PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 11034202-0 2000 Structural determinants of water permeation through aquaporin-1. Water 27-32 aquaporin 1 (Colton blood group) Homo sapiens 52-63 11034202-1 2000 Human red cell AQP1 is the first functionally defined member of the aquaporin family of membrane water channels. Water 97-102 aquaporin 1 (Colton blood group) Homo sapiens 15-19 10926515-0 2000 Three-dimensional fold of the human AQP1 water channel determined at 4 A resolution by electron crystallography of two-dimensional crystals embedded in ice. Water 41-46 aquaporin 1 (Colton blood group) Homo sapiens 36-40 10982394-2 2000 For the human aquaporin water channel AQP1, however, the initial four-segment-spanning topology at the ER membrane differs from the mature six-segment-spanning topology at the plasma membrane. Water 24-29 aquaporin 1 (Colton blood group) Homo sapiens 38-42 10982394-7 2000 AQP1 topological reorientation was also associated with maturation from a protease-sensitive conformation to a protease-resistant structure with water channel function. Water 145-150 aquaporin 1 (Colton blood group) Homo sapiens 0-4 11144661-4 2000 For example, the high water permeability of the proximal tubule has been shown to be imparted by the water channel, aquaporin AQP1; however, genetic knockout of this water channel is at least partially compensated by intrarenal feedback mechanisms. Water 22-27 aquaporin 1 (Colton blood group) Homo sapiens 126-130 11144661-4 2000 For example, the high water permeability of the proximal tubule has been shown to be imparted by the water channel, aquaporin AQP1; however, genetic knockout of this water channel is at least partially compensated by intrarenal feedback mechanisms. Water 101-106 aquaporin 1 (Colton blood group) Homo sapiens 126-130 11144661-4 2000 For example, the high water permeability of the proximal tubule has been shown to be imparted by the water channel, aquaporin AQP1; however, genetic knockout of this water channel is at least partially compensated by intrarenal feedback mechanisms. Water 101-106 aquaporin 1 (Colton blood group) Homo sapiens 126-130 10873606-2 2000 Like the kidney, the eye contains multiple water channel proteins (aquaporins) that transport water through membranes, including two (AQP1 and AQP4) in the ciliary body, the site of aqueous humor production. Water 43-48 aquaporin 1 (Colton blood group) Homo sapiens 134-138 10933509-4 2000 Well-ordered crystals of the water channel human aquaporin-1 (hAQP1) that diffract to 4 A resolution have been obtained with this approach. Water 29-34 aquaporin 1 (Colton blood group) Homo sapiens 49-60 10933509-4 2000 Well-ordered crystals of the water channel human aquaporin-1 (hAQP1) that diffract to 4 A resolution have been obtained with this approach. Water 29-34 aquaporin 1 (Colton blood group) Homo sapiens 62-67 10873606-3 2000 Previous results from our laboratory demonstrated that water channel activity of AQP1 was significantly increased by protein kinase A (PKA) activators such as cyclic-AMP (cAMP) and forskolin. Water 55-60 aquaporin 1 (Colton blood group) Homo sapiens 81-85 10873606-4 2000 The purpose of this study is to determine whether PKA-dependent protein phosphorylation is involved in the regulation of water channel activity of AQP1. Water 121-126 aquaporin 1 (Colton blood group) Homo sapiens 147-151 10873606-8 2000 In addition, they suggest important potential roles for AQP1 in several clinical disorders involving rapid water transport such as glaucoma. Water 107-112 aquaporin 1 (Colton blood group) Homo sapiens 56-60 10779387-2 2000 For AQP1, inhibition by mercury has been attributed to the formation of a mercaptide bond with cysteine residue 189 found in the putative pore-forming region loop E. Here we show that the nonmercurial compound, tetraethylammonium (TEA) chloride, reduces the water permeability of human AQP1 channels expressed in Xenopus oocytes. Water 258-263 aquaporin 1 (Colton blood group) Homo sapiens 4-8 10779387-3 2000 After preincubation of the oocytes for 15 min with 100 microM TEA, AQP1 water permeability was reduced by 20 to 40%, a degree of partial block similar to that obtained with 15 min of incubation in 100 microM HgCl(2). Water 72-77 aquaporin 1 (Colton blood group) Homo sapiens 67-71 10779387-8 2000 Oocyte expression of the mutant AQP1 channels showed that the water permeability of Y186F was equivalent to that of wild-type AQP1; the other mutant channels did not conduct water. Water 62-67 aquaporin 1 (Colton blood group) Homo sapiens 32-36 10779387-8 2000 Oocyte expression of the mutant AQP1 channels showed that the water permeability of Y186F was equivalent to that of wild-type AQP1; the other mutant channels did not conduct water. Water 174-179 aquaporin 1 (Colton blood group) Homo sapiens 32-36 10779387-10 2000 These results suggest that TEA reduces AQP1 water permeability by interacting with loop E. Water 44-49 aquaporin 1 (Colton blood group) Homo sapiens 39-43 10784341-2 2000 Null mutations in the water channel aquaporin 1 (AQP1) or the Na/H exchanger NHE3, two major fluid transporters in the proximal tubule, are states in which a reduction in proximal fluid absorption is accompanied by proportionate decrements in glomerular filtration rate. Water 22-27 aquaporin 1 (Colton blood group) Homo sapiens 49-53 10662724-5 2000 RT-PCR of microdissected segments showed that the water channel aquaporin-1 (AQP1) and the urea transporter UT-A2 were expressed in pure DTL, but not in pure ATL, and in DTL-type, but not in ATL-type, regions of mixed-type thin limbs. Water 50-55 aquaporin 1 (Colton blood group) Homo sapiens 77-81 10779387-0 2000 Inhibition of aquaporin-1 water permeability by tetraethylammonium: involvement of the loop E pore region. Water 26-31 aquaporin 1 (Colton blood group) Homo sapiens 14-25 10779387-1 2000 Previously, the only known blockers of water permeability through aquaporin-1 (AQP1) water channels were mercurial reagents such as HgCl(2). Water 39-44 aquaporin 1 (Colton blood group) Homo sapiens 66-77 10779387-1 2000 Previously, the only known blockers of water permeability through aquaporin-1 (AQP1) water channels were mercurial reagents such as HgCl(2). Water 39-44 aquaporin 1 (Colton blood group) Homo sapiens 79-83 10779387-1 2000 Previously, the only known blockers of water permeability through aquaporin-1 (AQP1) water channels were mercurial reagents such as HgCl(2). Water 85-90 aquaporin 1 (Colton blood group) Homo sapiens 66-77 10779387-1 2000 Previously, the only known blockers of water permeability through aquaporin-1 (AQP1) water