Unlocking the potential of cell‐permeable nanobodies for intracellular applications
FEBS Letters, EarlyView.This review outlines current strategies for delivery of nanobodies into cells and highlights recent examples of functional applications. By addressing and manipulating intracellular targets, these molecules hold great potential for treating cancer, respiratory diseases and neurological disorders, making this a vibrant area of research in the biomedical
Mariona Gené‐Verdés +2 more
wiley +1 more source
Annotation, phylogenetics, and expression of the nuclear receptors in
BMC Genomics, 2009 Background The nuclear receptor superfamily currently consists of seven gene subfamilies that encompass over 80 distinct receptor proteins. These transcription factors typically share a common five-domain structure with a highly conserved DNA-binding ...
Kwon Gwijun +4 more
doaj +1 more source
Comparing the paths of Hedgehog release in artificial and natural settings
FEBS Letters, EarlyView.Hh morphogens require solubilization factors to overcome their tight association with the plasma membrane and signal to distant cells, but the precise functions of these factors are controversial. Here, we use published in vivo observations as the most relevant evidence to test their suggested functions and discuss contradictions and gaps between in ...
Janna Puschmann, Kay Grobe
wiley +1 more source
Structural Dynamics and Allosteric Signaling in Ionotropic Glutamate Receptors [PDF]
, 2013 Ionotropic glutamate receptors (iGluRs) are ligand-gated ion channels that mediate excitatory neurotransmission events in the central nervous system. All distinct classes of iGluRs (AMPA, NMDA, Kainate) are composed of an N-terminal domain (NTD) and a ...
Dutta, Anindita
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How structural disorder and polyelectrolyte properties of prothymosin α enable its large interactome
FEBS Letters, EarlyView.In this review, complexes of the fully disordered and highly negatively charged prothymosin α are collected, described, and discussed. Linked to its poly‐electrostatic character, prothymosin α engages a large interactome through multiple different binding modes ranging from fully disordered complexes to short linear motif (SLiM)‐driven interactions ...
Ketty C. Tamburrini +3 more
wiley +1 more source
Structure and molecular interaction analysis of monoclonal antibodies in complex with receptor tyrosine kinases [PDF]
, 2010 Misregulated receptor tyrosine kinases (RTKs), i.e. the epidermal growth factor receptor EGFR or the insulin-like growth factor receptor 1 (IGF-1R), can be involved in the development of cancer.
Schmiedel, Judith
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A Genomic Point Mutation in the Extracellular Domain of the Thyrotropin Receptor in Patients with Graves’ Ophthalmopathy [PDF]
, 1994 Orbital and pretibial fibroblasts are targets of autoimmune attack in Graves' ophthalmopathy (GO) and pretibial dermopathy (PTD). The fibroblast autoantigen involved in these peripheral manifestations of Graves' disease and the reason for the association
Sarkar, Gobinda +4 more
core +1 more source
CdiA Effectors Use Modular Receptor-Binding Domains To Recognize Target Bacteria
mBio, 2017 Contact-dependent growth inhibition (CDI) systems encode CdiA effectors, which bind to specific receptors on neighboring bacteria and deliver C-terminal toxin domains to suppress target cell growth.
Zachary C. Ruhe +7 more
doaj +1 more source
Hijacking emergency granulopoiesis: Neutrophil ontogeny and reprogramming in cancer
Molecular Oncology, EarlyView.Neutrophils are highly plastic innate immune cells; their functions in cancer extend beyond the tumour microenvironment. This Review summarises current understanding of neutrophil maturation and heterogeneity and highlights tumour‐induced granulopoiesis as a systemic programme that expands immature, immunosuppressive neutrophils via tumour‐derived ...
Gabriela Marinescu, Yi Feng
wiley +1 more source
Structural and functional investigation of the cytoplasmic domain of the Fas death receptor [PDF]
, 2015 Activation of the transmembrane death receptor Fas (CD95/APO-1) by a membrane bound ligand (FasL/CD95L) activates the extrinsic pathway of apoptosis. Intracellular Fas death domains (DDs) are induced to oligomerise enabling binding to the adaptor protein
Wildsmith, GC
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