Ignet

Gene Information

Gene symbol: CLEC4M

Gene name: C-type lectin domain family 4, member M

HGNC ID: 13523

Synonyms: HP10347, DC-SIGNR, LSIGN, DCSIGNR, DC-SIGN2

Related Genes

#	Gene Symbol	Number of hits
1	CD209	1 hits
2	CD81	1 hits
3	ERVWE1	1 hits
4	ICAM3	1 hits
5	LDLR	1 hits
6	MAPK1	1 hits
7	MAPK3	1 hits
8	MRC1	1 hits
9	OCLN	1 hits
10	SCARB1	1 hits

Related Sentences

#	PMID	Sentence
1	12223058	The role of DC-SIGN and DC-SIGNR in HIV and Ebola virus infection: can potential therapeutics block virus transmission and dissemination?
2	12223058	DC-SIGN and a related molecule, termed DC-SIGNR, also enhance infection by Ebola virus.
3	12223058	The expression of these lectins on early targets of Ebola virus infection, like liver endothelial cells and alveolar macrophages, suggests an important role for DC-SIGN and DC-SIGNR in the establishment of Ebola infection.
4	12223058	This article reviews the interaction of DC-SIGN and DC-SIGNR with HIV and Ebola, discusses the mechanism of DC-SIGN-mediated viral transmission and examines how this process could be inhibited by potential therapeutics.
5	12223058	The role of DC-SIGN and DC-SIGNR in HIV and Ebola virus infection: can potential therapeutics block virus transmission and dissemination?
6	12223058	DC-SIGN and a related molecule, termed DC-SIGNR, also enhance infection by Ebola virus.
7	12223058	The expression of these lectins on early targets of Ebola virus infection, like liver endothelial cells and alveolar macrophages, suggests an important role for DC-SIGN and DC-SIGNR in the establishment of Ebola infection.
8	12223058	This article reviews the interaction of DC-SIGN and DC-SIGNR with HIV and Ebola, discusses the mechanism of DC-SIGN-mediated viral transmission and examines how this process could be inhibited by potential therapeutics.
9	12223058	The role of DC-SIGN and DC-SIGNR in HIV and Ebola virus infection: can potential therapeutics block virus transmission and dissemination?
10	12223058	DC-SIGN and a related molecule, termed DC-SIGNR, also enhance infection by Ebola virus.
11	12223058	The expression of these lectins on early targets of Ebola virus infection, like liver endothelial cells and alveolar macrophages, suggests an important role for DC-SIGN and DC-SIGNR in the establishment of Ebola infection.
12	12223058	This article reviews the interaction of DC-SIGN and DC-SIGNR with HIV and Ebola, discusses the mechanism of DC-SIGN-mediated viral transmission and examines how this process could be inhibited by potential therapeutics.
13	12223058	The role of DC-SIGN and DC-SIGNR in HIV and Ebola virus infection: can potential therapeutics block virus transmission and dissemination?
14	12223058	DC-SIGN and a related molecule, termed DC-SIGNR, also enhance infection by Ebola virus.
15	12223058	The expression of these lectins on early targets of Ebola virus infection, like liver endothelial cells and alveolar macrophages, suggests an important role for DC-SIGN and DC-SIGNR in the establishment of Ebola infection.
16	12223058	This article reviews the interaction of DC-SIGN and DC-SIGNR with HIV and Ebola, discusses the mechanism of DC-SIGN-mediated viral transmission and examines how this process could be inhibited by potential therapeutics.
17	15481146	Identification of the mycobacterial carbohydrate structure that binds the C-type lectins DC-SIGN, L-SIGN and SIGNR1.
18	15481146	Recent studies have demonstrated that M. tuberculosis targets the DC-specific C-type lectin DC-SIGN to inhibit the immuno-stimulatory function of DC through the interaction of the mycobacterial mannosylated lipoarabinomannan (ManLAM) to DC-SIGN, which prevents DC maturation and induces the immuno-suppressive cytokine IL-10.
19	15481146	Moreover, we demonstrate that the human and murine DC-SIGN homologue L-SIGN and SIGNR1, respectively, also interact with mycobacteria through ManLAM.
20	15481146	Identification of the mycobacterial carbohydrate structure that binds the C-type lectins DC-SIGN, L-SIGN and SIGNR1.
21	15481146	Recent studies have demonstrated that M. tuberculosis targets the DC-specific C-type lectin DC-SIGN to inhibit the immuno-stimulatory function of DC through the interaction of the mycobacterial mannosylated lipoarabinomannan (ManLAM) to DC-SIGN, which prevents DC maturation and induces the immuno-suppressive cytokine IL-10.
22	15481146	Moreover, we demonstrate that the human and murine DC-SIGN homologue L-SIGN and SIGNR1, respectively, also interact with mycobacteria through ManLAM.
23	16164025	Role of the C-type lectins DC-SIGN and L-SIGN in Leishmania interaction with host phagocytes.