channels were mercurial reagents such as HgCl(2). Water 85-90 aquaporin 1 (Colton blood group) Homo sapiens 79-83 10694901-8 2000 Osmotic water permeability (P( f)) measurements confirmed that functional AQP1 water channels are expressed in human NPE cells and the P(f) for these cells was 9.8 x 10( -3) cm/s at 10 degrees C. CONCLUSIONS: The presence of AQP1 in human NPE cells suggests that it may have a role in the fluid flow across epithelial membranes. Water 8-13 aquaporin 1 (Colton blood group) Homo sapiens 74-78 10694901-8 2000 Osmotic water permeability (P( f)) measurements confirmed that functional AQP1 water channels are expressed in human NPE cells and the P(f) for these cells was 9.8 x 10( -3) cm/s at 10 degrees C. CONCLUSIONS: The presence of AQP1 in human NPE cells suggests that it may have a role in the fluid flow across epithelial membranes. Water 79-84 aquaporin 1 (Colton blood group) Homo sapiens 74-78 10694901-8 2000 Osmotic water permeability (P( f)) measurements confirmed that functional AQP1 water channels are expressed in human NPE cells and the P(f) for these cells was 9.8 x 10( -3) cm/s at 10 degrees C. CONCLUSIONS: The presence of AQP1 in human NPE cells suggests that it may have a role in the fluid flow across epithelial membranes. Water 79-84 aquaporin 1 (Colton blood group) Homo sapiens 225-229 10692499-1 2000 Aquaporin-1 (AQP1) is a member of the membrane intrinsic protein (MIP) gene family and is known to provide pathways for water flux across cell membranes. Water 120-125 aquaporin 1 (Colton blood group) Homo sapiens 0-11 10692499-1 2000 Aquaporin-1 (AQP1) is a member of the membrane intrinsic protein (MIP) gene family and is known to provide pathways for water flux across cell membranes. Water 120-125 aquaporin 1 (Colton blood group) Homo sapiens 13-17 10692499-2 2000 We show here that cloned human AQP1 not only mediates water flux but also serves as a cGMP-gated ion channel. Water 54-59 aquaporin 1 (Colton blood group) Homo sapiens 31-35 10619865-1 2000 The mammalian lung expresses water channel aquaporin-1 (AQP1) in microvascular endothelia, AQP4 in airway epithelia, and AQP5 at the apical plasma membrane in type I cells of alveolar epithelia. Water 29-34 aquaporin 1 (Colton blood group) Homo sapiens 56-60 11045315-12 2000 Our results suggest that AQP-1 and AQP-4 may be important factors in water transport in patients undergoing CAPD. Water 69-74 aquaporin 1 (Colton blood group) Homo sapiens 25-30 10644652-6 2000 Several of the mammalian aquaporins (e.g., AQP1, AQP2, AQP4, and AQP5) appear to be highly selective for the passage of water, whereas others (recently termed aquaglyceroporins) also transport glycerol (e.g., AQP3 and AQP8) and even larger solutes (AQP9). Water 120-125 aquaporin 1 (Colton blood group) Homo sapiens 43-47 10235568-0 1999 Molecular identification and immunolocalization of the water channel protein aquaporin 1 in CBCECs. Water 55-60 aquaporin 1 (Colton blood group) Homo sapiens 77-88 10600556-1 1999 Aquaporin-1 is a water channel found in mammalian red blood cells that is responsible for high water permeability of its membrane. Water 17-22 aquaporin 1 (Colton blood group) Homo sapiens 0-11 10600556-1 1999 Aquaporin-1 is a water channel found in mammalian red blood cells that is responsible for high water permeability of its membrane. Water 95-100 aquaporin 1 (Colton blood group) Homo sapiens 0-11 10600556-6 1999 A pore found close to the center of the aquaporin-1 monomer is suggested to be the course of water flow with implications for the water selectivity. Water 93-98 aquaporin 1 (Colton blood group) Homo sapiens 40-51 10600556-6 1999 A pore found close to the center of the aquaporin-1 monomer is suggested to be the course of water flow with implications for the water selectivity. Water 130-135 aquaporin 1 (Colton blood group) Homo sapiens 40-51 10559675-0 1999 Aquaporin-1 is expressed by vascular smooth muscle cells and mediates rapid water transport across vascular cell membranes. Water 76-81 aquaporin 1 (Colton blood group) Homo sapiens 0-11 10559675-6 1999 Finally, by measuring the rate of change in cell size induced by changes in external osmolarity and demonstrating that water transport can be inhibited with mercuric chloride, we show that AQP-1 is responsible for water transport across human VSMC membranes. Water 119-124 aquaporin 1 (Colton blood group) Homo sapiens 189-194 10559675-6 1999 Finally, by measuring the rate of change in cell size induced by changes in external osmolarity and demonstrating that water transport can be inhibited with mercuric chloride, we show that AQP-1 is responsible for water transport across human VSMC membranes. Water 214-219 aquaporin 1 (Colton blood group) Homo sapiens 189-194 10414857-0 1999 Expression of aquaporin 1 (AQP1) water channels in human labial salivary glands. Water 33-38 aquaporin 1 (Colton blood group) Homo sapiens 14-25 10414857-0 1999 Expression of aquaporin 1 (AQP1) water channels in human labial salivary glands. Water 33-38 aquaporin 1 (Colton blood group) Homo sapiens 27-31 10518953-6 1999 Three-dimensional reconstruction of negatively stained lattices revealed the p42(1)2 packing arrangement that is also observed with the human erythrocyte water channel (AQP1). Water 154-159 aquaporin 1 (Colton blood group) Homo sapiens 169-173 10023655-0 1999 Expression of aquaporin-1 in a long-term peritoneal dialysis patient with impaired transcellular water transport. Water 97-102 aquaporin 1 (Colton blood group) Homo sapiens 14-25 10066454-2 1999 NaCl and D(+)-raffinose increased (2-2.5 fold) AQP-1 expression when medium osmolarity was 400 and 500 mOsm/kg.H2O. Water 111-114 aquaporin 1 (Colton blood group) Homo sapiens 47-52 10066454-5 1999 Furthermore, HRPTE cells increased (3-4 fold) AQP-1 expression when exposed to hyperosmolar Reno-60 and Hypaque-76 (diatrizoates, ionic) contrast agents at 400 and 500 mOsm/kg.H2O. Water 176-179 aquaporin 1 (Colton blood group) Homo sapiens 46-51 10066454-6 1999 Isosmolar (290 mOsm/kg H2O) Visipaque (iodixanol, non-ionic) at 10% (v/v) concentrations also increased AQP-1 expression, and 25% v/v of Visipaque rendered morphological alterations of HRPTE cells and a 3-fold increase in AQP-1 expression after 24h exposure. Water 23-26 aquaporin 1 (Colton blood group) Homo sapiens 104-109 10073616-3 1999 Aquaporin-1 (AQP1) is extremely abundant in the proximal tubule and descending thin limb, where it appears to provide the chief route for proximal nephron water reabsorption. Water 155-160 aquaporin 1 (Colton blood group) Homo sapiens 0-11 10073616-3 1999 Aquaporin-1 (AQP1) is