Results 51 to 60 of about 181,469 (186)

Domain integration of ADAM family proteins: Emerging themes from structural studies

Experimental Biology and Medicine, 2019
ADAM (a disintegrin and metalloproteinase) proteins are type-1 transmembrane and secreted proteins that function in cell adhesion and signal transduction. Here we review the structural features of ADAM proteins that direct their biological functions in ectodomain shedding and cell adhesion.
Tom CM Seegar, Stephen C Blacklow
openaire   +3 more sources

Distinct ADAM Metalloproteinases Regulate G Protein-coupled Receptor-induced Cell Proliferation and Survival [PDF]

Journal of Biological Chemistry, 2004
Cross-talk between G protein-coupled receptor (GPCR) and epidermal growth factor receptor (EGFR) signaling systems is widely established in a variety of normal and transformed cell types. Here, we demonstrate that the EGFR transactivation signal requires metalloproteinase cleavage of epidermal growth factor-like growth factor precursors in fibroblasts,
Schafer, B., Marg, B., Gschwind, A., Ullrich, A.   +3 more
openaire   +3 more sources

Rosetta Brains: A Strategy for Molecularly-Annotated Connectomics [PDF]

, 2014
We propose a neural connectomics strategy called Fluorescent In-Situ Sequencing of Barcoded Individual Neuronal Connections (FISSEQ-BOINC), leveraging fluorescent in situ nucleic acid sequencing in fixed tissue (FISSEQ).
Boyden, Edward S, Church, George M, Daugharthy, Evan R, Kalhor, Reza, Kebschull, Justus M, Kording, Konrad P, Lee, Je Hyuk, Marblestone, Adam H, Mishchenko, Yuriy, Peikon, Ian D, Shipman, Seth L, Zador, Anthony M   +11 more
core  

The role and therapeutic targeting of α-, β- and γ-secretase in Alzheimer's disease [PDF]

, 2015
Alzheimer's disease (AD) is the most common form of dementia in the elderly and its prevalence is set to increase rapidly in coming decades. However, there are as yet no available drugs that can halt or even stabilize disease progression. One of the main
Baillie, George S., Cameron, Ryan T., Hillert, Ellin-Kristina, MacLeod, Ruth   +3 more
core   +1 more source

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

Frontiers 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, Ariana A. Vasconcelos, Jorge C. Estrada, Victor David, Luciana S. Wermelinger, Fabio C. L. Almeida, Fabio C. L. Almeida, Russolina B. Zingali   +7 more
doaj   +1 more source

Convolutional LSTM Networks for Subcellular Localization of Proteins [PDF]

, 2015
Machine learning is widely used to analyze biological sequence data. Non-sequential models such as SVMs or feed-forward neural networks are often used although they have no natural way of handling sequences of varying length.
A Graves, A Höglund, A Prlić, C Magnan, G Dahl, HY Xiong, LJP Maaten Van Der, M Schuster, MCF Thomsen, O Emanuelsson, P Baldi, P Lena Di, S Briesemeister, S Henikoff, S Hochreiter, SF Altschul, T Blum, T Goldberg, T Petersen, Y Bengio   +19 more
core   +3 more sources

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

Frontiers 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, Amandine eBonnet, Anne eBernard, Yannick eMarchalant, Eliane eCharrat, Frédéric eChecler, Michel eKhrestchatisky, Kévin eBaranger, Santiago eRivera   +8 more
doaj   +1 more source

The telomeric protein AKTIP interacts with A- and B-type lamins and is involved in regulation of cellular senescence [PDF]

, 2016
AKTIP is a shelterin-interacting protein required for replication of telomeric DNA. Here, we show that AKTIP biochemically interacts with A- and B-type lamins and affects lamin A, but not lamin C or B, expression.
Astrologo, Letizia, Biroccio, Annamaria, Burla, Romina, Carcuro, Mariateresa, Crescenzi, Marco, Cundari, Enrico, D'Apice, Maria Rosaria, Fratini, Federica, Gatti, Maurizio, LA TORRE, Mattia, Lattanzi, Giovanna, Raffa, GRAZIA DANIELA, Raimondo, Domenico, Saggio, Isabella, Spitalieri, Paola   +14 more
core   +2 more sources

