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Search results 2201 to 2300 out of 4306 for C3

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Type Details Score
Publication
26903652 | J:230998
First Author: Park K
Year: 2016
Journal: Proc Natl Acad Sci U S A
Title: ER stress stimulates production of the key antimicrobial peptide, cathelicidin, by forming a previously unidentified intracellular S1P signaling complex.
Volume: 113
Issue: 10
Pages: E1334-42
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Publication
29787576 | J:263557
First Author: Riento K
Year: 2018
Journal: PLoS One
Title: Flotillin proteins recruit sphingosine to membranes and maintain cellular sphingosine-1-phosphate levels.
Volume: 13
Issue: 5
Pages: e0197401
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Publication
21331079 | J:203103
First Author: Hagen N
Year: 2011
Journal: Cell Death Differ
Title: Sphingosine-1-phosphate links glycosphingolipid metabolism to neurodegeneration via a calpain-mediated mechanism.
Volume: 18
Issue: 8
Pages: 1356-65
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Publication
36396932 | J:337626
First Author: Yuan F
Year: 2022
Journal: Cell Death Dis
Title: SphK-produced S1P in somatic cells is indispensable for LH-EGFR signaling-induced mouse oocyte maturation.
Volume: 13
Issue: 11
Pages: 963
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Publication
15746241 | J:347394
First Author: Isotani A
Year: 2005
Journal: Proc Natl Acad Sci U S A
Title: Genomic imprinting of XX spermatogonia and XX oocytes recovered from XX<-->XY chimeric testes.
Volume: 102
Issue: 11
Pages: 4039-44
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Publication
12538695 | J:118712
First Author: Zou X
Year: 2003
Journal: J Immunol
Title: Block in development at the pre-B-II to immature B cell stage in mice without Ig kappa and Ig lambda light chain.
Volume: 170
Issue: 3
Pages: 1354-61
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Publication
1660837 | J:122541
First Author: Niwa H
Year: 1991
Journal: Gene
Title: Efficient selection for high-expression transfectants with a novel eukaryotic vector.
Volume: 108
Issue: 2
Pages: 193-9
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Publication
21487305 | J:237901
First Author: Verhamme C
Year: 2011
Journal: J Neuropathol Exp Neurol
Title: Myelin and axon pathology in a long-term study of PMP22-overexpressing mice.
Volume: 70
Issue: 5
Pages: 386-98
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Publication
35501630 | J:338996
First Author: Bai Y
Year: 2022
Journal: Mol Neurobiol
Title: Treatment with IFB-088 Improves Neuropathy in CMT1A and CMT1B Mice.
Volume: 59
Issue: 7
Pages: 4159-4178
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Genotype
Genotype
Symbol: Tsix/? Tg(CAG-EGFP)50Osb/? Gt(ROSA)26Sor/Gt(ROSA)26Sor
Background: involves: 129P2/OlaHsd * 129S4/SvJae * C3H/HeSlc * C57BL/6J * C57BL/6Slc
Zygosity: cx
Has Mutant Allele: true
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Genotype
Genotype
Symbol: Tsix/Tsix Tg(CAG-EGFP)50Osb/? Gt(ROSA)26Sor/Gt(ROSA)26Sor
Background: involves: 129P2/OlaHsd * 129S4/SvJae * C3H/HeSlc * C57BL/6J * C57BL/6Slc
Zygosity: cx
Has Mutant Allele: true
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Genotype
Genotype
Symbol: Tsix/Tsix<+> Tg(CAG-EGFP)50Osb/? Gt(ROSA)26Sor/Gt(ROSA)26Sor
Background: involves: 129P2/OlaHsd * 129S4/SvJae * C3H/HeSlc * C57BL/6J * C57BL/6Slc
Zygosity: cx
Has Mutant Allele: true
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Genotype
Genotype
Symbol: C3/C3 Dysf/Dysf
Background: B6.129-Dysf C3
Zygosity: cx
Has Mutant Allele: true
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Genotype
Genotype
Symbol: C3/C3 Cd59a/Cd59a
Background: B6.129-Cd59a C3
Zygosity: cx
Has Mutant Allele: true
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Genotype
Genotype
Symbol: Tcra/Tcra Tg(Mx1-cre)1Cgn/?
