PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 26194854-1 2015 Natural Killer T (NKT) cells are unique lymphocytes characterized by their expression of a single invariant antigen receptor encoded by Valpha14Jalpha18 in mice and Valpha24Jalpha18 in humans, which recognizes glycolipid antigens in association with the monomorphic CD1d molecule. Glycolipids 210-220 CD1c molecule Homo sapiens 266-269 29559523-2 2018 A single class of major histocompatibility class-like molecules, called CD1 molecules, can present lipids and glycolipids to the immune system. Glycolipids 110-121 CD1c molecule Homo sapiens 72-75 23530121-6 2013 These studies identify antigen processing of a natural bacterial antigen in the human CD1c system, indicating that cells act on glycolipids to generate a highly simplified neoepitope composed of a sugar-free phosphate anion. Glycolipids 128-139 CD1c molecule Homo sapiens 86-90 18671950-1 2008 The glycolipid alpha-galactosylceramide (alpha-GalCer), when presented on CD1 molecules by antigen presenting cells (APCs) to invariant NKT (iNKT cells), is a potent immunomodulator. Glycolipids 4-14 CD1c molecule Homo sapiens 74-77 21711522-6 2011 RESULTS: NK cells were conjugated with B-cell targets lacking major histocompatibility complex class I 721.221 cells, and iNKT cells were conjugated with glycolipid-pulsed CD1-bearing targets, then prepared for thin-section electron microscopy. Glycolipids 154-164 CD1c molecule Homo sapiens 172-175 21603161-1 2011 Group I CD1 (CD1a, CD1b, and CD1c) glycoproteins expressed on immature and mature dendritic cells present nonpeptide antigens (i.e., lipid or glycolipid molecules mainly of microbial origin) to T cells. Glycolipids 142-152 CD1c molecule Homo sapiens 29-33 20100930-7 2010 The long endogenous ligand found inside the binding groove of chCD1-1, together with binding data on various glycolipids and mycolic acid, strongly suggest that the unique avian CD1 family could bind long dual- and possibly triacyl-chain lipids. Glycolipids 109-120 CD1c molecule Homo sapiens 64-67 19735672-1 2010 The CD1 molecules are cell-surface proteins that bind and present foreign lipids and glycolipids to T cells in a manner similar to the MHC system. Glycolipids 85-96 CD1c molecule Homo sapiens 4-7 17951048-0 2007 CD1 mediated T cell recognition of glycolipids. Glycolipids 35-46 CD1c molecule Homo sapiens 0-3 16597658-2 2006 Recent studies of CD1, an MHC class I homolog encoded outside the MHC, have revealed that it presents diverse glycolipids to T cells. Glycolipids 110-121 CD1c molecule Homo sapiens 18-21 17593659-1 2007 CD1 proteins present self and microbial glycolipids to CD 1-restricted T cells, or in the case of CD1d, to NKT cells. Glycolipids 40-51 CD1c molecule Homo sapiens 0-3 17593659-1 2007 CD1 proteins present self and microbial glycolipids to CD 1-restricted T cells, or in the case of CD1d, to NKT cells. Glycolipids 40-51 CD1c molecule Homo sapiens 55-59 17593661-2 2007 The CD1 molecules have a structure broadly similar to major histocompatibility complex (MHC) class I and class II proteins, but because the antigens CD 1 presents are so different from peptides, it is possible that glycolipid reactive TCRs have properties that distinguish them from TCRs expressed by conventional T cells. Glycolipids 215-225 CD1c molecule Homo sapiens 4-7 17593661-2 2007 The CD1 molecules have a structure broadly similar to major histocompatibility complex (MHC) class I and class II proteins, but because the antigens CD 1 presents are so different from peptides, it is possible that glycolipid reactive TCRs have properties that distinguish them from TCRs expressed by conventional T cells. Glycolipids 215-225 CD1c molecule Homo sapiens 149-153 17073257-4 2006 Rearranged gene-derived receptors like immunoglobulin (Ig) and MHC molecule-restricted