extremely abundant in the proximal tubule and descending thin limb, where it appears to provide the chief route for proximal nephron water reabsorption. Water 155-160 aquaporin 1 (Colton blood group) Homo sapiens 13-17 10023655-1 1999 Aquaporin-1 (AQP1) has been claimed to be the molecular counterpart of the transcellular pathway for free-water movement across the peritoneum during peritoneal dialysis. Water 106-111 aquaporin 1 (Colton blood group) Homo sapiens 0-11 10023655-1 1999 Aquaporin-1 (AQP1) has been claimed to be the molecular counterpart of the transcellular pathway for free-water movement across the peritoneum during peritoneal dialysis. Water 106-111 aquaporin 1 (Colton blood group) Homo sapiens 13-17 10023655-2 1999 We report the case of a 67-year-old man, on peritoneal dialysis for 11 years, in whom ultrafiltration failure due to an abolition of the transcellular water transfer (documented by a loss of sodium sieving) was associated with an apparently normal expression of AQP1. Water 151-156 aquaporin 1 (Colton blood group) Homo sapiens 262-266 9916045-0 1999 Membrane dynamics of the water transport protein aquaporin-1 in intact human red cells. Water 25-30 aquaporin 1 (Colton blood group) Homo sapiens 49-60 9916045-1 1999 Aquaporin-1 (AQP1) is the prototype integral membrane protein water channel. Water 62-67 aquaporin 1 (Colton blood group) Homo sapiens 0-11 9916045-1 1999 Aquaporin-1 (AQP1) is the prototype integral membrane protein water channel. Water 62-67 aquaporin 1 (Colton blood group) Homo sapiens 13-17 10021464-1 1999 The mammalian lung expresses water channel aquaporin-1 (AQP1) in microvascular endothelia and aquaporin-4 (AQP4) in airway epithelia. Water 29-34 aquaporin 1 (Colton blood group) Homo sapiens 56-60 10872456-1 1999 The high water permeability characteristic of mammalian red cell membranes is now known to be caused by the protein AQP1. Water 9-14 aquaporin 1 (Colton blood group) Homo sapiens 116-120 9612221-9 1998 These studies demonstrate selective expression of AQP1, AQP3, AQP4, and AQP5 in distinct ocular epithelia, predicting specific roles for each in the complex network through which water movements occur in the eye. Water 179-184 aquaporin 1 (Colton blood group) Homo sapiens 50-54 9837877-3 1998 To determine the roles of lipid composition and the aquaporin 1 (AQP1) water channel in altering CO2 flux across membranes, we developed a fluorometric assay to measure CO2 entry into vesicles. Water 71-76 aquaporin 1 (Colton blood group) Homo sapiens 52-63 9837877-3 1998 To determine the roles of lipid composition and the aquaporin 1 (AQP1) water channel in altering CO2 flux across membranes, we developed a fluorometric assay to measure CO2 entry into vesicles. Water 71-76 aquaporin 1 (Colton blood group) Homo sapiens 65-69 9837877-6 1998 When AQP1 purified from human red blood cells was reconstituted into proteoliposomes, however, it increased water and CO2 permeabilities markedly. Water 108-113 aquaporin 1 (Colton blood group) Homo sapiens 5-9 9837877-9 1998 AQP1 clearly serves to increase CO2 permeation, likely through the water pore; under certain circumstances, gas permeation through membranes is protein-mediated. Water 67-72 aquaporin 1 (Colton blood group) Homo sapiens 0-4 9824541-4 1998 Aquaporin-1 is involved in water reabsorption in the kidney"s proximal tubules and the thin descending Henle"s loop, aqueous humor formation in eye, cerebrospinal fluid formation in brain, and airway hydration in lung. Water 27-32 aquaporin 1 (Colton blood group) Homo sapiens 0-11 9874275-1 1998 Aquaporin 1 (AQP1) is the archetypal member of a family of integral membrane proteins that function as water channels. Water 103-108 aquaporin 1 (Colton blood group) Homo sapiens 0-11 9874275-1 1998 Aquaporin 1 (AQP1) is the archetypal member of a family of integral membrane proteins that function as water channels. Water 103-108 aquaporin 1 (Colton blood group) Homo sapiens 13-17 9843718-3 1998 Immunofluorescence demonstrated that in isolated cells the Na+-K+-ATPase, Na+-K+-2Cl- cotransporter, and aquaporin 1 water channel remained localized to the brush border, whereas the Cl-/HCO-3 (anion) exchanger type 2 was confined to the basolateral membrane. Water 117-122 aquaporin 1 (Colton blood group) Homo sapiens 105-116 9822113-1 1998 Several aquaporin-type water channels are expressed in mammalian kidney and lung: AQP1 in lung microvessels and kidney proximal tubule, thin descending limb of Henle, and vasa recta; AQP2 in apical membrane of collecting duct epithelium; AQP3 and AQP4 in basolateral membranes of airway and collecting duct epithelium; and AQP5 in alveolar epithelium. Water 23-28 aquaporin 1 (Colton blood group) Homo sapiens 82-86 9480747-1 1998 Water channel aquaporin-1 (AQP1) is expressed in erythrocytes and various epithelia and endothelia. Water 0-5 aquaporin 1 (Colton blood group) Homo sapiens 14-25 9480747-4 1998 After butyrate-induced erythroid differentiation, AQP1 transcript expression increased strongly, producing water-permeable cells with plasma membrane localization of immunoreactive AQP1. Water 107-112 aquaporin 1 (Colton blood group) Homo sapiens 50-54 9497312-2 1998 Like the kidney, the eye contains multiple water channel proteins (aquaporins) that transport water through membranes, including two (AQP1 and AQP4) in the ciliary body, the site of aqueous humor production. Water 43-48 aquaporin 1 (Colton blood group) Homo sapiens 134-138 9497312-3 1998 However, because humans with defective AQP1 are phenotypically normal and because the ocular application of phorbol esters reduce intraocular pressure, we postulated that the water channel activity of AQP4 may be regulated by these agents. Water 175-180 aquaporin 1 (Colton blood group) Homo sapiens 39-43 9480747-1 1998 Water channel aquaporin-1 (AQP1) is expressed in erythrocytes and various epithelia and endothelia. Water 0-5 aquaporin 1 (Colton blood group) Homo sapiens 27-31 9453414-0 1998 The expression of water channels AQP1 and AQP2 in a large series of ADPKD kidneys. Water 18-23 aquaporin 1 (Colton blood group) Homo sapiens 33-37 9374641-1 1997 The aquaporin-1 (AQP1) water channel protein is expressed in multiple mammalian tissues by several different developmental programs; however, the genetic regulation is undefined. Water 23-28 aquaporin 1 (Colton blood group) Homo sapiens 4-15 9425633-0 1997 Purification and functional reconstitution of the human CHIP28 water channel expressed in Saccharomyces cerevisiae. Water 63-68 aquaporin 1 (Colton blood group) Homo sapiens 56-62 9425633-1 1997 The yeast Saccharomyces cerevisiae