Background: involves: C57BL/6 * CBA
Zygosity: cn
Has Mutant Allele: true
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Publication
21258343 | J:170600
First Author: Rooryck C
Year: 2011
Journal: Nat Genet
Title: Mutations in lectin complement pathway genes COLEC11 and MASP1 cause 3MC syndrome.
Volume: 43
Issue: 3
Pages: 197-203
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Publication
15654079 | -
First Author: Birtley JR
Year: 2005
Journal: J Biol Chem
Title: Crystal structure of foot-and-mouth disease virus 3C protease. New insights into catalytic mechanism and cleavage specificity.
Volume: 280
Issue: 12
Pages: 11520-7
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Publication
19144641 | -
First Author: Lee CC
Year: 2009
Journal: J Biol Chem
Title: Structural basis of inhibition specificities of 3C and 3C-like proteases by zinc-coordinating and peptidomimetic compounds.
Volume: 284
Issue: 12
Pages: 7646-55
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Publication
21835784 | -
First Author: Costenaro L
Year: 2011
Journal: J Virol
Title: Structural basis for antiviral inhibition of the main protease, 3C, from human enterovirus 93.
Volume: 85
Issue: 20
Pages: 10764-73
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Publication
21795339 | -
First Author: Lu G
Year: 2011
Journal: J Virol
Title: Enterovirus 71 and coxsackievirus A16 3C proteases: binding to rupintrivir and their substrates and anti-hand, foot, and mouth disease virus drug design.
Volume: 85
Issue: 19
Pages: 10319-31
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Publication
18293057 | -
First Author: Le Gall O
Year: 2008
Journal: Arch Virol
Title: Picornavirales, a proposed order of positive-sense single-stranded RNA viruses with a pseudo-T = 3 virion architecture.
Volume: 153
Issue: 4
Pages: 715-27
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Publication
22534091 | -
First Author: Ye S
Year: 2012
Journal: Virology
Title: Identification and characterization of Iflavirus 3C-like protease processing activities.
Volume: 428
Issue: 2
Pages: 136-45
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Publication
2775751 | -
First Author: Birktoft JJ
Year: 1989
Journal: Biochemistry
Title: Refined crystal structure of cytoplasmic malate dehydrogenase at 2.5-A resolution.
Volume: 28
Issue: 14
Pages: 6065-81
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Publication
12644669 | -
First Author: Knappe S
Year: 2003
Journal: Plant Physiol
Title: Analysis of the plastidic phosphate translocator gene family in Arabidopsis and identification of new phosphate translocator-homologous transporters, classified by their putative substrate-binding site.
Volume: 131
Issue: 3
Pages: 1178-90
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Publication
12770764 | -
First Author: Martinez-Duncker I
Year: 2003
Journal: Biochimie
Title: The nucleotide-sugar transporter family: a phylogenetic approach.
Volume: 85
Issue: 3-4
Pages: 245-60
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Publication
11289511 | -
First Author: Windhövel A
Year: 2001
Journal: Plant Mol Biol
Title: Characterization of a novel class of plant homeodomain proteins that bind to the C4 phosphoenolpyruvate carboxylase gene of Flaveria trinervia.
Volume: 45
Issue: 2
Pages: 201-14
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Publication
9032387 | -
First Author: Suarez DL
Year: 1997
Journal: J Virol
Title: Size variation within the second hypervariable region of the surface envelope gene of the bovine lentivirus BIV in experimentally and naturally infected cattle.
Volume: 71
Issue: 3
Pages: 2482-6
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Publication
11448023 | -
First Author: Meas S
Year: 2001
Journal: Arch Virol
Title: Phylogenetic relationships of bovine immunodeficiency virus in cattle and buffaloes based on surface envelope gene sequences. Brief report.
Volume: 146
Issue: 5
Pages: 1037-45
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Publication
11695893 | -
First Author: Wei M
Year: 2001
Journal: Biochemistry
Title: Investigation of the role of the domain linkers in separate site catalysis by Clostridium symbiosum pyruvate phosphate dikinase.
Volume: 40
Issue: 45
Pages: 13466-73
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Publication
14684927 | -
First Author: Nakanishi T
Year: 2004
Journal: Acta Crystallogr D Biol Crystallogr
Title: Purification, crystallization and preliminary X-ray diffraction studies on pyruvate phosphate dikinase from maize.