The ADAMTS (A Disintegrin and Metalloproteinase with Thrombospondin motifs) family [PDF]

, 2015
The ADAMTS (A Disintegrin and Metalloproteinase with Thrombospondin motifs) enzymes are secreted, multi-domain matrix-associated zinc metalloendopeptidases that have diverse roles in tissue morphogenesis and patho-physiological remodeling, in ...
A Colige, A Didangelos, A Luque, A Moncada-Pazos, A Noel, A Tan Ide, AC Jonsson-Rylander, AC Nicholson, AJ Fosang, B Joe, BH Koo, BH Koo, BV Nusgens, C Casal, C Esselens, C Gendron, C Kintakas, C Lopez-Otin, C Ricciardelli, CB Kern, CG Viloria, CH Mjaatvedt, CJ Liu, CJ Liu, CL Jacobi, CM Dancevic, CN Brocker, CR Flannery, D Wagsater, DL Russell, DL Silver, DR Edwards, DR McCulloch, DT Jones, Dylan R Edwards, EA Lin, EC Arner, ED Karagiannis, EM Majerus, F Guo, F Vazquez, FG Brunet, FX Gomis-Ruth, FX Gomis-Ruth, G Gao, G Gao, G Hashimoto, G Murphy, GC Choi, GE Lind, GG Levy, GJ Wayne, Grant N Wheeler, H Enomoto, H Jin, H Stanton, H Stanton, HL Lung, HM Brown, I Abbaszade, I Peluso, Ines Desanlis, J Dubail, J Dubail, J Felsenstein, J Hofsteenge, J Huxley-Jones, J Huxley-Jones, J Morales, JA Pyun, JC Adams, JC Rodriguez-Manzaneque, JC Rodriguez-Manzaneque, JC Rodriguez-Manzaneque, JD Sandy, JM Longpre, K Demircan, K Fujikawa, K Gopalakrishnan, K Kuno, K Kuno, K Stankunas, K Tamura, K Yamamoto, K Yamamoto, L Angerer, L Faivre, L Mittaz, L Mosyak, L Troeberg, L Troeberg, L Troeberg, L Wagstaff, LA Collins-Racie, LE Dupuis, LM Ricketts, M Cudic, M Hour El, M Kashiwagi, M Krampert, M Llamazares, MA Aldahmesh, MD Tortorella, MN Vankemmelbeke, N Dagoneau, N Hattori, N Rocks, N Rocks, N Stupka, NH Lim, NV Lee, NV Lee, P Wang, PH Lo, PJ Koshy, PS Chockalingam, R Kelwick, RC Salter, RH Song, Richard Kelwick, RL Robker, RP Somerville, RP Somerville, RS Patel, S Abdul-Majeed, S Gerhardt, S Kumar, S Kumar, S Nandadasa, S Porter, S Porter, SS Apte, SS Glasson, T Fontanil, T Shindo, TN Wight, U Auf Dem Keller, W Du, W Zeng, WE Kutz, WM Wang, X Lu, X Pu, XL Zheng, YJ Liu, YP Hsu   +145 more
core   +1 more source

Loss of ADAM29 does not affect viability and fertility in mice but improves wound healing

iScience
Summary: ADAM29 (a disintegrin and metalloprotease domain 29) is a member of the membrane-anchored ADAM family of proteins, which is highly expressed in testis and may mediate different physiological and pathological processes.
Diana Campos-Iglesias, Alejandro A. Montero, Francisco Rodríguez, Carlos López-Otín, José M.P. Freije   +4 more
doaj   +1 more source