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Search results 301 to 355 out of 355 for Lpp

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0.023s
Type Details Score
Publication      
First Author: Mouse Genome Database and National Center for Biotechnology Information
Year: 2000
Journal: Database Release
Title: Entrez Gene Load
Publication      
First Author: Mouse Genome Informatics Group
Year: 2003
Journal: Database Procedure
Title: Automatic Encodes (AutoE) Reference
Publication      
First Author: Bairoch A
Year: 1999
Journal: Database Release
Title: SWISS-PROT Annotated protein sequence database
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and Loading Genome Assembly Coordinates from Ensembl Annotations
Publication      
First Author: Mouse Genome Informatics (MGI) and The National Center for Biotechnology Information (NCBI)
Year: 2010
Journal: Database Download
Title: Consensus CDS project
Publication      
First Author: Mouse Genome Informatics
Year: 2010
Journal: Database Release
Title: Protein Ontology Association Load.
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and loading genome assembly coordinates from NCBI annotations
Publication      
First Author: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Gene 1.0 ST Array Platform
Publication      
First Author: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome 430 2.0 Array Platform
Publication      
First Author: Allen Institute for Brain Science
Year: 2004
Journal: Allen Institute
Title: Allen Brain Atlas: mouse riboprobes
Publication  
First Author: Zhang XW
Year: 2023
Journal: Redox Biol
Title: Lpp of Escherichia coli K1 inhibits host ROS production to counteract neutrophil-mediated elimination.
Volume: 59
Pages: 102588
Publication
First Author: Boags AT
Year: 2019
Journal: Structure
Title: Binding from Both Sides: TolR and Full-Length OmpA Bind and Maintain the Local Structure of the E. coli Cell Wall.
Volume: 27
Issue: 4
Pages: 713-724.e2
GO Term
Publication
First Author: Shu W
Year: 2000
Journal: J Mol Biol
Title: Core structure of the outer membrane lipoprotein from Escherichia coli at 1.9 A resolution.
Volume: 299
Issue: 4
Pages: 1101-12
Publication
First Author: Liu J
Year: 2002
Journal: J Mol Biol
Title: Core side-chain packing and backbone conformation in Lpp-56 coiled-coil mutants.
Volume: 318
Issue: 3
Pages: 877-88
Publication
First Author: Liu J
Year: 2004
Journal: Proc Natl Acad Sci U S A
Title: Atomic structure of a tryptophan-zipper pentamer.
Volume: 101
Issue: 46
Pages: 16156-61
Publication
First Author: Liu J
Year: 2006
Journal: J Mol Biol
Title: Conformational transition between four and five-stranded phenylalanine zippers determined by a local packing interaction.
Volume: 361
Issue: 1
Pages: 168-79
Protein Domain
Type: Domain
Description: This is leucine-zipper is found in the enterobacterial outer membrane lipoprotein LPP []. It is likely that this domain oligomerises and is involved in protein-protein interactions. As such it is a bundle of α-helical coiled-coils, which are known to play key roles in mediating specific protein-protein interactions for in molecular recognition and the assembly of multi-protein complexes [, , ].
Publication
First Author: Mannen H
Year: 1991
Journal: Lab Anim
Title: Incomplete protection mechanism against vesico-ureteral reflux and hydronephrosis in the inbred mouse strain DDD.
Volume: 25
Issue: 2
Pages: 156-61
Publication
First Author: Sciorra VA
Year: 2002
Journal: Biochim Biophys Acta
Title: Roles for lipid phosphate phosphatases in regulation of cellular signaling.
Volume: 1582
Issue: 1-3
Pages: 45-51
Publication
First Author: Escalante-Alcalde D
Year: 2003
Journal: Development
Title: The lipid phosphatase LPP3 regulates extra-embryonic vasculogenesis and axis patterning.
Volume: 130
Issue: 19
Pages: 4623-37
Publication  
First Author: Zhang QX
Year: 2000
Journal: Biochem J
Title: Identification of structurally important domains of lipid phosphate phosphatase-1: implications for its sites of action.
Volume: 345 Pt 2
Pages: 181-4
Publication
First Author: Tomsig JL
Year: 2009
Journal: Biochem J
Title: Lipid phosphate phosphohydrolase type 1 (LPP1) degrades extracellular lysophosphatidic acid in vivo.
Volume: 419
Issue: 3
Pages: 611-8
Publication
First Author: Smyth SS
Year: 2003
Journal: J Biol Chem
Title: Lipid phosphate phosphatases regulate lysophosphatidic acid production and signaling in platelets: studies using chemical inhibitors of lipid phosphate phosphatase activity.
Volume: 278
Issue: 44
Pages: 43214-23
Publication
First Author: Hooks SB
Year: 1998
Journal: FEBS Lett
Title: Identification of a novel human phosphatidic acid phosphatase type 2 isoform.
