Saposin-like proteins (SAPLIP) carry out diverse functions on a common backbone structure
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A short guided tour through functional and structural features of saposin-like proteinsCrystal structure of saposin B reveals a dimeric shell for lipid bindingNMR structure of a fungal virulence factor reveals structural homology with mammalian saposin BInsights into the Membrane Interactions of the Saposin-Like Proteins Na-SLP-1 and Ac-SLP-1 from Human and Dog HookwormA vacuolar sorting domain may also influence the way in which proteins leave the endoplasmic reticulumRole of the N-terminal seven residues of surfactant protein B (SP-B)Crystallization and preliminary characterization of three different crystal forms of human saposin C heterologously expressed in Pichia pastoris.Interaction of the C-terminal peptide of pulmonary surfactant protein B (SP-B) with a bicellar lipid mixture containing anionic lipid.Shield as signal: lipopolysaccharides and the evolution of immunity to gram-negative bacteria.Critical structural and functional roles for the N-terminal insertion sequence in surfactant protein B analogs.Chapter 2: Kill the bacteria...and also their messengers?Characterization of Drosophila Saposin-related mutants as a model for lysosomal sphingolipid storage diseases.J3-crystallin of the jellyfish lens: similarity to saposinsPhospholipid membrane interactions of saposin C: in situ atomic force microscopic studySignals from the lysosome: a control centre for cellular clearance and energy metabolism.Host-microbe interactions and defense mechanisms in the development of amoebic liver abscesses.A 60-kilodalton protein component of the counting factor complex regulates group size in Dictyostelium discoideum.Biosynthesis and degradation of mammalian glycosphingolipids.Methionine oxidation within the cerebroside-sulfate activator protein (CSAct or Saposin B).Interactions of the C-terminus of lung surfactant protein B with lipid bilayers are modulated by acyl chain saturation.The immunological functions of saposins.NK-lysin and its shortened analog NK-2 exhibit potent activities against Trypanosoma cruziInteraction of NK lysin, a peptide produced by cytolytic lymphocytes, with endotoxin.Biophysical characterization of endotoxin inactivation by NK-2, an antimicrobial peptide derived from mammalian NK-lysin.Critical structure-function determinants within the N-terminal region of pulmonary surfactant protein SP-BThe effect of a C-terminal peptide of surfactant protein B (SP-B) on oriented lipid bilayers, characterized by solid-state 2H- and 31P-NMR.Establishing the yeast Kluyveromyces lactis as an expression host for production of the saposin-like domain of the aspartic protease cirsin.Amoebapores and NK-lysin, members of a class of structurally distinct antimicrobial and cytolytic peptides from protozoa and mammals: a comparative functional analysis.Differential expression and localization of saposin-like protein 2 of Fasciola hepatica.Cloning, expression and map assignment of chicken prosaposinCharacterization of secondary structure and lipid binding behavior of N-terminal saposin like subdomain of human Wnt3a.Stability of an amphipathic helix-hairpin surfactant peptide in liposomes.Crystal structure of the mammalian lipopolysaccharide detoxifier.Environmental adaptation of Acanthamoeba castellanii and Entamoeba histolytica at genome level as seen by comparative genomic analysis.The Saposin-Like Protein AplD Displays Pore-Forming Activity and Participates in Defense Against Bacterial Infection During a Multicellular Stage of Dictyostelium discoideum.A sulfur-free peptide mimic of surfactant protein B (B-YL) exhibits high in vitro and in vivo surface activitiesCharacterization of Sphingomyelin Phosphodiesterase Expression in Bumblebee (Bombus lantschouensis)
P2860
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P2860
Saposin-like proteins (SAPLIP) carry out diverse functions on a common backbone structure
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1995 nî lūn-bûn
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1995 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
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1995 թվականի օգոստոսին հրատարակված գիտական հոդված
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1995年の論文
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1995年学术文章
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1995年学术文章
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1995年学术文章
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1995年学术文章
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1995年学术文章
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1995年學術文章
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Saposin-like proteins (SAPLIP) carry out diverse functions on a common backbone structure
@ast
Saposin-like proteins (SAPLIP) carry out diverse functions on a common backbone structure
@en
Saposin-like proteins (SAPLIP) carry out diverse functions on a common backbone structure
@nl
type
label
Saposin-like proteins (SAPLIP) carry out diverse functions on a common backbone structure
@ast
Saposin-like proteins (SAPLIP) carry out diverse functions on a common backbone structure
@en
Saposin-like proteins (SAPLIP) carry out diverse functions on a common backbone structure
@nl
prefLabel
Saposin-like proteins (SAPLIP) carry out diverse functions on a common backbone structure
@ast
Saposin-like proteins (SAPLIP) carry out diverse functions on a common backbone structure
@en
Saposin-like proteins (SAPLIP) carry out diverse functions on a common backbone structure
@nl
P2093
P1476
Saposin-like proteins (SAPLIP) carry out diverse functions on a common backbone structure
@en
P2093
Munford RS
Sheppard PO
P304
P407
P577
1995-08-01T00:00:00Z