was used for heterologous expression of the human CHIP28 water Aquaporin-1 channel (Aquaporin-1). Water 92-97 aquaporin 1 (Colton blood group) Homo sapiens 85-91 9425633-1 1997 The yeast Saccharomyces cerevisiae was used for heterologous expression of the human CHIP28 water Aquaporin-1 channel (Aquaporin-1). Water 92-97 aquaporin 1 (Colton blood group) Homo sapiens 98-109 9425633-1 1997 The yeast Saccharomyces cerevisiae was used for heterologous expression of the human CHIP28 water Aquaporin-1 channel (Aquaporin-1). Water 92-97 aquaporin 1 (Colton blood group) Homo sapiens 119-130 9369468-15 1997 These results suggest that the structure of the aqueous pore of AQP3 resembles those of AQP1 and AQP2 and support the hypothesis that water and small molecules share a common pore in AQP3. Water 134-139 aquaporin 1 (Colton blood group) Homo sapiens 88-92 9374641-1 1997 The aquaporin-1 (AQP1) water channel protein is expressed in multiple mammalian tissues by several different developmental programs; however, the genetic regulation is undefined. Water 23-28 aquaporin 1 (Colton blood group) Homo sapiens 17-21 9176367-4 1997 DVR endothelium probably contains a "water-only" pathway most likely mediated by the aquaporin-1 (AQP1) water channel. Water 37-42 aquaporin 1 (Colton blood group) Homo sapiens 85-96 9299519-1 1997 Aquaporin 1 (AQP1), a six-transmembrane domain protein that functions as a water channel, is present in many fluid secreting and absorbing tissues such as kidney, brain, heart, and eye. Water 75-80 aquaporin 1 (Colton blood group) Homo sapiens 0-11 9299519-1 1997 Aquaporin 1 (AQP1), a six-transmembrane domain protein that functions as a water channel, is present in many fluid secreting and absorbing tissues such as kidney, brain, heart, and eye. Water 75-80 aquaporin 1 (Colton blood group) Homo sapiens 13-17 9299519-5 1997 In addition, our data reveal that atrial natriuretic peptide (ANP), a peptide hormone that plays an important role in the regulation of body fluid homeostasis, blocks the AQP1-mediated increase in water permeability. Water 197-202 aquaporin 1 (Colton blood group) Homo sapiens 171-175 9299519-6 1997 Incubation with 8-bromo-cAMP or direct 8-bromo-cAMP injection into oocytes expressing AQP1 cRNA significantly increased membrane permeability to water, suggesting that stimulation of AQP1 activity by AVP may involve a cAMP-dependent mechanism. Water 145-150 aquaporin 1 (Colton blood group) Homo sapiens 86-90 9299519-6 1997 Incubation with 8-bromo-cAMP or direct 8-bromo-cAMP injection into oocytes expressing AQP1 cRNA significantly increased membrane permeability to water, suggesting that stimulation of AQP1 activity by AVP may involve a cAMP-dependent mechanism. Water 145-150 aquaporin 1 (Colton blood group) Homo sapiens 183-187 9299519-7 1997 Regulation of water permeability by AVP and ANP has potential relevance to active water transport in a variety of tissues that express AQP1 including kidney, brain, and eye. Water 14-19 aquaporin 1 (Colton blood group) Homo sapiens 135-139 9299519-7 1997 Regulation of water permeability by AVP and ANP has potential relevance to active water transport in a variety of tissues that express AQP1 including kidney, brain, and eye. Water 82-87 aquaporin 1 (Colton blood group) Homo sapiens 135-139 9323711-12 1997 CONCLUSIONS: Our finding that aquaporin-1 mRNA is reproducibly induced in lung following CPB/HCA with 6 hr of reperfusion suggests an important role for the water channel in the setting of pulmonary edema. Water 157-162 aquaporin 1 (Colton blood group) Homo sapiens 30-41 9177354-2 1997 The archetypal aquaporin AQP1 is a partly glycosylated water-selective channel that is widely expressed in the plasma membranes of several water-permeable epithelial and endothelial cells. Water 55-60 aquaporin 1 (Colton blood group) Homo sapiens 25-29 9177354-2 1997 The archetypal aquaporin AQP1 is a partly glycosylated water-selective channel that is widely expressed in the plasma membranes of several water-permeable epithelial and endothelial cells. Water 139-144 aquaporin 1 (Colton blood group) Homo sapiens 25-29 9176367-4 1997 DVR endothelium probably contains a "water-only" pathway most likely mediated by the aquaporin-1 (AQP1) water channel. Water 37-42 aquaporin 1 (Colton blood group) Homo sapiens 98-102 9176367-4 1997 DVR endothelium probably contains a "water-only" pathway most likely mediated by the aquaporin-1 (AQP1) water channel. Water 104-109 aquaporin 1 (Colton blood group) Homo sapiens 85-96 9176367-4 1997 DVR endothelium probably contains a "water-only" pathway most likely mediated by the aquaporin-1 (AQP1) water channel. Water 104-109 aquaporin 1 (Colton blood group) Homo sapiens 98-102 9176368-0 1997 Evidence that aquaporin-1 mediates NaCl-induced water flux across descending vasa recta. Water 48-53 aquaporin 1 (Colton blood group) Homo sapiens 14-25 9176368-7 1997 We conclude that OMDVR water flux driven by NaCl gradients is most likely mediated by the AQP1 water channel and that NaCl and urea gradients drive water efflux in vivo by this route. Water 23-28 aquaporin 1 (Colton blood group) Homo sapiens 90-94 9176368-7 1997 We conclude that OMDVR water flux driven by NaCl gradients is most likely mediated by the AQP1 water channel and that NaCl and urea gradients drive water efflux in vivo by this route. Water 95-100 aquaporin 1 (Colton blood group) Homo sapiens 90-94 9176368-7 1997 We conclude that OMDVR water flux driven by NaCl gradients is most likely mediated by the AQP1 water channel and that NaCl and urea gradients drive water efflux in vivo by this route. Water 95-100 aquaporin 1 (Colton blood group) Homo sapiens 90-94 9095192-0 1997 Molecular design of aquaporin-1 water channel as revealed by electron crystallography. Water 32-37 aquaporin 1 (Colton blood group) Homo sapiens 20-31 9095192-1 1997 The electron crystallographic structure of the aquaporin-1 water channel, determined at approximately 6A, reveals that the protein has six transmembrane alpha-helices forming a trapezoid-like cylinder. Water 59-64 aquaporin 1 (Colton blood group) Homo sapiens 47-58 9096382-1 1997 A replication-deficient, recombinant adenovirus encoding human aquaporin-1 (hAQP1), the archetypal water channel, was constructed. Water 99-104 aquaporin 1 (Colton blood group) Homo sapiens 63-74 9360641-0 1997 Water channel AQP1, 3, and 4 in the human peritoneum and peritoneal dialysate. Water 0-5 aquaporin 1 (Colton blood group) Homo sapiens 14-18 9096382-1 1997 A replication-deficient, recombinant adenovirus encoding human aquaporin-1 (hAQP1), the archetypal water channel, was