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Search results 101 to 125 out of 125 for Gp2

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0.016s

Type

Details

Score

Publication

21866101 | J:219073

First Author:	Côté M
Year:	2011
Journal:	Nature
Title:	Small molecule inhibitors reveal Niemann-Pick C1 is essential for Ebola virus infection.
Volume:	477
Issue:	7364
Pages:	344-8

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Publication

23752178 | J:212588

First Author:	Chandrakesan P
Year:	2014
Journal:	Oncogene
Title:	Utility of a bacterial infection model to study epithelial-mesenchymal transition, mesenchymal-epithelial transition or tumorigenesis.
Volume:	33
Issue:	20
Pages:	2639-54

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Protein Domain

IPR042635 | SREC1/2

Type:

Family

Description:

The class F scavenger receptors (SCARFs or SRECs) have two isoforms, SCARF1/SREC-I and SCARF2/SREC-II. Similar to SREC-I, SREC-II contains multiple epidermal growth factor-like repeats in its extracellular domain. However, in contrast to SREC-I, SREC-II had little activity to internalize modified low density lipoproteins (LDL). SREC-II and SREC-I display strong heterophilic trans-interaction through the extracellular domains []. They are expressed in a specific temporal and spatial pattern during epidermal development [].Mutations in the SCARF2 gene cause Van den Ende-Gupta syndrome (VDEGS), a syndrome characterised by craniofacial and skeletal abnormalities []. The class F scavenger receptor 1 (SCARF1/SREC-I) contains epidermal growth factor (EGF)-like repeats in its extracellular domain, followed by a long C-terminal cytoplasmic tail composed of serine and proline-rich regions. SCARF1 is an endocytic receptor for acetylated low density lipoprotein, HSP70, HSP90, calreticulin, gp96, and GP2 [, , , , ]. Dendritic cells (DCs), macrophages and endothelial cells use SCARF1 to recognize and engulf apoptotic cells via the complement component C1q; this mediates apoptotic cells clearance, antigen clearance and prevents autoimmunity [].

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Publication

12154095 | J:79485

First Author:	Ishii J
Year:	2002
Journal:	J Biol Chem
Title:	SREC-II, a new member of the scavenger receptor type F family, trans-interacts with SREC-I through its extracellular domain.
Volume:	277
Issue:	42
Pages:	39696-702

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Protein

A0A338P7B0

Organism:	Mus musculus/domesticus
Length:	141
Fragment?:	true

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Publication

8437211 | -

First Author:	Will C
Year:	1993
Journal:	J Virol
Title:	Marburg virus gene 4 encodes the virion membrane protein, a type I transmembrane glycoprotein.
Volume:	67
Issue:	3
Pages:	1203-10

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Publication

17005688 | -

First Author:	Shimojima M
Year:	2006
Journal:	J Virol
Title:	Tyro3 family-mediated cell entry of Ebola and Marburg viruses.
Volume:	80
Issue:	20
Pages:	10109-16

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Publication

16775318 | -

First Author:	Marzi A
Year:	2006
Journal:	J Virol
Title:	The signal peptide of the ebolavirus glycoprotein influences interaction with the cellular lectins DC-SIGN and DC-SIGNR.
Volume:	80
Issue:	13
Pages:	6305-17

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Publication

11152533 | -

First Author:	Ito H
Year:	2001
Journal:	J Virol
Title:	Ebola virus glycoprotein: proteolytic processing, acylation, cell tropism, and detection of neutralizing antibodies.
Volume:	75
Issue:	3
Pages:	1576-80

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Publication

12482654 | -

First Author:	Sui J
Year:	2002
Journal:	Virology
Title:	Evidence against Ebola virus sGP binding to human neutrophils by a specific receptor.
Volume:	303
Issue:	1
Pages:	9-14

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Publication

16051836 | -

First Author:	Wahl-Jensen VM
Year:	2005
Journal:	J Virol
Title:	Effects of Ebola virus glycoproteins on endothelial cell activation and barrier function.
Volume:	79
Issue:	16
Pages:	10442-50