alphabeta-type of T-cell receptors (TCR) with high specificities and memories are used to recognize peptide antigens in the acquired immunity, whereas non-rearranged invaliant receptors such as toll-like receptors (TLR), gammasigmaTCR and CD1 molecule-restricted alphabeta TCR are employed to detect lipid/glycolipid or nucleic acid-related antigens in the innate immunity. Glycolipids 393-403 CD1c molecule Homo sapiens 326-329 16210906-1 2006 The recent discovery that T cells recognize endogenous and foreign lipid and glycolipid molecules presented by CD1 proteins has brought a major contribution in the understanding of innate and adaptive immune response to certain harmless antigens and infectious pathogens. Glycolipids 77-87 CD1c molecule Homo sapiens 111-114 16651026-3 2006 Recent studies suggest an association between the cellular machinery that loads CD1 molecules with glycolipids and several key proteins in lipid metabolism. Glycolipids 99-110 CD1c molecule Homo sapiens 80-83 15886110-1 2005 The discovery of the CD1 antigen-presenting system reveals that T cells survey the lipid content of target cells via T-cell receptor (TCR) contact with CD1 bound to lipids, glycolipids and small molecules. Glycolipids 173-184 CD1c molecule Homo sapiens 21-24 16445682-2 2006 CD1 glycoproteins comprise a family of molecules that are specialized for presenting lipids, glycolipids and lipopeptides to T lymphocytes. Glycolipids 93-104 CD1c molecule Homo sapiens 0-3 15886110-1 2005 The discovery of the CD1 antigen-presenting system reveals that T cells survey the lipid content of target cells via T-cell receptor (TCR) contact with CD1 bound to lipids, glycolipids and small molecules. Glycolipids 173-184 CD1c molecule Homo sapiens 152-155 15653315-3 2005 These unconventional T cells include glycolipid-specific CD1-restricted T cells and phospholigand-specific gammadelta T cells. Glycolipids 37-47 CD1c molecule Homo sapiens 57-60 15963780-2 2005 (2005) demonstrate in this issue of Immunity that bacterial infection leads to increased synthesis of autologous glycolipids that are recognized by CD1-restricted human T cells, indicating that recognition of inducible self-glycolipids could be a mechanism for microbial detection. Glycolipids 113-124 CD1c molecule Homo sapiens 148-151 15963780-2 2005 (2005) demonstrate in this issue of Immunity that bacterial infection leads to increased synthesis of autologous glycolipids that are recognized by CD1-restricted human T cells, indicating that recognition of inducible self-glycolipids could be a mechanism for microbial detection. Glycolipids 224-235 CD1c molecule Homo sapiens 148-151 15860372-1 2005 Invariant natural killer T (iNKT) cells are a subpopulation of T cells that are reactive with glycolipids that are bound by CD1d antigen-presenting molecules. Glycolipids 94-105 CD1c molecule Homo sapiens 124-127 14702138-4 2003 However, the discovery of CD1-mediated presentation of lipids and glycolipids to a variety of T-cell populations has greatly expanded the repertoire of antigens to which T cells can respond. Glycolipids 66-77 CD1c molecule Homo sapiens 26-29 15185366-1 2004 CD1 proteins present mammalian and microbial lipid and glycolipid antigens to different subsets of T cells. Glycolipids 55-65 CD1c molecule Homo sapiens 0-3 15185366-3 2004 In the present study we use four different glycolipids, some of which contain tumor-associated carbohydrate antigens, to develop a procedure to easily detect binding of glycolipids to CD1 proteins on viable cells. Glycolipids 43-54 CD1c molecule Homo sapiens 184-187 15185366-3 2004 In the present study we use four different glycolipids, some of which contain tumor-associated carbohydrate antigens, to develop a procedure to easily detect binding of glycolipids to CD1 proteins on viable cells. Glycolipids 