constructed. Water 99-104 aquaporin 1 (Colton blood group) Homo sapiens 76-81 8703203-3 1996 Recently, however, very strong evidence has been presented that the 28 kDa protein, CHIP28, found in the red cell membrane, is the locus of the water channel (see Agre et al., 1993). Water 144-149 aquaporin 1 (Colton blood group) Homo sapiens 84-90 9356672-1 1997 The recently identified molecular structure of the Colton blood group system is characterized by an amino acid substitution at position 45 (Colton a: alanine, Colton b: valine) of the archetypical water channel protein Aquaporin-1 (AQP1), which regulates water homeostasis in the erythrocyte membrane and in the proximal tubule of the nephron. Water 197-202 aquaporin 1 (Colton blood group) Homo sapiens 219-230 9356672-1 1997 The recently identified molecular structure of the Colton blood group system is characterized by an amino acid substitution at position 45 (Colton a: alanine, Colton b: valine) of the archetypical water channel protein Aquaporin-1 (AQP1), which regulates water homeostasis in the erythrocyte membrane and in the proximal tubule of the nephron. Water 197-202 aquaporin 1 (Colton blood group) Homo sapiens 232-236 8920898-1 1996 Aquaporin 1 is an integral membrane protein which functions as a water channel. Water 65-70 aquaporin 1 (Colton blood group) Homo sapiens 0-11 8921199-0 1996 A lectin screening method for membrane glycoproteins: application to the human CHIP28 water channel (AQP-1). Water 86-91 aquaporin 1 (Colton blood group) Homo sapiens 101-106 9000620-1 1996 Aquaporin-1 (AQP1) is an abundant protein in human erythrocyte membranes which functions as a specific and constitutively active water conducting pore. Water 129-134 aquaporin 1 (Colton blood group) Homo sapiens 0-11 9000620-1 1996 Aquaporin-1 (AQP1) is an abundant protein in human erythrocyte membranes which functions as a specific and constitutively active water conducting pore. Water 129-134 aquaporin 1 (Colton blood group) Homo sapiens 13-17 8703203-4 1996 CHIP28 transports water very rapidly but does not transport small nonelectrolytes such as urea. Water 18-23 aquaporin 1 (Colton blood group) Homo sapiens 0-6 8703203-11 1996 Thus, the conclusion on irreversible thermodynamic and other grounds that urea and water share a common channel is in disagreement with the view that CHIP28 provides the sole channel for water entrance into the cell. Water 187-192 aquaporin 1 (Colton blood group) Homo sapiens 150-156 8890563-9 1996 The gene for water channel of erythrocyte is designated as AQP1 and is one of gene family, MIP, consisting of 20 genes. Water 13-18 aquaporin 1 (Colton blood group) Homo sapiens 59-63 8928752-2 1996 This includes such examples as gramicidin A, the proximal tubule basolateral membrane, and the aquaporin 1 (CHIP28) water channel. Water 116-121 aquaporin 1 (Colton blood group) Homo sapiens 95-106 8760258-1 1996 Aquaporin-1 (AQP1), located in proximal tubules (PT) and descending thin limbs of Henle (DTL), and aquaporin-2 (AQP2), located in collecting ducts (CD), are channels involved in water transport across renal tubule epithelia. Water 178-183 aquaporin 1 (Colton blood group) Homo sapiens 0-11 8738333-6 1996 The procedure has been applied to the quantitation of a recently identified protein, aquaporin (CHIP28), assumed to be a major water channel in the red blood cell membrane. Water 127-132 aquaporin 1 (Colton blood group) Homo sapiens 96-102 8674648-0 1996 FTIR spectroscopic structural analysis of the CHIP28 water channel protein. Water 53-58 aquaporin 1 (Colton blood group) Homo sapiens 46-52 8576117-2 1996 The aquaporin-1 (AQP1) water transport protein contains a polymorphism corresponding to the Colton red blood cell antigens. Water 23-28 aquaporin 1 (Colton blood group) Homo sapiens 4-15 8576117-2 1996 The aquaporin-1 (AQP1) water transport protein contains a polymorphism corresponding to the Colton red blood cell antigens. Water 23-28 aquaporin 1 (Colton blood group) Homo sapiens 17-21 8576117-3 1996 To define the fraction of membrane water permeability mediated by AQP1, red cells were obtained from human kindreds with the rare Colton-null phenotype. Water 35-40 aquaporin 1 (Colton blood group) Homo sapiens 66-70 8576117-8 1996 AQP1 contributes approximately 64% (Pd = 1.5 x 10(-3) cm/s) of the total diffusional water permeability pathway, and lipid permeation apparently comprises approximately 23%. Water 85-90 aquaporin 1 (Colton blood group) Homo sapiens 0-4 8576117-9 1996 In contrast, AQP1 contributes > 85% (Pf = 19 x 10(-3) cm/s) of the total osmotic water permeability pathway, and lipid permeation apparently comprises only approximately 10%. Water 84-89 aquaporin 1 (Colton blood group) Homo sapiens 13-17 8772426-5 1996 The majority of molecular-level information about water-transporting mechanisms comes from studies on CHIP28, a 28-kDa glycoprotein that forms tetramers in membranes; each monomer contains six putative helical domains surrounding a central aqueous pathway and functions independently as a water-selective channel. Water 50-55 aquaporin 1 (Colton blood group) Homo sapiens 102-108 8772426-5 1996 The majority of molecular-level information about water-transporting mechanisms comes from studies on CHIP28, a 28-kDa glycoprotein that forms tetramers in membranes; each monomer contains six putative helical domains surrounding a central aqueous pathway and functions independently as a water-selective channel. Water 289-294 aquaporin 1 (Colton blood group) Homo sapiens 102-108 8928752-2 1996 This includes such examples as gramicidin A, the proximal tubule basolateral membrane, and the aquaporin 1 (CHIP28) water channel. Water 116-121 aquaporin 1 (Colton blood group) Homo sapiens 108-114 8928752-10 1996 This limiting condition corresponds to a water channel completely filled by water and may be applicable to the aquaporin 1 water channel. Water 41-46 aquaporin 1 (Colton blood group) Homo sapiens 111-122 8928752-10 1996 This limiting condition corresponds to a water channel completely filled by water and may be applicable to the aquaporin 1 water channel. Water 76-81 aquaporin 1 (Colton blood group) Homo sapiens 111-122 8928752-10 1996 This limiting condition corresponds to a water channel completely filled by water and may be applicable to the aquaporin 1 water channel. Water 76-81 aquaporin 1 (Colton blood group) Homo sapiens 111-122 8728163-5 1996 Water channels, like aquaporin-CHIP, could be the morphological equivalent of these pores. Water 0-5 aquaporin 1 (Colton blood group) Homo sapiens 21-35 8731978-7 1996 AQP-CHIP assembles into homotetramers