Results 31 to 40 of about 75,759 (281)

ADAM-17 is a poor prognostic indicator for patients with hilar cholangiocarcinoma and is regulated by FoxM1

BMC Cancer, 2018
Background A-disintegrin and metalloproteinases (ADAMs) are members of a family of multidomain transmembrane and secreted proteins. Specific ADAMs are upregulated in human cancers and correlated with tumor progression and poor outcome, but rarely studied
Xiaodong Jiao, Wenlong Yu, Jianxin Qian, Ying Chen, Peilian Wei, Wenzheng Fang, Guanzhen Yu   +6 more
doaj   +1 more source

A Metalloproteinase Cocktail from the Venom of Protobothrops flavoviridis Cleaves Amyloid Beta Peptides at the α-Cleavage Site

Toxins, 2023
A disintegrin and metalloproteinase (ADAM) family proteins are a major class of membrane-anchored multidomain proteinases that are responsible for the shedding of cell surface protein ectodomains, including amyloid precursor protein (APP).
Eugene Futai, Hajime Kawasaki, Shinichi Sato, Khadija Daoudi, Masafumi Hidaka, Taisuke Tomita, Tomohisa Ogawa   +6 more
doaj   +1 more source

Characterization of Mammalian ADAM2 and Its Absence from Human Sperm. [PDF]

PLoS ONE, 2016
The members of the ADAM (a disintegrin and metalloprotease) family are membrane-anchored multi-domain proteins that play prominent roles in male reproduction.
Heejin Choi, Sora Jin, Jun Tae Kwon, Jihye Kim, Juri Jeong, Jaehwan Kim, Suyeon Jeon, Zee Yong Park, Kang-Jin Jung, Kwangsung Park, Chunghee Cho   +10 more
doaj   +1 more source

Quantitative Proteomics Reveals That ADAM15 Can Have Proteolytic-Independent Functions in the Steady State

Membranes, 2022
A disintegrin and metalloproteinase 15 (ADAM15) is a member of the ADAM family of sheddases. Its genetic ablation in mice suggests that ADAM15 plays an important role in a wide variety of biological functions, including cartilage homeostasis ...
Chun-Yao Yang, Simone Bonelli, Matteo Calligaris, Anna Paola Carreca, Stephan A. Müller, Stefan F. Lichtenthaler, Linda Troeberg, Simone D. Scilabra   +7 more
doaj   +1 more source

Determining proteins responsible for the host range of potyviruses [PDF]

, 2022
The host range of a virus is important as it determines the characteristics of the virus and the distribution of the virus. The aim of this study was to use molecular dynamics simulations to model the interaction of specific virus proteins with plant ...
Adam Scanlon
core  

Expression of ADAM‐9 mRNA and protein in human breast cancer [PDF]

International Journal of Cancer, 2003
AbstractThe ADAMs (a disintegrin and metalloprotease) are membrane proteins containing both protease and adhesion domains and thus may be potentially important in cancer invasion and metastasis. The aim of our study was to investigate the distribution and potential clinical significance of ADAM‐9 in breast cancer.
O'Shea C, McKie N, Buggy Y, Duggan C, Hill ADK, McDermotti E, O'Higgins N, Duffy MJ   +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]

Journal 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.
Tousseyn, T, Thathiah, A, Jorissen, E, Raemaekers, T, Konietzko, U, Reiss, K, Maes, E, Snellinx, A, Serneels, L, Nyabi, O, Annaert, W, Saftig, P, Hartmann, D, De Strooper, B   +13 more
openaire   +2 more sources

Identification of ADAM 31: A Protein Expressed in Leydig Cells and Specialized Epithelia* [PDF]

Endocrinology, 2000
A family of proteins containing a disintegrin and metalloproteinase domain (ADAMs) has been identified recently. Here, we report the identification of a novel member of the ADAM protein family from mouse. This protein is designated ADAM 31. The complementary DNA sequence of ADAM 31 predicts a transmembrane protein with metalloproteinase, disintegrin ...
L, Liu, J W, Smith
openaire   +2 more sources

Leptospira interrogans endostatin-like outer membrane proteins bind host fibronectin, laminin and regulators of complement

, 2007
The pathogenic spirochete Leptospira interrogans disseminates throughout its hosts via the bloodstream, then invades and colonizes a variety of host tissues.
Matthew L Rotondi, Trevor P Creamer, Henry A. Choy, Brissette Catherine A., Kraiczy Peter, DeMoll, Edward, Edward Demoll, Peter Kraiczy, Stevenson, Brian, Suchard, Marc A, Creamer, Trevor P., Cooley Anne E., Matthew L. Rotondi, Kraiczy, Peter, Suchard, Marc A., Marc A. Suchard, Haake David A., Marija Pinne, Brissette, Catherine A, Catherine A. Brissette, Cooley, Anne E., Marc A Suchard, DeMoll Edward, Creamer, Trevor P, Pinne Marija, Verma, Ashutosh, Miller M. Clarke, Choy Henry A., Miller, M. Clarke, M Clarke Miller, Choy, Henry A, Pinne, Marija, Catherine A Brissette, Trevor P. Creamer, Verma Ashutosh, Haake, David A, Anne E. Cooley, Brissette, Catherine A., Rotondi, Matthew L., Suchard Marc A., Stevenson Brian, Creamer Trevor P., Brian Stevenson, Ashutosh Verma, M. Clarke Miller, Miller, M Clarke, Rotondi, Matthew L, Haake, David A., Rotondi Matthew L., Henry A Choy, David A Haake, Cooley, Anne E, Choy, Henry A., Anne E Cooley, David A. Haake   +54 more
core   +2 more sources

A widespread peroxiredoxin-like domain present in tumor suppression- and progression-implicated proteins. [PDF]

, 2010
Background Peroxide turnover and signalling are involved in many biological phenomena relevant to human diseases. Yet, all the players and mechanisms involved in peroxide perception are not known.
Grynberg Marcin, Marcin Grynberg, Lenart Anna, Anna Muszewska, Szczepińska Teresa, Lenart, Anna, Grynberg, Marcin, Krzysztof Pawłowski, Godzik, Adam, Muszewska Anna, Pawłowski Krzysztof, Muszewska, Anna, Teresa Szczepinska, Pawłowski, Krzysztof, Krzysztof Pawlowski, Godzik Adam, Anna Lenart, Adam Godzik, Szczepińska, Teresa   +18 more
core   +1 more source