Volume: 427
Issue: 2
Pages: 188-92
Publication
First Author: Flanagan JM
Year: 2009
Journal: Mol Cancer Ther
Title: Genomics screen in transformed stem cells reveals RNASEH2A, PPAP2C, and ADARB1 as putative anticancer drug targets.
Volume: 8
Issue: 1
Pages: 249-60
Publication
First Author: Panchatcharam M
Year: 2014
Journal: Arterioscler Thromb Vasc Biol
Title: Mice with targeted inactivation of ppap2b in endothelial and hematopoietic cells display enhanced vascular inflammation and permeability.
Volume: 34
Issue: 4
Pages: 837-45
Protein Domain
Type: Family
Description: Type 2 lipid phosphate phosphohydrolases (LPPs), formerly known as phosphatidic acid phosphatases (PAPs), are enzymes that catalyse the hydrolysis of a variety of lipid phosphate mono-esters, including lysophosphatidic acid (LPA), PA, diacylglycerolpyrophosphate, S1P and ceramide 1-phosphate (C-1-P). These are lipid mediators that exert complex effects on cell function through actions at cell surface receptors and on intracellular targets []. Type 2 LPPs are membrane bound enzymes, Mg2+-independent and N-ethylmaleimide-insensitive []. In humans, at least three genes coding for type 2 LPP enzymes have been identified (LPP1, LPP2 and LPP3).LPP1, also known as PPAP2A, exhibits a preference for glycerol-versus sphingoid base-containing lipids []. LPP1 plays a physiological role in controlling the degradation of circulating lysophosphatidic acid (LPA) [], a lipid mediator that stimulates cell proliferation and growth, and is involved in physiological and pathological processes such as wound healing, platelet activation, angiogenesis and the growth of tumours. LPP1 regulates LPA production and signaling in platelets [].
Protein Domain
Type: Family
Description: Type 2 lipid phosphate phosphohydrolases (LPPs), formerly known as phosphatidic acid phosphatases (PAPs), are enzymes that catalyse the hydrolysis of a variety of lipid phosphate mono-esters, including lysophosphatidic acid (LPA), PA, diacylglycerolpyrophosphate, S1P and ceramide 1-phosphate (C-1-P). These are lipid mediators that exert complex effects on cell function through actions at cell surface receptors and on intracellular targets []. Type 2 LPPs are membrane bound enzymes, Mg2+-independent and N-ethylmaleimide-insensitive []. In humans, at least three genes coding for type 2 LPP enzymes have been identified (LPP1, LPP2 and LPP3).This entry represents LPP2, also known as PPAP2C []. PPAP2C is overexpressed in several cancers. In cancer cells, PPAP2C is involved in S-phase progression and is regulated by p53 [].
Protein Domain
Type: Family
Description: Type 2 lipid phosphate phosphohydrolases (LPPs), formerly known as phosphatidic acid phosphatases (PAPs), are enzymes that catalyse the hydrolysis of a variety of lipid phosphate mono-esters, including lysophosphatidic acid (LPA), PA, diacylglycerolpyrophosphate, S1P and ceramide 1-phosphate (C-1-P). These are lipid mediators that exert complex effects on cell function through actions at cell surface receptors and on intracellular targets []. Type 2 LPPs are membrane bound enzymes, Mg2+-independent and N-ethylmaleimide-insensitive []. In humans, at least three genes coding for type 2 LPP enzymes have been identified (LPP1, LPP2 and LPP3).LPP3, also known as PPAP2B, is essential to the formation of the chorioallantoic placenta and extraembryonic vasculature. It also mediates gastrulation and axis formation, probably by regulating the Wnt signaling pathway []. A common PPAP2B polymorphism is associated with increased risk of coronary artery disease in humans [].
Publication
First Author: Nanjundan M
Year: 2001
Journal: Biochem J
Title: Pulmonary lipid phosphate phosphohydrolase in plasma membrane signalling platforms.
Volume: 358
Issue: Pt 3
Pages: 637-46
Publication
First Author: Asztely F
Year: 2000
Journal: Eur J Neurosci
Title: Afferent-specific modulation of short-term synaptic plasticity by neurotrophins in dentate gyrus.
Volume: 12
Issue: 2
Pages: 662-9
Publication
First Author: Mohammad M
Year: 2020
Journal: Sci Rep
Title: The role of Staphylococcus aureus lipoproteins in hematogenous septic arthritis.
Volume: 10
Issue: 1
Pages: 7936
Publication
First Author: Zhai J
Year: 2002
Journal: Neuropharmacology
Title: Modulation of lateral perforant path excitatory responses by metabotropic glutamate 8 (mGlu8) receptors.