Volume: 60
Issue: Pt 1
Pages: 193-4
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Publication
11950985 | -
First Author: Chastain CJ
Year: 2002
Journal: Plant Physiol
Title: Pyruvate,orthophosphate dikinase in leaves and chloroplasts of C(3) plants undergoes light-/dark-induced reversible phosphorylation.
Volume: 128
Issue: 4
Pages: 1368-78
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Publication
12082105 | -
First Author: Arcus VL
Year: 2002
Journal: J Biol Chem
Title: The Three-dimensional structure of a superantigen-like protein, SET3, from a pathogenicity island of the Staphylococcus aureus genome.
Volume: 277
Issue: 35
Pages: 32274-81
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Publication
15213171 | -
First Author: Al-Shangiti AM
Year: 2004
Journal: Infect Immun
Title: Structural relationships and cellular tropism of staphylococcal superantigen-like proteins.
Volume: 72
Issue: 7
Pages: 4261-70
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Publication
10475605 | -
First Author: Takayama Y
Year: 1999
Journal: Mol Immunol
Title: Gene structure of the P100 serine-protease component of the human Ra-reactive factor.
Volume: 36
Issue: 8
Pages: 505-14
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Publication
15327949 | -
First Author: Sulzenbacher G
Year: 2004
Journal: J Mol Biol
Title: Crystal structure of E.coli alcohol dehydrogenase YqhD: evidence of a covalently modified NADP coenzyme.
Volume: 342
Issue: 2
Pages: 489-502
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Publication
20924577 | -
First Author: Jarboe LR
Year: 2011
Journal: Appl Microbiol Biotechnol
Title: YqhD: a broad-substrate range aldehyde reductase with various applications in production of biorenewable fuels and chemicals.
Volume: 89
Issue: 2
Pages: 249-57
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Publication
19383697 | -
First Author: Liu X
Year: 2009
Journal: Microbiology (Reading)
Title: Two novel metal-independent long-chain alkyl alcohol dehydrogenases from Geobacillus thermodenitrificans NG80-2.
Volume: 155
Issue: Pt 6
Pages: 2078-2085
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Protein Domain
IPR004696 | Tpt_PEP_transl
Type: Family
Description: Functionally characterised members of the 6-8 TMS Triose-phosphate Transporter (TPT) family are derived from the inner envelopemembranes of chloroplasts and non-green plastids of plants. Under normal physiological conditions, chloroplast TPTs mediate a strict antiport of substrates, frequently exchanging an organic three carbon compound phosphate ester for inorganic phosphate (Pi) [, ].Normally, a triose-phosphate, 3-phosphoglycerate, or another phosphorylated C3compound made in the chloroplast during photosynthesis, exits the organelle into thecytoplasm of the plant cell in exchange for Pi. However, experiments with reconstituted translocator in artificial membranes indicate that transport can also occur by a channel-like uniport mechanism with up to 10-fold higher transport rates. Channel opening may be induced by a membrane potential of large magnitude and/or by high substrate concentrations. Non-green plastid and chloroplast carriers, such as those from maize endosperm and root membranes, mediate transport of C3 compounds phosphorylated at carbon atom 2, particularly phosphoenolpyruvate, in exchange for Pi. These are the phosphoenolpyruvate:Pi antiporters (PPT). Glucose-6-P has also been shown to be a substrate of some plastid translocators (GPT). The three types of proteins (TPT, PPT and GPT) are divergent in sequence as well as substrate specificity, but their substrate specificities overlap.TPT paralogues are also present in Saccharomyces cerevisiae, which are functionally uncharacterised.
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Protein Domain
IPR038565 | CLIP_sf
Type: Homologous_superfamily
Description: The CLIP domain is a regulatory domain which controls the proteinase action of various proteins of the trypsin family, e.g. easter and pap2. The domain is restricted to the arthropoda and found in varying copy numbers (from one to five in Drosophila proteins). It is always found N-terminal to the chymotrypsin serine protease domain, which belong to MEROPS peptidase family S1A. The CLIP domain remains linked to the protease domain after cleavage of a conserved residue which retains the protein in zymogen form. It is named CLIP because it can be drawn in the shape of a paper clip. It has many disulphide bonds and highly conserved cysteine residues, and so it folds extensively [, ]. The clip domain adopts an α/β mixed fold consisting of two helices and an antiparallel distorted β-sheet made of four strands. The two helices are antiparallel and are almost perpendicular to the β-sheet. Three disulfide bridges (C1-C5, C2-C4, C3-C6) stabilize the β-sheet, C3 being the only cysteine that is not located on a β-strand. The clip domain is located opposite the activation loop and contacts the C-terminal α-helix of the SP domain []. The CLIP domain is present in silkworm prophenoloxidase-activating enzyme [].
