Ly96 Antibody

1. We conclude that MD2 is a significant contributor in the Ang II-induced kidney inflammatory injury in chronic renal diseases. PMID:28322341
2. Blockade of MD2 prevents obesity-induced inflammation and nephropathy. PMID:28767204
3. MD2 is essential to obesity-related cardiac hypertrophy through activating JNK/ERK and NF-kappaB-dependent cardiac inflammatory pathways. Targeting MD2 would be a therapeutic approach to prevent obesity-induced cardiac injury and remodeling. PMID:28965884
4. RTFs contribute to the regulation of LPS-induced inflammatory response in RAW264.7 cells through TLR4/MD-2 mediated NF-kappaB and JNK pathway. It PMID:27235587
5. This study provides evidence that MD2 plays a key role in the pathogenesis of retinal I/R damage. PMID:29111459
6. Data suggest that C4bp prevents interaction between Tlr4/MD-2 and its ligand; C4bp does not appear to interact with Tlr3; C4bp binds to macrophage surface Tlr4 and inhibits Tlr/Tlr ligand interaction, thereby inhibiting Tlr4 activation. (C4bp = complement component 4 binding protein; Tlr = toll-like receptor; MD-2 = myeloid differentiation protein-2) PMID:28542817
7. MD2 plays an important role in induction of allergic sensitization to cat dander and common pollens relevant to human allergic diseases. PMID:26586036
8. Oxidative stress in retinal ischemia-reperfusion injury activates TLR4 signaling via MD2. PMID:28063877
9. Neoseptin-3 and lipid A form dissimilar molecular contacts to achieve receptor activation; hence strong TLR4/MD-2 agonists need not mimic LPS PMID:26831104
10. Here we demonstrate that cholesterol binds to myeloid differentiation-2 (MD-2), a TLR4 ancillary molecule. PMID:26806306
11. MD-2 is a critical regulator of the establishment of allergic airway sensitization to HDM in mice. Serum MD-2 may represent a potential biomarker for the amplification of allergic sensitization and allergic inflammation. PMID:26344079
12. Data show that myeloid differentiation factor 2 (MD-2) binds specifically to disulfide isoform of box protein 1, high mobility group (HMGB1) to facilitate toll-like receptor 4 (TLR4)-dependent signaling. PMID:25559892
13. Carbon monoxide treatment reduces the expression of the TLR4/MD2 complex on the surface of myeloid cells, which renders them resistant to lipopolysaccharide priming in vitro, as well as in vivo in a model of endotoxic shock. PMID:25179131
14. Mechanistically, engagement of MD-2 by PTX3-opsonized Aspergillus conidia activated the TLR4/Toll/IL-1R domain-containing adapter inducing IFN-beta-dependent signaling pathway converging on IL-10. PMID:25049357
15. SAA3 directly binds MD-2 and activates the MyD88-dependent TLR4/MD-2 pathway. PMID:23858030
16. Monophosphoryl lipid A is unable to efficiently form TLR4/MD-2 heterotetramers, but it still needs heterotetramer formation for the full extent of signaling it is able to achieve. PMID:23638128
17. Data show that rifampin binds to myeloid differentiation protein 2 (MD-2), the key coreceptor for innate immune TLR4. PMID:23568774
18. Gb4 is an endogenous ligand for TLR4-MD-2 and is capable of attenuating LPS toxicity, indicating the possibility for its therapeutic application in endotoxin shock. PMID:23471986
19. Data provide structural evidence of the agonistic property of lipid IVa on TLR4/MD-2 and deepen understanding of the ligand binding and dimerization mechanism by the structurally diverse Lipopolysaccharide (LPS) variants. PMID:22532668
20. GL and ILG modulate the TLR4/MD-2 complex at the receptor level, leading to suppress LPS-induced activation of signaling cascades and cytokine production PMID:22422925
21. Data show that morphine binds to an accessory protein of Toll-like receptor 4 (TLR4), myeloid differentiation protein 2 (MD-2), thereby inducing TLR4 oligomerization and triggering proinflammation. PMID:22474354
22. Data show that LPS priming of tolerant FLDCs inhibited the up-regulation of TLR4/MD-2 expression. PMID:21802073
23. According to our murine TLR4/MD-2-activation model, the two phosphates on lipid A were predicted to interact extensively with the two positively charged patches on mouse TLR4activation PMID:21865549
