Human serum amyloid P component is an invariant constituent of amyloid deposits and has a uniquely homogeneous glycostructure.
about
Light chain (AL) amyloidosis: update on diagnosis and managementIn vitro inhibition of transthyretin aggregate-induced cytotoxicity by full and peptide derived forms of the soluble receptor for advanced glycation end products (RAGE)Serum amyloid P is a sialylated glycoprotein inhibitor of influenza A virusesSerum amyloid P component prevents proteolysis of the amyloid fibrils of Alzheimer disease and systemic amyloidosisMolecular dissection of Alzheimer's disease neuropathology by depletion of serum amyloid P componentPentraxins: structure, function, and role in inflammationSerum amyloid P aids complement-mediated immunity to Streptococcus pneumoniae.Mass spectrometric-based proteomic analysis of amyloid neuropathy type in nerve tissue.Examining serum amyloid P component microheterogeneity using capillary isoelectric focusing and MALDI-MSIsolation and characterization of pharmaceutical grade human pentraxins, serum amyloid P component and C-reactive protein, for clinical use.Novel approaches to the treatment of primary amyloidosis.The pentraxins, C-reactive protein and serum amyloid P component, are cleared and catabolized by hepatocytes in vivo.Dynamic PET and SPECT imaging with radioiodinated, amyloid-reactive peptide p5 in mice: a positive role for peptide dehalogenation.Amyloid-like IgM deposition neuropathy: a distinct clinico-pathologic and proteomic profiled disorderAnalysis of amyloid deposition in a transgenic mouse model of homozygous familial amyloidotic polyneuropathyDC-SIGN activation mediates the differential effects of SAP and CRP on the innate immune system and inhibits fibrosis in miceRole of serum amyloid P component in bacterial infection: protection of the host or protection of the pathogenAmyloid accomplices and enforcersPattern recognition by pentraxinsThe "sweet" side of a long pentraxin: how glycosylation affects PTX3 functions in innate immunity and inflammation.Drug Insight: emerging therapies for amyloidosis.Function and control of human invasive trophoblast subtypes: Intrinsic vs. maternal control.Potential roles of abundant extracellular chaperones in the control of amyloid formation and toxicity.In situ characterization of protein aggregates in human tissues affected by light chain amyloidosis: a FTIR microspectroscopy study.Hereditary hepatic and systemic amyloidosis caused by a new deletion/insertion mutation in the apolipoprotein AI geneSAP suppresses the development of experimental autoimmune encephalomyelitis in C57BL/6 mice.Serum amyloid A and protein AA: molecular mechanisms of a transmissible amyloidosis.beta(2)-microglobulin: from physiology to amyloidosis.Proteomic typing of amyloid deposits in systemic amyloidoses.Light-chain amyloidosis: SCT, novel agents and beyond.Clinical proteomics for diagnosis and typing of systemic amyloidoses.The long pentraxin PTX3: a paradigm for humoral pattern recognition molecules.Characterization of heparin binding by a peptide from amyloid P component using capillary electrophoresis, surface plasmon resonance and isothermal titration calorimetry.Advances in proteomic study of cardiac amyloidosis: progress and potential.Loss of prohormone convertase 2 promotes beta cell dysfunction in a rodent transplant model expressing human pro-islet amyloid polypeptide.Amyloid plaques beyond Aβ: a survey of the diverse modulators of amyloid aggregation.Fibrillar amyloid protein present in atheroma activates CD36 signal transduction.A unique biofilm in human deep mycoses: fungal amyloid is bound by host serum amyloid P component.Investigating interactions of the pentraxins serum amyloid P component and C-reactive protein by mass spectrometry.New features of invasive candidiasis in humans: amyloid formation by fungi and deposition of serum amyloid P component by the host.
P2860
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P2860
Human serum amyloid P component is an invariant constituent of amyloid deposits and has a uniquely homogeneous glycostructure.
description
1994 nî lūn-bûn
@nan
1994 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
1994 թվականի հունիսին հրատարակված գիտական հոդված
@hy
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
name
Human serum amyloid P componen ...... ly homogeneous glycostructure.
@ast
Human serum amyloid P componen ...... ly homogeneous glycostructure.
@en
type
label
Human serum amyloid P componen ...... ly homogeneous glycostructure.
@ast
Human serum amyloid P componen ...... ly homogeneous glycostructure.
@en
prefLabel
Human serum amyloid P componen ...... ly homogeneous glycostructure.
@ast
Human serum amyloid P componen ...... ly homogeneous glycostructure.
@en
P2093
P2860
P356
P1476
Human serum amyloid P componen ...... ly homogeneous glycostructure.
@en
P2093
J R Gallimore
P N Hawkins
P Williams
S Amatayakul-Chantler
S R Nelson
T W Rademacher
W L Hutchinson
P2860
P304
P356
10.1073/PNAS.91.12.5602
P407
P50
P577
1994-06-01T00:00:00Z