169-180 CD1c molecule Homo sapiens 184-187 14711586-2 2004 To date, much of our understanding of the biology of the CD1/NKT system comes from studies that utilise non-natural glycolipid ligands. Glycolipids 116-126 CD1c molecule Homo sapiens 57-60 12803931-3 2003 Glycolipids are components of important antigen systems and membrane receptors; they participate in intracellular signalling mechanisms and may be presented to the immune system in the context of the novel CD1 molecules present on T lymphocytes. Glycolipids 0-11 CD1c molecule Homo sapiens 206-209 12818619-5 2003 The former two MHC molecules can present processed peptide antigens, whereas the last CD1 molecule can present glycolipid/lipid antigens. Glycolipids 111-121 CD1c molecule Homo sapiens 86-89 12761085-1 2003 CD1-restricted presentation of lipid or glycolipid antigens derived from Mycobacterium tuberculosis has been demonstrated by in vitro experiments using cultured T-cell lines. Glycolipids 40-50 CD1c molecule Homo sapiens 0-3 12644623-1 2003 T cells may recognize glycolipids and lipids of bacterial and self origin associated with the CD1 antigen-presenting molecules. Glycolipids 22-33 CD1c molecule Homo sapiens 94-97 12644623-2 2003 Understanding the mechanisms governing CD1-self glycolipid interaction will provide information on the molecular rules of glycolipid presentation and suggest new approaches to immunotherapy. Glycolipids 48-58 CD1c molecule Homo sapiens 39-42 11722638-0 2001 Glycolipid targets of CD1-mediated T-cell responses. Glycolipids 0-10 CD1c molecule Homo sapiens 22-25 11880205-2 2002 These novel T lymphocytes produce both Th1 and Th2 cytokines, recognize phospholipid and glycolipid antigens presented by CD1 molecules in a similar manner as peptides are recognized by cytotoxic T lymphocytes (CTL), and kill tumor cell targets by a perforin-dependent mechanism like NK cells and CTL. Glycolipids 89-99 CD1c molecule Homo sapiens 122-125 12580540-1 2003 In humans, group 1 CD1 glycoproteins present foreign and self lipid and glycolipid antigens to T-cells. Glycolipids 72-82 CD1c molecule Homo sapiens 19-22 12077262-7 2002 Using guinea pig cell lines transfected with individual CD1 isoforms as target cells in cytotoxic T cell assays, we found that guinea pig CD1b and CD1c molecules presented M. tuberculosis glycolipid Ags to T cells raised by mycobacterial lipid immunization. Glycolipids 188-198 CD1c molecule Homo sapiens 147-151 11722638-1 2001 Members of the CD1 family of antigen-presenting molecules bind and present a variety of mammalian and microbial glycolipids for specific recognition by T cells. Glycolipids 112-123 CD1c molecule Homo sapiens 15-18 11722638-3 2001 Most models of CD1-restricted T cells function in infectious, neoplastic, or autoimmune diseases and are based on the premise that CD1-restricted T-cell responses are initiated by alterations in cellular glycolipid content. Glycolipids 204-214 CD1c molecule Homo sapiens 15-18 11722638-3 2001 Most models of CD1-restricted T cells function in infectious, neoplastic, or autoimmune diseases and are based on the premise that CD1-restricted T-cell responses are initiated by alterations in cellular glycolipid content. Glycolipids 204-214 CD1c molecule Homo sapiens 131-134 11580851-6 2001 The primary function of CD1 molecules is to present lipid and glycolipid antigens to T cells. Glycolipids 62-72 CD1c molecule Homo sapiens 24-27 11693433-4 2001 Glycolipids insert their hydrophobic lipid tails in two pockets below the antigen-binding groove and position their hydrophilic heads on the external part of CD1 molecules. Glycolipids 0-11 CD1c molecule Homo sapiens 158-161 11145856-2 2000 Human group 1 CD1 molecules (CD1a, CD1b, CD1c) are expressed mainly on professional antigen-presenting cells, and mediate presentation of microbial lipid and