in the plasma membrane and each CHIP monomer appears to form a functional water pore. Water 112-117 aquaporin 1 (Colton blood group) Homo sapiens 0-8 8569068-5 1995 The results indicate that CHIP28 transports water selectively, that CHIP28 monomers are assembled in membranes as tetramers, but that individual monomers function independently. Water 44-49 aquaporin 1 (Colton blood group) Homo sapiens 26-32 7589481-0 1995 Functional expression of the human CHIP28 water channel in a yeast secretory mutant. Water 42-47 aquaporin 1 (Colton blood group) Homo sapiens 35-41 7589481-1 1995 The temperature-sensitive Saccharomyces cerevisiae mutant strain NY17, deficient in the secretory pathway (sec6-4 mutation), is used for the heterologous expression of the human CHIP28 water channel. Water 185-190 aquaporin 1 (Colton blood group) Homo sapiens 178-184 7589481-3 1995 Immunodetection and water transport studies, directly made on the vesicles, showed that CHIP28 is highly expressed and active in the yeast membranes. Water 20-25 aquaporin 1 (Colton blood group) Homo sapiens 88-94 8569068-5 1995 The results indicate that CHIP28 transports water selectively, that CHIP28 monomers are assembled in membranes as tetramers, but that individual monomers function independently. Water 44-49 aquaporin 1 (Colton blood group) Homo sapiens 68-74 8569068-7 1995 Based on these data and recent electron crystallography results, a model for water transport is proposed in which water moves through narrow pores located within individual CHIP28 monomers. Water 77-82 aquaporin 1 (Colton blood group) Homo sapiens 173-179 8569068-7 1995 Based on these data and recent electron crystallography results, a model for water transport is proposed in which water moves through narrow pores located within individual CHIP28 monomers. Water 114-119 aquaporin 1 (Colton blood group) Homo sapiens 173-179 7552739-0 1995 The CHIP28 water channel visualized in ice by electron crystallography. Water 11-16 aquaporin 1 (Colton blood group) Homo sapiens 4-10 7552739-1 1995 Electron crystallography of frozen-hydrated two-dimensional crystals of deglycosylated human erythrocyte CHIP28 reveals an aqueous vestibule in each monomer leading to the water-selective channel that is enclosed by multiple transmembrane alpha-helices. Water 172-177 aquaporin 1 (Colton blood group) Homo sapiens 105-111 7552740-1 1995 Using cryo-electron microscopy we have determined a projection map of the structure of the water selective pore aquaporin-1. Water 91-96 aquaporin 1 (Colton blood group) Homo sapiens 112-123 7473422-7 1995 These results indicate that the erythrocyte and proximal tubule water channel, CHIP28, is not present in sperm membranes but that sperm membrane glucose transporters may have a secondary water channel function. Water 64-69 aquaporin 1 (Colton blood group) Homo sapiens 79-85 7473422-7 1995 These results indicate that the erythrocyte and proximal tubule water channel, CHIP28, is not present in sperm membranes but that sperm membrane glucose transporters may have a secondary water channel function. Water 187-192 aquaporin 1 (Colton blood group) Homo sapiens 79-85 7491270-1 1995 Permeabilities to glycerol and small non-electrolytes of three Aquaporin 1 CHIP (AQP1) water channels were measured in AQP1 cRNA-injected Xenopus laevis oocytes and in human AQP1 channels reconstituted in proteoliposomes. Water 87-92 aquaporin 1 (Colton blood group) Homo sapiens 119-123 7491270-8 1995 In AQP1 cRNA-injected oocytes and in proteoliposomes, the value of the glycerol reflection coefficient was 0.74-0.80, indicating that water and glycerol share the same pathway. Water 134-139 aquaporin 1 (Colton blood group) Homo sapiens 3-7 8590218-4 1995 There are constitutive water channels (aquaporin 1), which are involved in the bulk of water reabsorption in the kidney. Water 23-28 aquaporin 1 (Colton blood group) Homo sapiens 39-50 7539501-1 1995 Aquaporin CHIP, a 28 kDa channel forming protein, has been proposed to function as water channel in both erythrocyte and kidney proximal tubule. Water 83-88 aquaporin 1 (Colton blood group) Homo sapiens 0-14 7540052-4 1995 Together with the low activation energy of human spermatozoa for Lp, this suggests that CHIP28 water channel may be present in the plasma membrane of human spermatozoa. Water 95-100 aquaporin 1 (Colton blood group) Homo sapiens 88-94 7535000-2 1995 In proximal tubules and thin descending limbs of normal kidneys, the high transepithelial water permeability of these segments is due to the presence of the water channel protein, aquaporin-CHIP (AQP-CHIP, i.e., AQP-1). Water 90-95 aquaporin 1 (Colton blood group) Homo sapiens 180-194 7535000-2 1995 In proximal tubules and thin descending limbs of normal kidneys, the high transepithelial water permeability of these segments is due to the presence of the water channel protein, aquaporin-CHIP (AQP-CHIP, i.e., AQP-1). Water 90-95 aquaporin 1 (Colton blood group) Homo sapiens 196-204 7535000-2 1995 In proximal tubules and thin descending limbs of normal kidneys, the high transepithelial water permeability of these segments is due to the presence of the water channel protein, aquaporin-CHIP (AQP-CHIP, i.e., AQP-1). Water 157-162 aquaporin 1 (Colton blood group) Homo sapiens 180-194 7535000-2 1995 In proximal tubules and thin descending limbs of normal kidneys, the high transepithelial water permeability of these segments is due to the presence of the water channel protein, aquaporin-CHIP (AQP-CHIP, i.e., AQP-1). Water 157-162 aquaporin 1 (Colton blood group) Homo sapiens 196-204 7532004-9 1995 In reconstituted proteoliposomes, deglycosylated CHIP28 had a single channel water permeability (pf) of 3.1 x 10(-14) cm3/s (10 degrees C), not different from that of 3.2 x 10(-14) cm3/s for native CHIP28. Water 77-82 aquaporin 1 (Colton blood group) Homo sapiens 49-55 8590218-4 1995 There are constitutive water channels (aquaporin 1), which are involved in the bulk of water reabsorption in the kidney. Water 87-92 aquaporin 1 (Colton blood group) Homo sapiens 39-50 7558688-8 1995 Osmotic transport of H2O through specific H2O channels such as CHIP 28 is hydraulic if the pore is impermeable to the solute and diffusive if the pore is permeable. Water 21-24 aquaporin 1 (Colton blood group) Homo sapiens 63-70 8542028-1 1995 The recent identification of the red cell water transporter (AQP1) has led to the identification of the "aquaporins", a new class of membrane proteins which function as water-selective transport proteins and are involved in many physiological processes. Water 42-47 aquaporin 1 (Colton blood