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Protein Domain
IPR024175 | Pept_S1A_C1r/C1S/mannan-bd
Type: Family
Description: These proteins belong to MEROPS peptidase family S1 (chymotrypsin family, clan PA(S)), subfamily S1A.This family contains the mammalian mannan-binding lectin-associated serine proteases 1 and 2 (MASP1 and MASP2) and complement components C1s and C1r. The C1 complex, containing C1q, C1s, and C1r, triggers the classical complement pathway. When C1q interacts with antibody, C1r becomes autocatalytically activated. Activated C1r in turn activates C1s, which then cleaves C2 and C4 in the classical pathway.Mannose-binding lectin (MBL) complexes with MASP1, MASP2, and a smaller alternative splice product of the MASP2 gene. Binding of MBL to carbohydrates on the surface of microorganisms triggers activation of the associated MASPs. Then MASP1 activates C3 and C2, whereas MASP2 activates C4 and C2 []. Based on the fact that the gene structures of MASP1, C1r, and C1s are similar except that C1r and C1s lack introns in the region encoding the trypsin domain, it has been proposed that the MASP proteins evolved earlier than C1r and C1s []. The complement pathway is also involved in development [].These sequences typically contain a signal sequence, followed by a CUB domain, an EGF-like domain (which often is not detected), a second CUB domain, two sushi domains (sometimes only one is detected), and a trypsin domain.
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Protein Domain
IPR010121 | Pyruvate_phosphate_dikinase
Type: Family
Description: Pyruvate phosphate dikinase (PPDK, or pyruvate orthophosphate dikinase) is found in plants, bacteria and archaea. The amino acid sequence identity between bacterial and plant enzymes is high, and they are similar in sequence to other PEP-utilizing enzymes. PPDK catalyses the reversible conversion of ATP and pyruvate to AMP and PEP (phosphoenolpyruvate). In bacteria such as Clostridium symbiosum (Bacteroides symbiosus), PPDK uses Mg2+ and NH4+ ions as cofactors []. The enzyme has three domains: the N- and C-terminal domains each have an active site centre that catalyses a different step in the reaction, and the middle domain has a carrier histidine residue that moves between the two active centres.In plants, PPDK is localised predominantly in chloroplast stroma where it catalyses the rate-limiting step in the C4 photosynthetic pathway, namely the synthesis of PEP, which acts as the primary CO2 acceptor in C4 photosynthesis []. PPDK activity in C4 plants is strictly regulated by light, its activity decreasing in darkness. This response is regulated by phosphorylation and dephosphorylation of the enzyme using ADP; such regulation is not seen in the bacterial form of the enzyme. PPDK is also found in C3 plants, but it is not known to have a photosynthetic role [].
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Protein Domain
IPR022700 | CLIP
Type: Domain
Description: The CLIP domain is a regulatory domain which controls the proteinase action of various proteins of the trypsin family, e.g. easter and pap2. The domain is restricted to the arthropoda and found in varying copy numbers (from one to five in Drosophila proteins). It is always found N-terminal to the chymotrypsin serine protease domain, which belong to MEROPS peptidase family S1A. The CLIP domain remains linked to the protease domain after cleavage of a conserved residue which retains the protein in zymogen form. It is named CLIP because it can be drawn in the shape of a paper clip. It has many disulphide bonds and highly conserved cysteine residues, and so it folds extensively [, ]. The clip domain adopts an α/β mixed fold consisting of two helices and an antiparallel distorted β-sheet made of four strands. The two helices are antiparallel and are almost perpendicular to the β-sheet. Three disulfide bridges (C1-C5, C2-C4, C3-C6) stabilize the β-sheet, C3 being the only cysteine that is not located on a β-strand. The clip domain is located opposite the activation loop and contacts the C-terminal α-helix of the SP domain []. The CLIP domain is present in silkworm prophenoloxidase-activating enzyme [].
