interactions ...
Hudson P. Pace, Alyssa Borges, Charles Arnaud, Tove Karlsson, Nina K. Bröker, Stefanie Barbirz, Marta Bally   +6 more
wiley   +1 more source

ACAP1 assembles into an unusual protein lattice for membrane deformation through multiple stages.

PLoS Computational Biology, 2019
Studies on the Bin-Amphiphysin-Rvs (BAR) domain have advanced a fundamental understanding of how proteins deform membrane. We previously showed that a BAR domain in tandem with a Pleckstrin Homology (PH domain) underlies the assembly of ACAP1 (Arfgap ...
Chun Chan, Xiaoyun Pang, Yan Zhang, Tongxin Niu, Shengjiang Yang, Daohui Zhao, Jian Li, Lanyuan Lu, Victor W Hsu, Jian Zhou, Fei Sun, Jun Fan   +11 more
doaj   +1 more source

F-BAR domains: multifunctional regulators of membrane curvature [PDF]

Journal of Cell Science, 2008
The F-BAR-domain-containing proteins (F-BAR proteins) are a group of adaptor proteins, members of which are found in all eukaryotes except plants. Also known as Pombe/Cdc15 homology (PCH)-family proteins, they have essential roles in fundamental biological processes, such as endocytosis ...
Robert J W, Heath, Robert H, Insall
openaire   +2 more sources

ABL kinase‐dependent phosphorylation of SH proteins promotes their direct interaction with CRK family SH2 domains

FEBS Letters, EarlyView.
CT10 regulator of kinase (CRK) and CRK‐Like (CRKL) are signaling adaptors driving cell adhesion, motility, differentiation, and proliferation. SH2‐domain containing (SH) proteins are enriched in YXXP motifs which when phosphorylated create preferred binding sites for CRK family SH2 domains.
Phoebe M. Cousens, Brendan W. Chandler, Anna M. Schmoker, Jaye L. Weinert, Charlotte A. Kearns, Warren T. Yacawych, Amila Šemić, Alicia M. Ebert, Bryan A. Ballif   +8 more
wiley   +1 more source

Distinct Bin/Amphiphysin/Rvs (BAR) family proteins may assemble on the same tubule to regulate membrane organization in vivo

Heliyon
Intracellular membrane tubules play a crucial role in diverse cellular processes, and their regulation is facilitated by Bin-Amphiphysin-Rvs (BAR) domain-containing proteins.
Bhagaban Mallik, Srikanth Pippadpally, Anjali Bisht, Sajad Bhat, Surabhi Mukherjee, Vimlesh Kumar   +5 more
doaj   +1 more source

Reconstructing enzyme evolution by protein engineering

FEBS Letters, EarlyView.
Natural enzyme evolution can be retraced by protein engineering methods such as directed evolution, rational design, and ancestral sequence reconstruction. These approaches reveal how enzymes emerged from ligand‐binding scaffolds, developed varying substrate preferences, formed oligomeric complexes, adapted to environmental changes, and evolved novel ...
Lukas Drexler, Markus R. Busch, Reinhard Sterner   +2 more
wiley   +1 more source

Structure‐forward targeting of claudins with synthetic binders

FEBS Letters, EarlyView.
Claudins form the paracellular barriers between epithelial and endothelial tissues at tight junctions and are targets for molecular binders with the goal of modulating barrier permeability. Claudin‐binding molecules are relevant in drug delivery or in altering claudin interactions with disease‐causing proteins.
Alex J. Vecchio
wiley   +1 more source

The BAR Domain Proteins: Molding Membranes in Fission, Fusion, and Phagy [PDF]

Microbiology and Molecular Biology Reviews, 2006
SUMMARYThe Bin1/amphiphysin/Rvs167 (BAR) domain proteins are a ubiquitous protein family. Genes encoding members of this family have not yet been found in the genomes of prokaryotes, but within eukaryotes, BAR domain proteins are found universally from unicellular eukaryotes such as yeast through to plants, insects, and vertebrates. BAR domain proteins
Ren, Gang, Vajjhala, Parimala, S. Lee, Janet, Winsor, Barbara, L. Munn, Alan   +4 more
openaire   +6 more sources