group) Homo sapiens 61-65 7524655-0 1994 Projection structure of the CHIP28 water channel in lipid bilayer membranes at 12-A resolution. Water 35-40 aquaporin 1 (Colton blood group) Homo sapiens 28-34 7536292-6 1994 It may correspond to CHIP28, the water channel of the human erythrocyte. Water 33-38 aquaporin 1 (Colton blood group) Homo sapiens 21-27 7524655-1 1994 Osmotic water transport across plasma membranes in erythrocytes and several epithelial cell types is facilitated by CHIP28, a water-selective membrane channel protein. Water 8-13 aquaporin 1 (Colton blood group) Homo sapiens 116-122 7526855-0 1994 Cloning of a novel cDNA homologous to CHIP28 water channel from ocular ciliary epithelium. Water 45-50 aquaporin 1 (Colton blood group) Homo sapiens 38-44 7530838-1 1994 The aquaporin CHIP, AQP-CHIP, is a 28-kDa integral membrane protein that functions as a water channel in kidney and red blood cells. Water 88-93 aquaporin 1 (Colton blood group) Homo sapiens 20-28 7530838-10 1994 Further, this study provides strong evidence that AQP-CHIP is an endothelial cell water channel found within salivary gland tissue which may contribute to water permeability in the capillary beds. Water 82-87 aquaporin 1 (Colton blood group) Homo sapiens 50-58 7530838-10 1994 Further, this study provides strong evidence that AQP-CHIP is an endothelial cell water channel found within salivary gland tissue which may contribute to water permeability in the capillary beds. Water 155-160 aquaporin 1 (Colton blood group) Homo sapiens 50-58 7504987-0 1994 The human gene for water channel aquaporin 1 (AQP1) is localized on chromosome 7p15-->p14. Water 19-24 aquaporin 1 (Colton blood group) Homo sapiens 33-44 7521540-1 1994 The gene aquaporin-1 encodes channel-forming integral protein (CHIP), a member of a large family of water transporters found throughout nature. Water 100-105 aquaporin 1 (Colton blood group) Homo sapiens 9-20 7524336-1 1994 The water channel CHIP28 accounts for the high water permeability of proximal tubules and thin descending limbs of Henle; a homologous water channel, WCH-CD, in the apical membrane of collecting duct principal cells, may be the vasopressin-sensitive water channel. Water 4-9 aquaporin 1 (Colton blood group) Homo sapiens 18-24 7524336-1 1994 The water channel CHIP28 accounts for the high water permeability of proximal tubules and thin descending limbs of Henle; a homologous water channel, WCH-CD, in the apical membrane of collecting duct principal cells, may be the vasopressin-sensitive water channel. Water 47-52 aquaporin 1 (Colton blood group) Homo sapiens 18-24 7524336-1 1994 The water channel CHIP28 accounts for the high water permeability of proximal tubules and thin descending limbs of Henle; a homologous water channel, WCH-CD, in the apical membrane of collecting duct principal cells, may be the vasopressin-sensitive water channel. Water 47-52 aquaporin 1 (Colton blood group) Homo sapiens 18-24 7524336-1 1994 The water channel CHIP28 accounts for the high water permeability of proximal tubules and thin descending limbs of Henle; a homologous water channel, WCH-CD, in the apical membrane of collecting duct principal cells, may be the vasopressin-sensitive water channel. Water 47-52 aquaporin 1 (Colton blood group) Homo sapiens 18-24 7531521-3 1994 AQP CHIP is localized to the luminal and contraluminal membranes of the proximal tubule and descending thin limb cells, i.e., in tubule segments that exhibit a constitutive high permeability to water that is insensitive to vasopressin. Water 194-199 aquaporin 1 (Colton blood group) Homo sapiens 0-8 7520041-1 1994 Two recently cloned water channels, CHIP28 and WCH-CD, are homologous to MIP26, an integral membrane channel-forming protein found in lens fiber plasma membranes. Water 20-25 aquaporin 1 (Colton blood group) Homo sapiens 36-42 7521882-3 1994 The red cell water channel-forming integral protein (Aquaporin CHIP) is a homotetramer with only one N-glycosylated subunit, however no CHIP-associated blood group antigens have yet been identified. Water 13-18 aquaporin 1 (Colton blood group) Homo sapiens 53-67 7528593-8 1994 A correlation between the content in CHIP 28 and the relative water permeability among RBC from different vertebrate species was attempted. Water 62-67 aquaporin 1 (Colton blood group) Homo sapiens 37-44 7529179-1 1994 Aquaporin-CHIP, a 28 kDa channel forming protein already referred to as CHIP28, has been identified as the water channel in red blood cells as well as in mammalian renal tubule cells. Water 107-112 aquaporin 1 (Colton blood group) Homo sapiens 0-14 7529179-1 1994 Aquaporin-CHIP, a 28 kDa channel forming protein already referred to as CHIP28, has been identified as the water channel in red blood cells as well as in mammalian renal tubule cells. Water 107-112 aquaporin 1 (Colton blood group) Homo sapiens 72-78 7529179-3 1994 The present study investigates the possible presence of CHIP28-like proteins in amphibian urinary bladder, where the presence of water channels has been postulated. Water 129-134 aquaporin 1 (Colton blood group) Homo sapiens 56-62 7504987-0 1994 The human gene for water channel aquaporin 1 (AQP1) is localized on chromosome 7p15-->p14. Water 19-24 aquaporin 1 (Colton blood group) Homo sapiens 46-50 7504987-1 1994 The chromosomal localization of the gene encoding aquaporin 1 (previously called CHIP28), which acts as a water channel in erythrocytes and in the renal proximal tubules and descending limbs of Henle, was determined. Water 106-111 aquaporin 1 (Colton blood group) Homo sapiens 50-61 7504987-1 1994 The chromosomal localization of the gene encoding aquaporin 1 (previously called CHIP28), which acts as a water channel in erythrocytes and in the renal proximal tubules and descending limbs of Henle, was determined. Water 106-111 aquaporin 1 (Colton blood group) Homo sapiens 81-87 8218257-0 1993 Nonpolar environment of tryptophans in erythrocyte water channel CHIP28 determined by fluorescence quenching. Water 51-56 aquaporin 1 (Colton blood group) Homo sapiens 65-71 8218257-1 1993 CHIP28 is an abundant water-transporting protein in erythrocytes, kidney proximal tubule, and other fluid-transporting tissues. Water 22-27 aquaporin 1 (Colton blood group) Homo sapiens 0-6 8218257-3 1993 Functional analysis showed that CHIP28 water permeability was not affected by the polar quenchers iodide and acrylamide nor the nonpolar n-anthroyloxy fatty acids (n-AF). Water 39-44 aquaporin 1 (Colton blood group) Homo sapiens 32-38 7693713-1 1993 Channel forming integral protein of 28 kD (CHIP28) functions as a water channel