Volume: 43
Issue: 2
Pages: 223-30
Publication
First Author: Young K
Year: 2022
Journal: Zygote
Title: 5,10-Methylenetetrahydrofolate reductase becomes phosphorylated during meiotic maturation in mouse oocytes.
Volume: 30
Issue: 5
Pages: 674-688
Publication
First Author: Chen YH
Year: 2014
Journal: PLoS One
Title: Urethral dysfunction in female mice with estrogen receptor β deficiency.
Volume: 9
Issue: 9
Pages: e109058
Publication
First Author: Zhang H
Year: 2009
Journal: Physiol Genomics
Title: Lasp1 gene disruption is linked to enhanced cell migration and tumor formation.
Volume: 38
Issue: 3
Pages: 372-85
Publication
First Author: Hoffman LM
Year: 2003
Journal: Mol Cell Biol
Title: Targeted disruption of the murine zyxin gene.
Volume: 23
Issue: 1
Pages: 70-9
Publication
First Author: Waters NS
Year: 1994
Journal: Behav Brain Res
Title: Analysis of two measures of paw preference in a large population of inbred mice.
Volume: 63
Issue: 2
Pages: 195-204
Publication
First Author: Zheng K
Year: 2005
Journal: Neuropeptides
Title: Age-related impairments of synaptic plasticity in the lateral perforant path input to the dentate gyrus of galanin overexpressing mice.
Volume: 39
Issue: 3
Pages: 259-67
Publication
First Author: Schmaler M
Year: 2009
Journal: J Immunol
Title: Lipoproteins in Staphylococcus aureus mediate inflammation by TLR2 and iron-dependent growth in vivo.
Volume: 182
Issue: 11
Pages: 7110-8
Publication
First Author: Gregory Call S
Year: 2011
Journal: Biochem Biophys Res Commun
Title: A zyxin-nectin interaction facilitates zyxin localization to cell-cell adhesions.
Volume: 415
Issue: 3
Pages: 485-9
Protein Domain
Type: Family
Description: Members of this protein family are the TolB periplasmic protein of Gram-negative bacteria. TolB is part of the Tol-Pal (peptidoglycan-associated lipoprotein) multiprotein complex, comprising five envelope proteins, TolQ, TolR, TolA, TolB and Pal, which form two complexes. The TolQ, TolR and TolA inner-membrane proteins interact via their transmembrane domains. The β-propeller domain of the periplasmic protein TolB is responsible for its interaction with Pal. TolB also interacts with the outer-membrane peptidoglycan-associated proteins Lpp and OmpA. TolA undergoes a conformational change in response to changes in the proton-motive force, and interacts with Pal in an energy-dependent manner. The C-terminal periplasmic domain of TolA also interacts with the N-terminal domain of TolB. The Tol-PAL system is required for bacterial outer membrane integrity. Escherichia coli TolB is involved in the tonB-independent uptake of group A colicins (colicins A, E1, E2, E3 and K), and is necessary for the colicins to reach their respective targets after initial binding to the bacteria. It is also involved in uptake of filamentous DNA. Study of its structure suggests that the TolB protein might be involved in the recycling of peptidoglycan or in its covalent linking with lipoproteins. The Tol-Pal system is also implicated in pathogenesis of E. coli, Haemophilus ducreyi, Salmonella enterica and Vibrio cholerae, but the mechanism(s) is unclear.
Publication
First Author: Lee SH
Year: 2023
Journal: Mol Brain
Title: Presenilins regulate synaptic plasticity in the perforant pathways of the hippocampus.
Volume: 16
Issue: 1
Pages: 17
Publication
First Author: Bouta EM
Year: 2014
Journal: J Physiol
Title: In vivo quantification of lymph viscosity and pressure in lymphatic vessels and draining lymph nodes of arthritic joints in mice.
Volume: 592
Issue: 6
Pages: 1213-23
Publication  
First Author: Mercier MS
Year: 2013
Journal: Neuropharmacology
Title: Characterisation of an mGlu8 receptor-selective agonist and antagonist in the lateral and medial perforant path inputs to the dentate gyrus.
Volume: 67
Pages: 294-303
Publication
First Author: Waggoner DW
Year: 1999
Journal: Biochim Biophys Acta
Title: Structural organization of mammalian lipid phosphate phosphatases: implications for signal transduction.
Volume: 1439
Issue: 2
Pages: 299-316
Publication
First Author: Carman GM
Year: 2006
Journal: Trends Biochem Sci
Title: Roles of phosphatidate phosphatase enzymes in lipid metabolism.
Volume: 31
Issue: 12
Pages: 694-9
Protein
Organism: Mus musculus/domesticus
Length: 312  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 283  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 276  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 220  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 284  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 288  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 158  
Fragment?: false