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Protein Domain
IPR019742 | MacrogloblnA2_CS
Type: Conserved_site
Description: This entry contains serum complement C3 and C4 precursors and alpha-macrogrobulins. The alpha-macroglobulin (aM) family of proteins includes protease inhibitors [], typified by the human tetrameric a2-macroglobulin (a2M); they belong to the MEROPS proteinase inhibitor family I39, clan IL. These protease inhibitors share several defining properties, which include (i) the ability to inhibit proteases from all catalytic classes, (ii) the presence of a 'bait region' and a thiol ester, (iii) a similar protease inhibitorymechanism and (iv) the inactivation of the inhibitory capacity by reaction of the thiol ester with small primary amines. aM protease inhibitors inhibit by steric hindrance []. The mechanism involves protease cleavage of the bait region, a segment of the aM thatis particularly susceptible to proteolytic cleavage, which initiates a conformational change such that the aM collapses about the protease. In the resulting aM-protease complex, the active site of the protease is sterically shielded, thus substantially decreasing access to protein substrates. Two additional events occur as a consequence of bait region cleavage, namely (i) the h-cysteinyl-g-glutamyl thiol ester becomes highly reactive and (ii) a major conformational change exposes a conserved COOH-terminal receptor binding domain [](RBD). RBD exposure allows the aM protease complex to bind to clearance receptors and be removed from circulation []. Tetrameric, dimeric, and, more recently, monomeric aM protease inhibitors have been identified [, ].This entry represents a conserved region, located towards the C terminus, which contains the two residues involved in the thiol ester bond.
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Protein Domain
IPR044731 | BDH-like
Type: Family
Description: Butanol dehydrogenase (BDH) is involved in the final step of the butanol formation pathway, in which it catalyses the conversion of butyraldehyde to butanol with the cofactor NAD(P)H being oxidised in the process. The NADH-BDH has higher activity with longer chained aldehydes and is inhibited by metabolites containing an adenine moiety. This protein family belongs to the so-called iron-containing alcohol dehydrogenase superfamily. Members in this family use divalent ions, preferentially iron or zinc []. This family also includes E. coli YqhD enzyme, an NADP-dependent dehydrogenase whose activity measurements with several alcohols demonstrate preference for alcohols longer than C3 [, ]. The active site of YqhD contains a zinc atom, and a modified NADPH cofactor bearing OH groups on the saturated C5 and C6 atoms, possibly due to oxygen stress on the enzyme, which would functionally work under anaerobic conditions.This entry also includes Long-chain-alcohol dehydrogenase 2 from Geobacillus thermodenitrificans which is able to oxidise a broad range of alkyl alcohols from methanol to 1-triacontanol (C1 to C30), whose best substrate is 1-octanol. In contrast to other members of the family, it apparently does not use iron or other metals as cofactor [].
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Protein Domain
IPR001599 | Macroglobln_a2
Type: Domain
Description: This entry contains serum complement C3 and C4 precursors and alpha-macrogrobulins. The alpha-macroglobulin (aM) family of proteins includes protease inhibitors [, ], typified by the human tetrameric a2-macroglobulin (a2M); they belong to the MEROPS proteinase inhibitor family I39, clan IL. These protease inhibitors share several defining properties, which include (i) the ability to inhibit proteases from all catalytic classes, (ii) the presence of a 'bait region' and a thioester, (iii) a similar protease inhibitory mechanism and (iv) the inactivation of the inhibitory capacity by reaction of the thiol ester with small primary amines. aM protease inhibitors inhibit by steric hindrance []. The mechanism involves protease cleavage of the bait region, a segment of the aM that is particularly susceptible to proteolytic cleavage, which initiates a conformational change such that the aM collapses about the protease. In the resulting aM-protease complex, the active site of the protease is sterically shielded, thus substantially decreasing access to protein substrates. Two additional events occur as a consequence of bait region cleavage, namely (i) the h-cysteinyl-g-glutamyl thiol ester becomes highly reactive and (ii) a major conformational change exposes a conserved COOH-terminal receptor binding domain [](RBD). RBD exposure allows the aM protease complex to bind to clearance receptors and be removed from circulation []. Tetrameric, dimeric, and, more recently, monomeric aM protease inhibitors have been identified [, ].