glycolipid antigens to T cells. Glycolipids 158-168 CD1c molecule Homo sapiens 41-45 11154926-1 2001 Recently, different members of the CD1 family of MHC-like molecules have been shown to sample different intracellular compartments to present lipid and glycolipid antigens to T cells. Glycolipids 152-162 CD1c molecule Homo sapiens 35-38 11145858-1 2000 The MHC class I-like, non-polymorphic CD1 molecules represent a novel system for the presentation of glycolipid antigens to T lymphocytes. Glycolipids 101-111 CD1c molecule Homo sapiens 38-41 11256748-4 2000 Structural and biochemical analyses demonstrate that antigens presented by CD1 are nonpeptide lipid or glycolipid structures, including examples found in the cell walls of pathogenic mycobacteria. Glycolipids 103-113 CD1c molecule Homo sapiens 75-78 10873422-4 2000 The most surprising finding of the CD1 antigen-presenting system is that the antigens presented by CD1 are not peptides, but rather lipid and glycolipid in nature. Glycolipids 142-152 CD1c molecule Homo sapiens 35-38 10873422-4 2000 The most surprising finding of the CD1 antigen-presenting system is that the antigens presented by CD1 are not peptides, but rather lipid and glycolipid in nature. Glycolipids 142-152 CD1c molecule Homo sapiens 99-102 10779786-1 2000 Both the CD4-CD8- (double negative) and CD4-CD8+ T cell lineages have been shown to contain T cells which recognize microbial lipid and glycolipid Ags in the context of human CD1 molecules. Glycolipids 136-146 CD1c molecule Homo sapiens 175-178 9846364-1 1998 Human CD1 molecules bind and display or present lipid and glycolipid antigens from mycobacteria for recognition by T cells. Glycolipids 58-68 CD1c molecule Homo sapiens 6-9 10631954-2 1999 All four of the known human CD1 proteins (CD1a, CD1b, CD1c and CD1d) as well as murine CD1d have now been shown to mediate T-cell recognition of lipid or glycolipid antigens. Glycolipids 154-164 CD1c molecule Homo sapiens 54-58 10358761-0 1999 The CD1 system: antigen-presenting molecules for T cell recognition of lipids and glycolipids. Glycolipids 82-93 CD1c molecule Homo sapiens 4-7 10358761-4 1999 Identification of naturally occurring antigens presented by CD1 has revealed the surprising finding that these are predominantly a variety of foreign lipids and glycolipids, including several found prominently in the cell walls and membranes of pathogenic mycobacteria. Glycolipids 161-172 CD1c molecule Homo sapiens 60-63 10358761-5 1999 Structural, biochemical, and biophysical studies support the view that CD1 proteins bind the hydrophobic alkyl portions of these antigens directly and position the polar or hydrophilic head groups of bound lipids and glycolipids for highly specific interactions with T cell antigen receptors. Glycolipids 217-228 CD1c molecule Homo sapiens 71-74 9987600-2 1999 In contrast to MHC-encoded antigen-presenting molecules, CD1 binds and presents lipid and glycolipid antigens for specific recognition by T cell antigen receptors. Glycolipids 90-100 CD1c molecule Homo sapiens 57-60 10375559-0 1999 CD1-mediated immune responses to glycolipids. Glycolipids 33-44 CD1c molecule Homo sapiens 0-3 9782129-4 1998 Mouse or human CD1 molecules can present the glycolipid alpha-galactosylceramide (alpha-GalCer) to NK T cells from either species. Glycolipids 45-55 CD1c molecule Homo sapiens 15-18 9576005-3 1998 Unlike the MHC molecules, which bind short peptides in their antigen-binding groove for presentation to either CD4+ or CD8+ T cells bearing alpha beta T cell receptors, the CD1 molecules appear to accommodate lipid and glycolipid antigens in their hydrophobic cavity for presentation to a wide variety of T cells, including double-negative alpha beta and gamma delta T cells and CD8+ alpha beta T cells. Glycolipids 219-229 CD1c molecule Homo sapiens 173-176