24. Demonstrate a novel, critical role for MD-2 and TLR4 through NADPH activation in liver steatosis, and fibrosis in a NASH model in mice. PMID:21233280
25. species-specific activation of lipid IV(A) PMID:20592019
26. Neutralizing toll-like receptor 4/myeloid differentiation protein-2 is highly efficacious in protecting against bacterial infection-induced toxemia. PMID:17947685
27. MD-2-mediated ionic interactions between lipid A and TLR4 are essential for receptor activation PMID:20018893
28. MD-2 in complex with toll-like receptor 4 mediates signal transduction induced by the amino acid-containing bacterial lipid, flavolipin. PMID:11884465
29. MD-2 is essential for correct intracellular distribution and LPS-recognition of TLR4. PMID:12055629
30. By alanine-scanning mutagenesis of MD-2, important amino acid residues have been identified that confer lipopolysaccharide and taxol responsiveness on TLR4 and enable formation of cell surface TLR4-MD-2 complex recognized by specific monoclonal antibody. PMID:12496426
31. TLR4 and its partner molecule MD-2 may play an important role in Kupffer cell activation and ischemia-reperfusion injury. PMID:15334694
32. Results show that the N-terminal region of toll-like receptor 4 is essential for association with MD-2, which is required for the cell surface expression and hence the responsiveness to lipopolysaccharide. PMID:15337750
33. Collectively, MD-2 is essential for the recognition of LPS by TLR4 but not for that of PGN by TLR2 of mast cells. PMID:15369778
34. Results indicate that amino acid residues 57, 61, and 122 of mouse MD-2 are critical to determine the agonist-antagonist activity of lipid IVa and suggest that these amino acid residues may be involved in the discrimination of lipid A structure. PMID:16407172
35. agonistic mAb to Toll-Like Receptor 4 (TLR4)/MD-2 protected mice from lipopolysaccharide/d-galactosamine-induced acute lethal hepatitis by delivering a protective signal activating NF-kappaB through TLR4/MD-2 PMID:16547261
36. This study shows regulatory roles for MD-2 in initiating and terminating ligand-induced TLR4 oligomerization. PMID:16670331
37. a unique complex of TLR4, MD-2, and CD44 recognizes hyaluronan in signaling tissue injury PMID:17400552
38. Data show that lipopolysaccharides act through both MyD88-dependent and -independent TLR4/MD2 signaling pathways to directly inhibit GHR gene expression. PMID:17601656
39. Based on structural analysis and mutagenesis experiments on MD-2 and TLR4, we propose a model of TLR4-MD-2 dimerization induced by LPS. PMID:17803912
40. The lower expression of the CD14 and TLR-4/MD-2 receptors may be partly responsible for the immunodeficiency observed in the malnourished mice. PMID:17950615
41. MD-2 is a newly recognized type II acute-phase reactant, an opsonin for Gram-negative bacteria, and a cofactor essential for the activation of TLR4-expressing cells. PMID:18056837
42. role of the TLR4/MD-2 signaling axis in bacterial recognition by phagocytes PMID:18203953
43. Data compare the inflammatory potency of two types of Neisseria meningitidis endotoxins in lungs: wild type (hexaacylated, LOS(wt)) and mutant type (pentaacylated, LOS(msbB)), and describe the importance of MD-2 in endotoxin responses in lungs in vivo. PMID:18203970
44. The species-specific difference between human and murine MD-2 activation of TLR4 by PTX can be explained by alterations of surface charge distribution (i.e. electrostatic potential), binding pocket size, and the locus of PTX binding within the MD-2 pocket PMID:18650420
45. Myeloid differentiation protein-2 has an important role in the CD14-independent LPS-mediated cascade of neutrophil influx PMID:18988922
46. the leucine at position 815 is required for the normal maturation of TLR4 and for formation of the TLR4.MD-2 complex. PMID:19064998
47. These findings reveal novel roles of lysines 122, 125, and 58 in human MD-2 that contribute to the functional differences between human and murine MD-2 and, potentially, to differences in the sensitivity of humans and mice to endotoxin. PMID:19783674

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UNIGENE: Mm.116844

KEGG: mmu:17087

STRING: 10090.ENSMUSP00000026881