Results 51 to 60 of about 1,094 (157)

Saposins modulate human invariant Natural Killer T cells self-reactivity and facilitate lipid exchange with CD1d molecules during antigen presentation.

, 2013
Lipid transfer proteins, such as molecules of the saposin family, facilitate extraction of lipids from biological membranes for their loading onto CD1d molecules.
Dushek, Omer, Cypen, Jeremy, Van Der Merwe, PA, Qi, X, Qi, Xiaoyang, Gileadi, U, Napolitani, G, Cresswell, P, Cypen, J, Cerundolo, Vincenzo, Gileadi, Uzi, Dushek, O, Salio, Mariolina, Cerundolo, V, Wojno, Justyna, Aichinger, MC, Cox, Liam R; id_orcid, Napolitani, Giorgio, Yuan, W, Cresswell, Peter, Besra, GS, Veerapen, Natacha, Besra, Gurdyal S; id_orcid, Salio, M, Shepherd, D, Aichinger, Michael C, Ghadbane, H, Van Der Merwe, Philip, Veerapen, N, Ghadbane, Hemza, Cox, LR, Yuan, Weiming, Shepherd, Dawn, van der Merwe, P Anton, Wojno, J   +34 more
core   +1 more source

Saposins and Their Precursor, Prosaposin: Multifunctional Glycoproteins.

Trends in Glycoscience and Glycotechnology, 1996
Hiraiwa, Masao, Kishimoto, Yasuo
openaire   +2 more sources

Structural Investigations of Saposin/Hydrolase Systems [PDF]

, 2019
The degradation of sphingolipids (SLs) in mammals relies on the interplay between a set of lysosomal hydrolases and their cofactor proteins, the saposins.
Xiong, ZiJian
core   +2 more sources

Structural and Functional Studies of the Human Saposin Proteins

, 2012
The human saposins are four homologous activator proteins that are essential for the lysosomal degradation of sphingolipids (SLs) with small headgroups. They function in part to increase the solvent accessibility of these SLs to specific acid hydrolases
Popovic, Konstantin
core   +2 more sources

Characterization of Drosophila Saposin-related mutants as a model for lysosomal sphingolipid storage diseases

Disease Models & Mechanisms, 2017
Sphingolipidoses are inherited diseases belonging to the class of lysosomal storage diseases (LSDs), which are characterized by the accumulation of indigestible material in the lysosome caused by specific defects in the lysosomal degradation machinery ...
Julia Sellin, Heike Schulze, Marie Paradis, Dominic Gosejacob, Cyrus Papan, Andrej Shevchenko, Olympia Ekaterina Psathaki, Achim Paululat, Melanie Thielisch, Konrad Sandhoff, Michael Hoch   +10 more
doaj   +1 more source

The lipid transfer protein Saposin B does not directly bind CD1d for lipid antigen loading [version 2; peer review: 3 approved]

Wellcome Open Research, 2019
Background: Lipid antigens are presented on the surface of cells by the CD1 family of glycoproteins, which have structural and functional similarity to MHC class I molecules.
Maria Shamin, Tomasz H. Benedyk, Stephen C. Graham, Janet E. Deane   +3 more
doaj   +1 more source

Structural studies of the saposins and PagP

, 2004
This thesis comprises two parts. The first chapters describe structural studies of sphingolipid activator proteins, the saposins. This is followed by studies of the outer membrane protein PagP.
Ahn, Victoria Elizabeth
core   +1 more source

Cathepsin-mediated regulation of autophagy in saposin C deficiency [PDF]

Autophagy, 2013
Saposin C deficiency, a rare variant form of Gaucher disease, is due to mutations in the prosaposin gene (PSAP) affecting saposin C expression and/or function. We previously reported that saposin C mutations affecting one cysteine residue result in autophagy dysfunction.
Tatti M, Motta M, DI BARTOLOMEO, Sabrina, Cianfanelli V, Salvioli R.   +4 more
openaire   +2 more sources

Molecular role of sulfated glycoprotein-1 (SGP-I/Prosaposin) in Sertoli cells [PDF]

, 1995
Sulfated Glycoprotein- 1 (SGP- 1) is a major polypeptide secreted by rat Sertoli cells. Sequence analysis revealed a 70% sequence similarity with human prosaposin and a 80% similarity with mouse prosaposin.
Morales, C.R., Igdoura, S., Zhao, Q., El-Alfy, M.   +3 more
core  

Immunolocalization of the saposin-like insert of plant aspartic proteinases exhibiting saposin C activity. Expression in young flower tissues and in barley seeds

, 2005
The plant- specific insert ( PSI) of cypro11 gene- encoding cyprosin, an aspartic proteinase from Cynara cardunculus, has been cloned by polymerase chain reaction ( PCR) into a bacterial expression vector.
Marttila, S, Al-Karadaghi, Salam, Picaud, S, Hiraiwa, M, Brodelius, M, Brodelius, P E   +5 more
core   +1 more source