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1 AFGP/ice dynamics was dominated by fast-scale motions (n
2 AFGPs appear to remain undegraded in the intestinal mili
3 AFGPs in both fishes are made as a family of discretely
4 ucture as its overall conformation, although AFGP does adopt other conformations during the course of
5 d genomic DNA libraries for AFGP-bearing and AFGP-lacking species across the gadid phylogeny and perf
6 a combination of freeze avoidance offered by AFGPs and subsequent exploitation of new habitats and op
7 e protease), and surprisingly three chimeric AFGP/TLP, one of which was previously hypothesized to be
9 te from a pancreatic trypsinogen, Arctic cod AFGP genes share no sequence identity with the trypsinog
10 type length variation results from different AFGP copy number, suggesting substantial dynamism existe
14 We constructed genomic DNA libraries for AFGP-bearing and AFGP-lacking species across the gadid p
17 of the 14-amino acid antifreeze glycoprotein AFGP-8 have concluded that the molecule lacks long-range
18 e protein (AFP) and antifreeze glycoprotein (AFGP) are attached onto the surface of well-defined Au c
20 adaptive phenotype, antifreeze glycoprotein (AFGP) that enables Antarctic notothenioid survival in th
22 roteins (AFPs) and antifreeze glycoproteins (AFGPs) enable the survival of organisms living in subfre
24 ave found that the antifreeze glycoproteins (AFGPs) of the predominant Antarctic fish taxon, the noto
25 proteins (AFPs) or antifreeze glycoproteins (AFGPs) to avoid inoculative freezing by internalized ice
26 uce near-identical antifreeze glycoproteins (AFGPs) to survive in their respective freezing environme
29 o the nature of conformations and motions in AFGP-8, we have undertaken molecular dynamics simulation
31 rption of intact pancreas-derived intestinal AFGPs, and not the liver, is the likely source of circul
34 saida were dimethylated at the N-terminus (m*AFGP) and their dynamics and conformational properties w
35 tein genes, with each gene encoding multiple AFGP molecules linked in tandem by small cleavable space
37 uence divergence (4-7%) between notothenioid AFGP and trypsinogen genes indicates that the transforma
39 nto the molecular mechanisms of notothenioid AFGP gene family evolution driven by Southern Ocean glac
42 effect of hydration on the local mobility of AFGP and the lack of significant change in the backbone
43 eoclimate, we demonstrate that the origin of AFGP occurred between 42 and 22 Ma, which includes a per
45 he exocrine pancreas to be the major site of AFGP synthesis and secretion in all life stages, and tha
46 we conclude that the stabilizing effects of AFGPs on intact cells during chilling reported by Rubins
48 t least 10 million years after the origin of AFGPs, during a second cooling event in the Late Miocene
50 : the complete absence of liver synthesis of AFGPs in any life stage of the Antarctic notothenioids,
52 tion in all life stages, and that pancreatic AFGPs enter the intestinal lumen via the pancreatic duct
54 la-Ala unit from which the extant repetitive AFGP-coding sequence (cds) arose through tandem duplicat
57 se two polar fishes evolved their respective AFGPs separately and thus arrived at the same AFGPs thro
60 that the presence of prolines in this small AFGP structure facilitates the adoption of the poly-prol
61 (363.6 kbp and 467.4 kbp) containing tandem AFGP, two TLP (trypsinogen-like protease), and surprisin
66 usly, Rubinsky et al. provided evidence that AFGPs block ion fluxes across membranes during cooling,
67 d substructures provide strong evidence that AFGPs in these two polar fishes in fact evolved independ
68 tifreeze activity may be induced because the AFGP perturbs the aqueous solvent over long distances.
69 n the frigid Southern Ocean, we isolated the AFGP genomic locus from a bacterial artificial chromosom
71 arent similarities, detailed analyses of the AFGP gene sequences and substructures provide strong evi
76 ard bulk water behavior strongly reduces the AFGP antifreeze activity, further supporting our model.
78 thenioids and the Arctic cod show that their AFGPs are both encoded by a family of polyprotein genes,