Results 81 to 90 of about 1,124 (173)

Comparative proteomic analysis of cold seep clam Archivesica marissinica and shallow water shellfish Ruditapes philippinarum provides insights into the adaptation mechanisms of deep-sea mollusks

Frontiers in Marine Science
IntroductionThe deep-sea environment is always characterized by high hydrostatic pressure, fluctuating temperatures, heavy metals, darkness, and others.
Xue Kong, Xue Kong, Xue Kong, Wei Wang, Wei Wang, Sunan Chen, Sunan Chen, Ning Mao, Ning Mao, Yuefeng Cai, Yuefeng Cai, Yuefeng Cai, Yanan Li, Sunan Xia, Sunan Xia, Haibin Zhang, Xin Shen, Xin Shen, Xin Shen   +18 more
doaj   +1 more source

Interaction of saposins, acidic lipids, and glucosylceramidase.

Journal of Biological Chemistry, 1990
Activity of lysosomal glucosylceramidase is stimulated by two small glycoproteins, saposin A and C, which are, together with two other similar glycoproteins, derived from a single precursor protein. This enzyme is also stimulated by naturally occurring acidic lipids, such as phosphatidylserine and gangliosides. Using highly purified glucosylceramidase,
S, Morimoto, Y, Kishimoto, J, Tomich, S, Weiler, T, Ohashi, J A, Barranger, K A, Kretz, J S, O'Brien   +7 more
openaire   +2 more sources

Saposin fold revealed by the NMR structure of NK-lysin.

, 1997
NK-lysin is the first representative of a family of sequence related proteins--saposins, surfactant-associated protein B, pore forming amoeba proteins, and domains of acid sphingomyelinase, acyloxyacylhydrolase and plant aspartic proteinases--for which a
Liepinsh, E, Otting, G, Andersson, M,, Jean-Marie Ruysschaert, Gottfried Otting, Andersson, M, Ruysschaert, Jean Marie, Edvards Liepinsh, Mats Andersson, Ruysschaert, JM   +9 more
core   +1 more source

Deficiency of Glucocerebrosidase Activity beyond Gaucher Disease: PSAP and LIMP-2 Dysfunctions [PDF]

Int J Mol Sci
Glucocerebrosidase (GCase) is a lysosomal enzyme that catalyzes the breakdown of glucosylceramide in the presence of its activator saposin C (SapC). SapC arises from the proteolytical cleavage of prosaposin (encoded by PSAP gene), which gives rise to ...
Pavan E, Peruzzo P, Cattarossi S, Bergamin N, Bordugo A, Sechi A, Scarpa M, Biasizzo J, Colucci F, Dardis A.   +9 more
europepmc   +2 more sources

Scatter plots of signature proteins for specific worm tissues or processes to illustrate the extent of variation between heads and tails.

, 2016
The format of the plot is the same as for Fig 1 Those genes with a > fourfold difference in the heads are demarcated by an ellipse. A, nervous system; B, tegument; C, Gut secreted proteins and saposins; D, Muscle and cytoskeleton; E, Parenchyma (glycogen
R. Alan Wilson (91815), Sally James (834532), Peter D. Ashton (834533), William Castro Borges (834534), Juliana Vitoriano-Souza (297615), Sandy MacDonald (834530), Ricardo DeMarco (80218), Xiao Hong Li (834529), Luciana C. C. Leite (185297), Leonardo P. Farias (253307), Leandro Xavier Neves (834531)   +10 more
core   +1 more source

Estudio computacional de proteínas transportadoras de lípidos inmunológicamente relevantes y de su interacción con ligandos unidos a membranas

, 2019
Allergic diseases are an increasing concern, yet, unfortunately, most of the molecular events that lead to an immune response against an innocuous protein (“allergen”) still remain unknown.
Mínguez Toral, Marina
core  

CD1d function is regulated by microsomal triglyceride transfer protein

, 2004
CD1d is a major histocompatibility complex (MHC) class I-related molecule that functions in glycolipid antigen presentation to distinct subsets of T cells that express natural killer receptors and an invariant T-cell receptor-α chain (invariant NKT cells)
Timothy Kuo, Kaser, Arthur, Masaru Yoshida, Kuo, Timothy, Nadia Corazza, Arthur Kaser, Azucena Salas, Nagaishi, Takashi, Brozovic, Suzana, Kim, Jin Yong, Blumberg, Richard S., Young, Stephen G., Alicia Little, Exley, Mark, Jin Yong Kim, Mark Exley, Richard S Blumberg, Betz, Stephanie, Glickman, Jonathan, Yoshida, Masaru, Stephen G Young, Colgan, Sean P., Jonathan Glickman, Jamin Morrison, Daohong Chen, Suzana Brozovic, Chen, Daohong, Morrison, Jamin, Takashi Nagaishi, Sean P Colgan, Salas, Azucena, Corazza, Nadia, Little, Alicia, Stephanie Betz   +33 more
core   +1 more source

Functional Organization of Saposin C [PDF]

Journal of Biological Chemistry, 1996
Xiaoyang Qi, Wen Qin, Ying Sun, Keiji Kondoh, Gregory A. Grabowski   +4 more
openaire   +1 more source

Expression of prosaposin and its G protein-coupled receptor (GPR) 37 in mouse cochlear and vestibular nuclei. [PDF]

J Vet Med Sci, 2023
Fuyuki A, Yamamoto S, Sohel MSH, Homma T, Kitamura K, Onouchi S, Saito S.   +6 more
europepmc   +1 more source

Reduced prosaposin levels in HepG2 cells with long-term coenzyme Q10 deficiency. [PDF]

J Clin Biochem Nutr, 2022
Takeuchi H, Sugawara K, Okamoto M, Nakamura A, Tanaka T, Fujita Y, Ishiguro K, Yamazaki H, Okada M, Mikami A, Fujisawa A, Yamamoto Y, Kashiba M.   +12 more
europepmc   +1 more source