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Protein Domain
IPR008411 | BIV_Surface_Envelope
Type: Family
Description: (Bovine immunodeficiency virus) (BIV), like the human immunodeficiency virus, is a lentivirus. It shows a great deal of genomic diversity, mostly in the viral envelope gene []. This property of the BIV group of viruses may play an important role in the pathobiology of the virus, particularly the conserved (C) 2, hypervariable (V) 1, V2 and C3 regions [].The surface protein (SU) attaches the virus to the host cell by binding to its receptor. This interaction triggers the refolding of the transmembrane protein (TM) and is thought to activate its fusogenic potential by unmasking its fusion peptide. Fusion occurs at the host cell plasma membrane.The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm.
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Publication
9214622 | J:41124
First Author: Watanabe N
Year: 1997
Journal: EMBO J
Title: p140mDia, a mammalian homolog of Drosophila diaphanous, is a target protein for Rho small GTPase and is a ligand for profilin.
Volume: 16
Issue: 11
Pages: 3044-56
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Publication
9670022 | J:48926
First Author: Alberts AS
Year: 1998
Journal: EMBO J
Title: Activation of RhoA and SAPK/JNK signalling pathways by the RhoA-specific exchange factor mNET1.
Volume: 17
Issue: 14
Pages: 4075-85
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Publication
2993295 | J:32275
First Author: Nonaka M
Year: 1985
Journal: J Biol Chem
Title: Complete nucleotide and derived amino acid sequences of the fourth component of mouse complement (C4). Evolutionary aspects.
Volume: 260
Issue: 20
Pages: 10936-43
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Publication
9635436 | J:354373
First Author: Cachero TG
Year: 1998
Journal: Cell
Title: The small GTP-binding protein RhoA regulates a delayed rectifier potassium channel.
Volume: 93
Issue: 6
Pages: 1077-85
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Publication
11444019 | J:70003
First Author: Kawamura T
Year: 2001
Journal: Biochem Genet
Title: cDNA of a novel mRNA expressed predominantly in mouse kidney.
Volume: 39
Issue: 1-2
Pages: 33-42
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Publication
9203580 | J:41234
First Author: Kinoshita M
Year: 1997
Journal: Genes Dev
Title: Nedd5, a mammalian septin, is a novel cytoskeletal component interacting with actin-based structures.
Volume: 11
Issue: 12
Pages: 1535-47
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Publication
12732659 | J:83277
First Author: Díaz de Ståhl T
Year: 2003
Journal: J Exp Med
Title: A role for complement in feedback enhancement of antibody responses by IgG3.
Volume: 197
Issue: 9
Pages: 1183-90
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Publication
36359858 | J:331432
 
First Author: Ng ESY
Year: 2022
Journal: Cells
Title: Membrane Attack Complex Mediates Retinal Pigment Epithelium Cell Death in Stargardt Macular Degeneration.
Volume: 11
Issue: 21
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Publication
30021765 | J:264511
First Author: Pore D
Year: 2018
Journal: J Immunol
Title: Cutting Edge: Deletion of Ezrin in B Cells of Lyn-Deficient Mice Downregulates Lupus Pathology.
Volume: 201
Issue: 5
Pages: 1353-1358
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Publication
30926239 | J:282445
First Author: Bottermann M
Year: 2019
Journal: Cell Host Microbe
Title: Complement C4 Prevents Viral Infection through Capsid Inactivation.
Volume: 25
Issue: 4
Pages: 617-629.e7
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Publication
11726230 | J:115418
First Author: Welch TR
Year: 2001
Journal: Clin Immunol
Title: Evidence of a role for C4 in modulating interstitial inflammation in experimental glomerulonephritis.
Volume: 101
Issue: 3
Pages: 366-70
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Publication
31486767 | J:278994
   
First Author: Wu B
Year: 2019
Journal: Elife
Title: TRPC3 is a major contributor to functional heterogeneity of cerebellar Purkinje cells.
Volume: 8
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Publication
30415998 | J:269834
First Author: Litvinchuk A
Year: 2018
Journal: Neuron
Title: Complement C3aR Inactivation Attenuates Tau Pathology and Reverses an Immune Network Deregulated in Tauopathy Models and Alzheimer's Disease.
Volume: 100
Issue: 6
Pages: 1337-1353.e5
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Publication
15147568 | J:90499
First Author: Hutchinson WL
Year: 2004
Journal: Immunology
Title: Classical and alternative pathway complement activation are not required for reactive systemic AA amyloid deposition in mice.
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