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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

APAF1 interacting protein

Apaf-1-interacting protein, APIP
APIP is an APAF1 (MIM 602233)-interacting protein that acts as a negative regulator of ischemic/hypoxic injury (Cho et al., 2004 [PubMed 15262985]).[supplied by OMIM, Dec 2008] (from NCBI)
Top mentioned proteins: Apaf-1, PrP, caspase-9, caspase-3, HAD
Papers on Apaf-1-interacting protein
Mitogen-Activated Protein Kinases Are Activated in Placental Injury in Rat Model of Acute Pancreatitis in Pregnancy.
Guo et al., Wuhan, China. In Pancreas, Nov 2015
OBJECTIVES: To establish a rat model of acute pancreatitis in pregnancy (APIP) and evaluate its general presentations, assess placental injury, and discuss possible mechanisms.
CD44-SLC1A2 fusion transcripts in primary colorectal cancer.
Sugimura et al., Hamamatsu, Japan. In Pathol Oncol Res, Jul 2015
A CD44-SLC1A2 fusion has recently been discovered in a subset of primary gastric cancers, and an APIP-SLC1A2 fusion has been described in a colon cancer cell line (SNU-C1); however, whether such SLC1A2 fusions occur in primary colorectal cancer (CRC) and whether such fusions are specific for gastrointestinal cancers remain uncertain.
Somatic mutations of amino acid metabolism-related genes in gastric and colorectal cancers and their regional heterogeneity--a short report.
Lee et al., Seoul, South Korea. In Cell Oncol (dordr), 2014
METHODS: Through a public database search, we found that a number of genes known to be involved in amino acid metabolism, i.e., AGXT, ALDH2, APIP, MTR, DNMT1, ASH1L, ASPA, CAD, DDC, GCDH, DLD, LAP3, MCEE and MUT, harbor mononucleotide repeats that may serve as mutation targets in cancers exhibiting microsatellite instability (MSI).
Network analysis in the identification of special mechanisms between small cell lung cancer and non-small cell lung cancer.
Lei et al., Tianjin, China. In Thorac Cancer, 2014
Moreover, a potential biomarker of SCLC is the interaction between APIP and apoptotic protease activating factor (APAF)1, which share a common module.
Structural and biochemical basis for the inhibition of cell death by APIP, a methionine salvage enzyme.
Yang et al., Seoul, South Korea. In Proc Natl Acad Sci U S A, 2014
APIP, Apaf-1 interacting protein, has been known to inhibit two main types of programmed cell death, apoptosis and pyroptosis, and was recently found to be associated with cancers and inflammatory diseases.
Breakpoint analysis of transcriptional and genomic profiles uncovers novel gene fusions spanning multiple human cancer types.
Pollack et al., Stanford, United States. In Plos Genet, 2013
From these, we validated and further characterized novel gene fusions involving ROS1 tyrosine kinase in angiosarcoma (CEP85L/ROS1), SLC1A2 glutamate transporter in colon cancer (APIP/SLC1A2), RAF1 kinase in pancreatic cancer (ATG7/RAF1) and anaplastic astrocytoma (BCL6/RAF1), EWSR1 in melanoma (EWSR1/CREM), CDK6 kinase in T-cell acute lymphoblastic leukemia (FAM133B/CDK6), and CLTC in breast cancer (CLTC/VMP1).
Crystallization and preliminary X-ray crystallographic analysis of human Apaf-1-interacting protein.
Yang et al., Seoul, South Korea. In Acta Crystallogr Sect F Struct Biol Cryst Commun, 2013
Apaf-1-interacting protein (APIP) is known to inhibit two different types of cell death: caspase-1-dependent pyroptosis and caspase-9-dependent apoptosis.
Functional genetic screen of human diversity reveals that a methionine salvage enzyme regulates inflammatory cell death.
Miller et al., Seattle, United States. In Proc Natl Acad Sci U S A, 2012
A common SNP associated with reduced expression of a putative methionine salvage pathway dehydratase, apoptotic protease activating factor 1 (APAF1)-interacting protein (APIP), was associated with increased caspase-1-mediated cell death in response to Salmonella.
Down-regulated expression of apoptosis-associated genes APIP and UACA in non-small cell lung carcinoma.
Benkova et al., Praha, Czech Republic. In Int J Oncol, 2012
The down-regulation of APIP and UACA expression suggests that the threshold to activate the apoptosome apparatus may be decreased in non-small cell lung cancer cells.
Functional identification of APIP as human mtnB, a key enzyme in the methionine salvage pathway.
Lane et al., Genève, Switzerland. In Plos One, 2011
Using a bioinformatics approach, we propose that a protein called APIP could perform this role.
Ruthenium(II) polypyridyl complexes: synthesis and studies of DNA binding, photocleavage, cytotoxicity, apoptosis, cellular uptake, and antioxidant activity.
Huang et al., Guangzhou, China. In Dna Cell Biol, 2011
Two ruthenium (II) complexes [Ru(dmb)2(APIP)](ClO4)2 (APIP=2-(2-aminophenyl)imidazo[4,5-f ][1,10]phenanthroline, dmb=4,4'-dimethyl-2,2'-bipyridine; 1) and [Ru(dmb)2(HAPIP)](ClO4)2 (HAPIP=2-(2-hydroxyl-4-aminophenyl)imidazo[4,5-f ][1,10]phenanthroline; 2) were synthesized and characterized.
High-resolution copy number and gene expression microarray analyses of head and neck squamous cell carcinoma cell lines of tongue and larynx.
Monni et al., Helsinki, Finland. In Genes Chromosomes Cancer, 2008
We identified a number of altered regions including nine high-level amplifications such as 6q12-q14 (CD109, MYO6), 9p24 (JAK2, CD274, SLC1A1, RLN1), 11p12-p13 (TRAF6, COMMD9, TRIM44, FJX1, CD44, PDHX, APIP), 11q13 (FADD, PPFIA1, CTTN), and 14q24 (ABCD4, HBLD1, LTBP2, ZNF410, COQ6, ACYP1, JDP2) where 9% to 64% of genes showed overexpression.
Positive regulation of apoptosis by HCA66, a new Apaf-1 interacting protein, and its putative role in the physiopathology of NF1 microdeletion syndrome patients.
Poyet et al., Paris, France. In Cell Death Differ, 2007
We report here the identification of a novel Apaf-1 interacting protein, hepatocellular carcinoma antigen 66 (HCA66) that is able to modulate selectively Apaf-1-dependent apoptosis through its direct association with the CED4 domain of Apaf-1.
Suppression of hypoxic cell death by APIP-induced sustained activation of AKT and ERK1/2.
Jung et al., Kwangju, South Korea. In Oncogene, 2007
Apaf-1-interacting protein (APIP) was previously isolated as an inhibitor of mitochondrial cell death interacting with Apaf-1.
Induced inhibition of ischemic/hypoxic injury by APIP, a novel Apaf-1-interacting protein.
Jung et al., Kwangju, South Korea. In J Biol Chem, 2004
APIP functions to inhibit muscle ischemic damage by binding to Apaf-1 in the Apaf-1/caspase-9 apoptosis pathway.
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