24	16164025	We have also found that the DC-SIGN-related molecule L-SIGN, specifically expressed in lymph node and liver sinusoidal endothelial cells, acts as a receptor for L. infantum, the parasite responsible for visceral leishmaniasis, but does not recognize L. pifanoi, which causes the cutaneous form of the disease.
25	16164025	Therefore, DC-SIGN and L-SIGN differ in their ability to interact with Leishmania species responsible for either visceral or cutaneous leishmaniasis.
26	16164025	Role of the C-type lectins DC-SIGN and L-SIGN in Leishmania interaction with host phagocytes.
27	16164025	We have also found that the DC-SIGN-related molecule L-SIGN, specifically expressed in lymph node and liver sinusoidal endothelial cells, acts as a receptor for L. infantum, the parasite responsible for visceral leishmaniasis, but does not recognize L. pifanoi, which causes the cutaneous form of the disease.
28	16164025	Therefore, DC-SIGN and L-SIGN differ in their ability to interact with Leishmania species responsible for either visceral or cutaneous leishmaniasis.
29	16164025	Role of the C-type lectins DC-SIGN and L-SIGN in Leishmania interaction with host phagocytes.
30	16164025	We have also found that the DC-SIGN-related molecule L-SIGN, specifically expressed in lymph node and liver sinusoidal endothelial cells, acts as a receptor for L. infantum, the parasite responsible for visceral leishmaniasis, but does not recognize L. pifanoi, which causes the cutaneous form of the disease.
31	16164025	Therefore, DC-SIGN and L-SIGN differ in their ability to interact with Leishmania species responsible for either visceral or cutaneous leishmaniasis.
32	22090124	Respiratory syncytial virus glycoprotein G interacts with DC-SIGN and L-SIGN to activate ERK1 and ERK2.
33	22090124	Therefore, we asked whether RSV infection involves DC-SIGN (CD209) or its isoform L-SIGN (CD299) (DC-SIGN/R).
34	22090124	RSV G interaction with DC- or L-SIGN was shown to stimulate ERK1 and ERK2 phosphorylation, with statistically significant increases relative to mock-infected cells.
35	22090124	Neutralization of DC- and L-SIGN reduced ERK1/2 phosphorylation.
36	22090124	Respiratory syncytial virus glycoprotein G interacts with DC-SIGN and L-SIGN to activate ERK1 and ERK2.
37	22090124	Therefore, we asked whether RSV infection involves DC-SIGN (CD209) or its isoform L-SIGN (CD299) (DC-SIGN/R).
38	22090124	RSV G interaction with DC- or L-SIGN was shown to stimulate ERK1 and ERK2 phosphorylation, with statistically significant increases relative to mock-infected cells.
39	22090124	Neutralization of DC- and L-SIGN reduced ERK1/2 phosphorylation.
40	22090124	Respiratory syncytial virus glycoprotein G interacts with DC-SIGN and L-SIGN to activate ERK1 and ERK2.
41	22090124	Therefore, we asked whether RSV infection involves DC-SIGN (CD209) or its isoform L-SIGN (CD299) (DC-SIGN/R).
42	22090124	RSV G interaction with DC- or L-SIGN was shown to stimulate ERK1 and ERK2 phosphorylation, with statistically significant increases relative to mock-infected cells.
43	22090124	Neutralization of DC- and L-SIGN reduced ERK1/2 phosphorylation.
44	22090124	Respiratory syncytial virus glycoprotein G interacts with DC-SIGN and L-SIGN to activate ERK1 and ERK2.
45	22090124	Therefore, we asked whether RSV infection involves DC-SIGN (CD209) or its isoform L-SIGN (CD299) (DC-SIGN/R).
46	22090124	RSV G interaction with DC- or L-SIGN was shown to stimulate ERK1 and ERK2 phosphorylation, with statistically significant increases relative to mock-infected cells.
47	22090124	Neutralization of DC- and L-SIGN reduced ERK1/2 phosphorylation.
48	25224349	Dextran-binding receptors in humans include the DC-SIGN (dendritic cell-specific intercellular adhesion molecule 3-grabbing nonintegrin) family receptors: DC-SIGN (CD209) and L-SIGN (the liver and lymphatic endothelium homologue of DC-SIGN), the mannose receptor (CD206), and langerin.
49	25997338	Hepatitis c virus (HCV) infection has become one of the global public health problem,while there is no vaccine to prevent HCV infection, the so-called "cocktail" therapy that use a combination of drugs targeting multiple steps in the HCV infection cycle could achieve better curative effect. the process of HCV entering into host cell is the important step of drug intervention, in which HCV envelope protein El and E2, Host cell factors including Heparan sulfate(HS), CD81, scavenger receptor class B type I (SR-BI), Occludin (OCLD), Claudin (CLDN), low densitity lipoprotein receptor (LDLR), dendritic cell-specific ICAM-3-grabbing nonintegrin (DC-SIGN), Liver/lymph node specific ICAM-3-grabbing integrin(L-SIGN), trans- ferrin receptor 1 (TfR1) and so on play a important role.