Results 51 to 60 of about 171,066 (327)

Extracellular proteolysis in structural and functional plasticity of mossy fiber synapses in hippocampus

open access: yesFrontiers in Cellular Neuroscience, 2015
Brain is continuously altered in response to experience and environmental changes. One of the underlying mechanisms is synaptic plasticity, which is manifested by modification of synapse structure and function.
Grzegorz eWiera   +3 more
doaj   +1 more source

Cell‐free and extracellular vesicle microRNAs with clinical utility for solid tumors

open access: yesMolecular Oncology, EarlyView.
Cell‐free microRNAs (cfmiRs) are small‐RNA circulating molecules detectable in almost all body biofluids. Innovative technologies have improved the application of cfmiRs to oncology, with a focus on clinical needs for different solid tumors, but with emphasis on diagnosis, prognosis, cancer recurrence, as well as treatment monitoring.
Yoshinori Hayashi   +6 more
wiley   +1 more source

Structure-Function Relationship of the Disintegrin Family: Sequence Signature and Integrin Interaction

open access: yesFrontiers in Molecular Biosciences, 2021
Disintegrins are small cysteine-rich proteins found in a variety of snake venom. These proteins selectively modulate integrin function, heterodimeric receptors involved in cell-cell and cell-matrix interaction that are widely studied as therapeutic ...
Ariana A. Vasconcelos   +7 more
doaj   +1 more source

Role of host-derived ADAM-9 in tumor invasion and metastasis of malignant melanoma [PDF]

open access: yes, 2012
A Disintegrin And Metalloproteases (ADAMs) represents a family of transmembrane proteins with a distinct multidomain structure including a metalloprotease, disintegrin, and cysteine-rich domain.
Ngum, Anna Abety
core  

Detection rate for ESR1 mutations is higher in circulating‐tumor‐cell‐derived genomic DNA than in paired plasma cell‐free DNA samples as revealed by ddPCR

open access: yesMolecular Oncology, EarlyView.
Analysis of ESR1 mutations in plasma cell‐free DNA (cfDNA) is highly important for the selection of treatment in patients with breast cancer. Using multiplex‐ddPCR and identical blood draws, we investigated whether circulating tumor cells (CTCs) and cfDNA provide similar or complementary information for ESR1 mutations.
Stavroula Smilkou   +11 more
wiley   +1 more source

Differential Spatio-Temporal Regulation of MMPs in the 5xFAD Mouse Model of Alzheimer’s disease: Evidence for aPro-Amyloidogenic Role of MT1-MMP

open access: yesFrontiers in Aging Neuroscience, 2014
Matrix metalloproteinases (MMPs) are pleiotropic endopeptidases involved in a variety of neurodegenerative/neuroinflammatory processes through their interactions with a large number of substrates.
Nathalie ePy   +8 more
doaj   +1 more source

RNAi-mediated knockdown of gut receptor-like genes prohibitin and α-amylase altered the susceptibility of Galleria mellonella to Cry1AcF toxin

open access: yesBMC Genomics, 2022
Background Due to the prolonged usage of Bt-based biopesticides and Bt-transgenic crops worldwide, insects are continually developing resistance against Cry toxins.
Tushar K. Dutta   +6 more
doaj   +1 more source

ADAM11 a novel regulator of Wnt and BMP4 signaling in neural crest and cancer

open access: yesFrontiers in Cell and Developmental Biology, 2023
Introduction: Cranial neural crest (CNC) cells are induced at the border of the neural plate by a combination of FGF, Wnt, and BMP4 signaling. CNC then migrate ventrally and invade ventral structures where they contribute to craniofacial development ...
Ankit Pandey   +3 more
doaj   +1 more source

Drosophila metalloproteases in development and differentiation: The role of ADAM proteins and their relatives

open access: yesEuropean Journal of Cell Biology, 2011
ADAM metalloproteases are membrane bound glycoproteins that control many biological processes during development and differentiation, mainly by acting as ectodomain sheddases. The Drosophila genome contains five genes that code for classical ADAM proteins which are characterized by a highly conserved domain structure with the respective catalytic ...
Heiko Meyer   +7 more
openaire   +3 more sources

ADAM10, the Rate-limiting Protease of Regulated Intramembrane Proteolysis of Notch and Other Proteins, Is Processed by ADAMS-9, ADAMS-15, and the γ-Secretase [PDF]

open access: yesJournal of Biological Chemistry, 2009
ADAM10 is involved in the proteolytic processing and shedding of proteins such as the amyloid precursor protein (APP), cadherins, and the Notch receptors, thereby initiating the regulated intramembrane proteolysis (RIP) of these proteins. Here, we demonstrate that the sheddase ADAM10 is also subject to RIP.
Elke Maes   +16 more
openaire   +3 more sources

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