Results 11 to 20 of about 181,469 (186)

Nuclear translocation and signalling of L1-CAM in human carcinoma cells requires ADAM10 and presenilin/gamma-secretase activity [PDF]

open access: yes, 2009
L1-CAM (L1 cell-adhesion molecule), or more simply L1, plays an important role in the progression of human carcinoma. Overexpression promotes tumour-cell invasion and motility, growth in nude mice and tumour metastasis.
Riedle, Svenja   +6 more
core   +2 more sources

ADAM-10 Regulates MMP-12 during Lipopolysaccharide-Induced Inflammatory Response in Macrophages

open access: yesJournal of Immunology Research, 2022
A disintegrin and metalloprotease 10 (ADAM-10), a member of the ADAM protease family, has biological activities related to TNF-α activation, cell adhesion, and migration, among other functions.
Yan Jiang   +9 more
doaj   +1 more source

Epigenetic Regulation of a Disintegrin and Metalloproteinase (ADAM) Transcription in Colorectal Cancer Cells: Involvement of β-Catenin, BRG1, and KDM4

open access: yesFrontiers in Cell and Developmental Biology, 2020
A disintegrin and metalloproteinase (ADAM) family of proteins play versatile roles in cancer development and progression. In the present study, we investigated the role of ADAM proteins in colorectal cancer (CRC) cell migration and invasion focusing on ...
Lina Sun   +9 more
doaj   +1 more source

Polymeric ADAM Protein Mimics Interrogate Mammalian Sperm–Egg Binding [PDF]

open access: yesChemBioChem, 2009
AbstractROMPing with the ADAMs family: The sperm‐surface display of egg adhesion proteins was investigated using multivalent polymer sperm mimics. Ruthenium‐catalyzed ring opening metathesis polymerization (ROMP) was used to synthesize heterovalent polymers.magnified imageThe sperm proteins ADAM2 and ADAM3, members of the ADAM family of proteins, have ...
Younjoo, Lee, Nicole S, Sampson
openaire   +2 more sources

Preferred SH3 domain partners of ADAM metalloproteases include shared and ADAM-specific SH3 interactions. [PDF]

open access: yesPLoS ONE, 2015
A disintegrin and metalloproteinases (ADAMs) constitute a protein family essential for extracellular signaling and regulation of cell adhesion. Catalytic activity of ADAMs and their predicted potential for Src-homology 3 (SH3) domain binding show a ...
Iivari Kleino   +4 more
doaj   +1 more source

ADAMDEC1 accelerates GBM progression via activation of the MMP2-related pathway

open access: yesFrontiers in Oncology, 2022
The ADAM (a disintegrin and metalloprotease) gene-related family including ADAM, ADAMTS, and ADAM-like decysin-1 has been reported to play an important role in the pathogenesis of multiple diseases, including cancers (lung cancer, gliomas, colorectal ...
Huimin Qi   +11 more
doaj   +1 more source

Secretion-Positive LGI1 Mutations Linked to Lateral Temporal Epilepsy Impair Binding to ADAM22 and ADAM23 Receptors [PDF]

open access: yes, 2016
Autosomal dominant lateral temporal epilepsy (ADTLE) is a focal epilepsy syndrome caused by mutations in the LGI1 gene, which encodes a secreted protein.
Belluzzi, Elisa   +7 more
core   +3 more sources

Evolutionary divergence and functions of the ADAM and ADAMTS gene families

open access: yesHuman Genomics, 2009
The 'A-disintegrin and metalloproteinase' (ADAM) and 'A-disintegrin and metalloproteinase with thrombospondin motifs' (ADAMTS) genes make up two similar, yet distinct, gene families.
Brocker Chad N   +2 more
doaj   +1 more source

ADAM10 Localization in Temporomandibular Joint Disk with Internal Derangement: An Ex Vivo Immunohistochemical Study [PDF]

open access: yes, 2016
The purpose of this study was to determine the presence of ADAM10 in temporomandibular joint disk with internal derangement. Twenty-five paraffin blocks of displaced temporomandibular joint (TMJ) disk specimens from earlier investigations were retrieved ...
Almeida, Luis Eduardo   +7 more
core   +2 more sources

The ADAMs family of metalloproteases: multidomain proteins with multiple functions [PDF]

open access: yesGenes & Development, 2003
The ADAMs family of transmembrane proteins belongs to the zinc protease superfamily. Members of the family have a modular design, characterized by the presence of metalloprotease and integrin receptor-binding activities, and a cytoplasmic domain that in many family members specifies binding sites for various signal transducing proteins.
Darren F, Seals, Sara A, Courtneidge
openaire   +2 more sources

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