About: Jerrold P. Weiss

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About: Jerrold P. Weiss Goto Sponge NotDistinct Permalink

An Entity of Type : wikibase:Item, within Data Space : wikidata.demo.openlinksw.com associated with source document(s)

researcher ORCID ID = 0000-0003-1476-4485

Attributes	Values
rdf:type	Item
description	Forscher (de) дослідник (uk) эрдэмтэн (mn) वैज्ञानिक (hi) изилдөөчү (ky) 研究者 (zh) onderzoeker (nl) researcher ORCID ID = 0000-0003-1476-4485 (en) научный исследователь (ru)
rdfs:label	Jerrold P Weiss (es) Jerrold P Weiss (nl) Jerrold P Weiss (ast) Jerrold P. Weiss (de) Jerrold P. Weiss (en) Джерролд П. Вайс (ru)
skos:prefLabel	Jerrold P Weiss (es) Jerrold P Weiss (nl) Jerrold P Weiss (ast) Jerrold P. Weiss (de) Jerrold P. Weiss (en) Джерролд П. Вайс (ru)
name	Jerrold P Weiss (es) Jerrold P Weiss (nl) Jerrold P Weiss (ast) Jerrold P. Weiss (de) Jerrold P. Weiss (en) Джерролд П. Вайс (ru)
Scopus author ID	wds:Q59569325-2F46F460-6F5B-478E-95D0-C545C0E9B5D3
Scopus author ID	7402740912
instance of	wds:Q59569325-8433B9F8-76BE-4B11-853C-997F3F850A90
instance of	Homo sapiens
skos:altLabel	Weiss (en) J. Weiss (en) J P Weiss (en) J Weiss (en) J. P. Weiss (en) Jerrold P Weiss (en) Jerrold Weiss (en) Weiss J. (en) Weiss J. P. (en) Weiss JP (en)
occupation	wds:Q59569325-9B2159AD-75DD-49F6-847C-EE2CEFCBB218
employer	wds:Q59569325-148B370C-F7CB-4AF6-8E9E-70F8C19A4952
educated at	wds:Q59569325-A6722348-226C-4D85-BEA5-105D7B5B264E
family name	wds:Q59569325-F7EBED39-9D85-441C-ACF3-643A863872ED
occupation	researcher
employer	University of Iowa
educated at	NYU Langone Medical Center
family name	Weiss
ORCID iD	wds:Q59569325-39FAD0D2-42EB-4FDC-B728-B4C894D7B139
Dimensions author ID	wds:Q59569325-422EB970-EA92-4E80-A381-16A893999009
ORCID iD	https://orcid.org/0000-0003-1476-4485
ORCID iD	0000-0003-1476-4485
Dimensions author ID	012362264647.95
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q59569325
is cites work of	Rat enterocyte injury by oxygen-dependent processes
is cites work of	wds:Q41130048-2CDD7422-F21E-4D72-9C42-513FBB6D4A5A
is author of	Neutrophil elastase targets virulence factors of enterobacteria Killing of gram-negative bacteria by polymorphonuclear leukocytes: role of an O2-independent bactericidal system. High-mobility group nucleosome-binding protein 1 acts as an alarmin and is critical for lipopolysaccharide-induced immune responses IFN-α and lipopolysaccharide upregulate APOBEC3 mRNA through different signaling pathways. Novel roles of lysines 122, 125, and 58 in functional differences between human and murine MD-2. Isolation of an endotoxin-MD-2 complex that produces Toll-like receptor 4-dependent cell activation at picomolar concentrations Transfer of monomeric endotoxin from MD-2 to CD14: characterization and functional consequences Effect of D-alanylation of (lipo)teichoic acids of Staphylococcus aureus on host secretory phospholipase A2 action before and after phagocytosis by human neutrophils Low concentrations of indomethacin inhibit phospholipase A2 of rabbit polymorphonuclear leukocytes The potent anti-Staphylococcus aureus activity of a sterile rabbit inflammatory fluid is due to a 14-kD phospholipase A2. Endotoxin responsiveness of human airway epithelia is limited by low expression of MD-2 Role of the bactericidal/permeability-increasing protein in host defence. The bactericidal/permeability-increasing protein (BPI), a potent element in host-defense against gram-negative bacteria and lipopolysaccharide. Neutrophil bleaching of GFP-expressing staphylococci: probing the intraphagosomal fate of individual bacteria Role of charge properties of bacterial envelope in bactericidal action of human group IIA phospholipase A2 against Staphylococcus aureus Synergy between extracellular group IIA phospholipase A2 and phagocyte NADPH oxidase in digestion of phospholipids of Staphylococcus aureus ingested by human neutrophils. Basis for the failure of Francisella tularensis lipopolysaccharide to prime human polymorphonuclear leukocytes. Partial characterization and purification of a rabbit granulocyte factor that increases permeability of Escherichia coli Early and discrete changes in permeability of Escherichia coli and certain other gram-negative bacteria during killing by granulocytes. Reversible envelope effects during and after killing of Escherichia coli w by a highly-purified rabbit polymorpho-nuclear leukocyte fraction Molecular basis of reduced potency of underacylated endotoxins Biochemical and functional characterization of membrane blebs purified from Neisseria meningitidis serogroup B. Bidirectional movement of a nascent polypeptide across microsomal membranes reveals requirements for vectorial translocation of proteins The TLR4 antagonist Eritoran protects mice from lethal influenza infection LBP/BPI proteins and their relatives: conservation over evolution and roles in mutualism Organism-specific neutrophil-endothelial cell interactions in response to Escherichia coli, Streptococcus pneumoniae, and Staphylococcus aureus Wall teichoic acid deficiency in Staphylococcus aureus confers selective resistance to mammalian group IIA phospholipase A(2) and human beta-defensin 3 The bactericidal/permeability-increasing protein (BPI) in infection and inflammatory disease. Evidence of a specific interaction between new synthetic antisepsis agents and CD14. A synthetic lipid A mimetic modulates human TLR4 activity Uniform lipopolysaccharide (LPS)-loaded magnetic nanoparticles for the investigation of LPS-TLR4 signaling. Bactericidal/permeability-increasing protein (rBPI21) and fluoroquinolone mitigate radiation-induced bone marrow aplasia and death The carboxyl-terminal domain of closely related endotoxin-binding proteins determines the target of protein-lipopolysaccharide complexes Human bactericidal/permeability-increasing protein and a recombinant NH2-terminal fragment cause killing of serum-resistant gram-negative bacteria in whole blood and inhibit tumor necrosis factor release induced by the bacteria An opsonic function of the neutrophil bactericidal/permeability-increasing protein depends on both its N- and C-terminal domains. Lipopolysaccharide (LPS)-binding proteins BPI and LBP form different types of complexes with LPS. Structural and functional organization of the human neutrophil 60 kDa bactericidal/permeability-increasing protein Respiratory syncytial virus fusion protein-induced toll-like receptor 4 (TLR4) signaling is inhibited by the TLR4 antagonists Rhodobacter sphaeroides lipopolysaccharide and eritoran (E5564) and requires direct interaction with MD-2. NMR studies of hexaacylated endotoxin bound to wild-type and F126A mutant MD-2 and MD-2·TLR4 ectodomain complexes Essential roles of hydrophobic residues in both MD-2 and toll-like receptor 4 in activation by endotoxin Molecular Basis of the Functional Differences between Soluble Human Versus Murine MD-2: Role of Val135 in Transfer of Lipopolysaccharide from CD14 to MD-2. The cationic amphiphile 3,4-bis(tetradecyloxy)benzylamine inhibits LPS signaling by competing with endotoxin for CD14 binding

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