PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
32101030-0	2020	Postbiotics for NOD2 require nonhematopoietic RIPK2 to improve blood glucose and metabolic inflammation in mice.	Glucose	69-76	nucleotide-binding oligomerization domain containing 2	Mus musculus	16-20	
32722085-3	2020	Muramyl dipeptide (MDP) is a bacterial cell wall component which has been shown to improve insulin sensitivity and glucose tolerance in diet-induced obese mice by acting through the nucleotide oligomerization domain 2 (NOD2) receptor.	Glucose	115-122	nucleotide-binding oligomerization domain containing 2	Mus musculus	219-223	
32722085-5	2020	We hypothesized that MDP enhances glucose tolerance by inducing intestinal GLP-1 secretion through NOD2 activation.	Glucose	34-41	nucleotide-binding oligomerization domain containing 2	Mus musculus	99-103	
32101030-9	2020	We found that whole body deletion of RIPK2 prevented the glucose-lowering effects of repeated NOD2 activation that were evident during a glucose tolerance test (GTT) in high-fat diet (HFD)-fed wild-type (WT) mice.	Glucose	57-64	nucleotide-binding oligomerization domain containing 2	Mus musculus	94-98	
32101030-9	2020	We found that whole body deletion of RIPK2 prevented the glucose-lowering effects of repeated NOD2 activation that were evident during a glucose tolerance test (GTT) in high-fat diet (HFD)-fed wild-type (WT) mice.	Glucose	137-144	nucleotide-binding oligomerization domain containing 2	Mus musculus	94-98	
32101030-10	2020	NOD2 activation lowered glucose during a GTT and lowered adipose tissue inflammation in mice with RIPK2 deleted in hematopoietic cells.	Glucose	24-31	nucleotide-binding oligomerization domain containing 2	Mus musculus	0-4	
32101030-11	2020	We conclude that RIPK2 in nonhematopoietic cells mediates the glucose lowering and anti-inflammatory effects of NOD2-activating postbiotics.	Glucose	62-69	nucleotide-binding oligomerization domain containing 2	Mus musculus	112-116	
28373658-4	2017	Nod2 -/- HFD mice developed hyperlipidemia, hyperglycemia, glucose intolerance, increased adiposity, and steatosis, with large lipid droplets in their hepatocytes.	Glucose	59-66	nucleotide-binding oligomerization domain containing 2	Mus musculus	0-4	
23594678-5	2013	In vitro, NOD2 induced proinflammatory response and impaired insulin signaling and insulin-induced glucose uptake in podocytes.	Glucose	99-106	nucleotide-binding oligomerization domain containing 2	Mus musculus	10-14	
23594678-6	2013	Moreover, podocytes treated with high glucose, advanced glycation end-products, tumor necrosis factor-alpha, or transforming growth factor-beta (common detrimental factors in diabetic nephropathy) significantly increased NOD2 expression.	Glucose	38-45	nucleotide-binding oligomerization domain containing 2	Mus musculus	221-225	
23594678-8	2013	Further, knockdown of NOD2 expression attenuated high glucose-induced nephrin downregulation in vitro, supporting an essential role of NOD2 in mediating hyperglycemia-induced podocyte dysfunction.	Glucose	54-61	nucleotide-binding oligomerization domain containing 2	Mus musculus	22-26	
23594678-8	2013	Further, knockdown of NOD2 expression attenuated high glucose-induced nephrin downregulation in vitro, supporting an essential role of NOD2 in mediating hyperglycemia-induced podocyte dysfunction.	Glucose	54-61	nucleotide-binding oligomerization domain containing 2	Mus musculus	135-139	
21715553-10	2011	NOD2 ligands only modestly reduced peripheral glucose disposal.	Glucose	46-53	nucleotide-binding oligomerization domain containing 2	Mus musculus	0-4