•

Publication

15681442 | -

First Author:	Wahl-Jensen V
Year:	2005
Journal:	J Virol
Title:	Role of Ebola virus secreted glycoproteins and virus-like particles in activation of human macrophages.
Volume:	79
Issue:	4
Pages:	2413-9

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Publication

15922673 | J:99529

First Author:	Hwang M
Year:	2005
Journal:	Gene Expr Patterns
Title:	The temporal and spatial expression of the novel Ca++-binding proteins, Scarf and Scarf2, during development and epidermal differentiation.
Volume:	5
Issue:	6
Pages:	801-8

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Publication

20887961 | -

First Author:	Anastasio N
Year:	2010
Journal:	Am J Hum Genet
Title:	Mutations in SCARF2 are responsible for Van Den Ende-Gupta syndrome.
Volume:	87
Issue:	4
Pages:	553-9

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Protein Domain

IPR014625 | GPC_FiloV

Type:

Family

Description:

Proteins in this family include the envelope glycoprotein and the pre-small/secreted glycoprotein from Filoviridae []. The envelope glycoprotein can be cleaved into 3 chains: GP1, GP2 and GP2-delta.GP1 is responsible for binding to the receptor(s), such as CD209 and CLEC4M, on target cells. These interactions not only facilitate virus cell entry, but also allow capture of viral particles by dendritic cells (DCs) and subsequent transmission to susceptible cells without DCs infection (trans infection) [].GP2 acts as a class I viral fusion protein. It is responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane []. GP1,2 peplomers mediates endothelial cell activation and decreases endothelial barrier function. It mediates activation of primary macrophages. At terminal stages of the viral infection, when its expression is high, GP1,2 down-modulates the expression of various host cell surface molecules that are essential for immune surveillance and cell adhesion [].GP2delta is part of the complex GP1,2delta released by host ADAM17 metalloprotease. This secreted complex may play a role in the pathogenesis of the virus by efficiently blocking the neutralizing antibodies that would otherwise neutralize the virus surface glycoproteins GP1,2. Might therefore contribute to the lack of inflammatory reaction seen during infection in spite the of extensive necrosis and massive virus production. GP1,2delta does not seem to be involved in activation of primary macrophage [].pre-small/secreted glycoprotein sGP seems to possess an anti-inflammatory activity as it can reverse the barrier-decreasing effects of TNF alpha. It might therefore contribute to the lack of inflammatory reaction seen during infection in spite the of extensive necrosis and massive virus production. It does not seem to be involved in activation of primary macrophages. It does not seem to interact specifically with neutrophils [, , , ].

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Protein

Q5ND28

Organism:	Mus musculus/domesticus
Length:	820
Fragment?:	false

•

Protein

B7ZC28

Organism:	Mus musculus/domesticus
Length:	478
Fragment?:	false

•

Protein

Q68EF1

Organism:	Mus musculus/domesticus
Length:	474
Fragment?:	false

•

Protein

P59222

Organism:	Mus musculus/domesticus
Length:	833
Fragment?:	false

•

Protein

A0A338P7B2

Organism:	Mus musculus/domesticus
Length:	566
Fragment?:	false

•

Protein

Q58A84

Organism:	Mus musculus/domesticus
Length:	833
Fragment?:	false

•

Publication

22771211 | -

First Author:	Roy A
Year:	2012
Journal:	Structure
Title:	Small terminase couples viral DNA binding to genome-packaging ATPase activity.
Volume:	20
Issue:	8
Pages:	1403-13

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Publication

16141072 | J:99680

First Author:	Carninci P
Year:	2005
Journal:	Science
Title:	The transcriptional landscape of the mammalian genome.
Volume:	309
Issue:	5740
Pages:	1559-63

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Publication

21183079 | J:292518

First Author:	Huttlin EL
Year:	2010
Journal:	Cell
Title:	A tissue-specific atlas of mouse protein phosphorylation and expression.
Volume:	143
Issue:	7
Pages:	1174-89

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Publication

19468303 | -

First Author:	Church DM
Year:	2009
Journal:	PLoS Biol
Title:	Lineage-specific biology revealed by a finished genome assembly of the mouse.
Volume:	7
Issue:	5
Pages:	e1000112

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Search results 101 to 125 out of 125 for Gp2

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