in erythrocytes, kidney proximal tubule and thin descending limb of Henle. Water 66-71 aquaporin 1 (Colton blood group) Homo sapiens 43-49 7693713-3 1993 Liposomes reconstituted with HPLC-purified CHIP28 from human erythrocytes had a high osmotic water permeability (Pf0.04 cm/s) that was inhibited by HgCl2. Water 93-98 aquaporin 1 (Colton blood group) Homo sapiens 43-49 7693713-10 1993 These results provide a morphological signature for CHIP28 water channels and evidence for a tetrameric assembly of CHIP28 monomers in reconstituted proteoliposomes and cell membranes. Water 59-64 aquaporin 1 (Colton blood group) Homo sapiens 52-58 7694481-0 1993 Aquaporin CHIP: the archetypal molecular water channel. Water 41-46 aquaporin 1 (Colton blood group) Homo sapiens 0-14 8340403-2 1993 Aquaporin-CHIP is the first known molecular water channel. Water 44-49 aquaporin 1 (Colton blood group) Homo sapiens 0-14 8346245-2 1993 The aquaporin CHIP (channel-forming integral membrane protein of 28 kDa), a molecular water channel, is abundant in erythrocytes and water-permeable segments of the nephron. Water 86-91 aquaporin 1 (Colton blood group) Homo sapiens 20-71 8346245-2 1993 The aquaporin CHIP (channel-forming integral membrane protein of 28 kDa), a molecular water channel, is abundant in erythrocytes and water-permeable segments of the nephron. Water 133-138 aquaporin 1 (Colton blood group) Homo sapiens 20-71 7859027-7 1993 Second is the elucidation of several important protein structures via complementary DNA cloning, including the arginine vasopressin V1 and V2 receptors, several organic osmolyte transporters, and the CHIP28 water channel. Water 207-212 aquaporin 1 (Colton blood group) Homo sapiens 200-206 8508761-4 1993 Similar results were obtained with the homologous human erythrocyte protein CHIP28, recently identified as the erythrocyte water channel. Water 123-128 aquaporin 1 (Colton blood group) Homo sapiens 76-82 1510932-0 1992 Reconstitution of functional water channels in liposomes containing purified red cell CHIP28 protein. Water 29-34 aquaporin 1 (Colton blood group) Homo sapiens 86-92 1526967-0 1992 Functional reconstitution of the isolated erythrocyte water channel CHIP28. Water 54-59 aquaporin 1 (Colton blood group) Homo sapiens 68-74 1526967-6 1992 We report direct evidence that CHIP28 is the erythrocyte water channel. Water 57-62 aquaporin 1 (Colton blood group) Homo sapiens 31-37 1526967-12 1992 These data establish a procedure to reconstitute functional water channels into liposomes and demonstrate that CHIP28 is the erythrocyte water channel. Water 60-65 aquaporin 1 (Colton blood group) Homo sapiens 111-117 1526967-12 1992 These data establish a procedure to reconstitute functional water channels into liposomes and demonstrate that CHIP28 is the erythrocyte water channel. Water 137-142 aquaporin 1 (Colton blood group) Homo sapiens 111-117 1510932-7 1992 The magnitude of CHIP28-mediated water flux (11.7 x 10(-14) cm3/s per CHIP28) corresponds to the known Pf of intact RBCs. Water 33-38 aquaporin 1 (Colton blood group) Homo sapiens 17-23 1510932-7 1992 The magnitude of CHIP28-mediated water flux (11.7 x 10(-14) cm3/s per CHIP28) corresponds to the known Pf of intact RBCs. Water 33-38 aquaporin 1 (Colton blood group) Homo sapiens 70-76 1510932-8 1992 These results demonstrate that CHIP28 protein functions as a molecular water channel and also indicate that CHIP28 is responsible for most transmembrane water movement in RBCs. Water 71-76 aquaporin 1 (Colton blood group) Homo sapiens 31-37 1510932-8 1992 These results demonstrate that CHIP28 protein functions as a molecular water channel and also indicate that CHIP28 is responsible for most transmembrane water movement in RBCs. Water 71-76 aquaporin 1 (Colton blood group) Homo sapiens 108-114 1510932-8 1992 These results demonstrate that CHIP28 protein functions as a molecular water channel and also indicate that CHIP28 is responsible for most transmembrane water movement in RBCs. Water 153-158 aquaporin 1 (Colton blood group) Homo sapiens 31-37 1510932-8 1992 These results demonstrate that CHIP28 protein functions as a molecular water channel and also indicate that CHIP28 is responsible for most transmembrane water movement in RBCs. Water 153-158 aquaporin 1 (Colton blood group) Homo sapiens 108-114 33807998-3 2021 Aquaporin 1 (AQP1), as component of transmembrane-water-channel family proteins, has been documented in different human tumors and, recently, also in ovarian carcinoma. Water 50-55 aquaporin 1 (Colton blood group) Homo sapiens 0-11 33811938-4 2021 Recent studies in animal models of hepatocellular cholestasis show that the hepatic delivery of AdhAQP1, an adenovector encoding for the archetypical water channel human aquaporin-1 (hAQP1), improves bile secretion and restores to normal the elevated serum bile salt levels. Water 150-155 aquaporin 1 (Colton blood group) Homo sapiens 170-181 33811938-4 2021 Recent studies in animal models of hepatocellular cholestasis show that the hepatic delivery of AdhAQP1, an adenovector encoding for the archetypical water channel human aquaporin-1 (hAQP1), improves bile secretion and restores to normal the elevated serum bile salt levels. Water 150-155 aquaporin 1 (Colton blood group) Homo sapiens 98-103 33811938-5 2021 AdhAQP1-transduced hepatocytes show that the canalicularly-expressed hAQP1 not only enhances osmotic membrane water permeability but also induces the transport activities of BSEP/ABCB11 and MRP2/ABCC2 by redistribution in canalicular cholesterol-rich microdomains likely through interactions with the cholesterol-binding protein caveolin-1. Water 110-115 aquaporin 1 (Colton blood group) Homo sapiens 2-7 33777930-4 2021 Aquaporin (AQP) 1, 3, and 5 are water channels that contribute to the progression of esophageal squamous cell carcinoma (ESCC) and GC. Water 32-37 aquaporin 1 (Colton blood group) Homo sapiens 0-27 33807998-3 2021 Aquaporin 1 (AQP1), as component of transmembrane-water-channel family proteins, has been documented in different human tumors and, recently, also in ovarian carcinoma. Water 50-55 aquaporin 1 (Colton blood group) Homo sapiens 13-17 32891005-12 2020 Most notably, the expression of the aquaporin family of genes (e.g. AQP1 and AQP9) were found to be significantly higher in the placentas of active women suggesting an adaptive response for the transport of water and glycerol in this population. Water 207-212 aquaporin 1 (Colton blood group) Homo sapiens 68-72 34627746-6 2022 AQP1 is mainly a water channel and thus is thought to be involved in the response to hyper-osmotic stress by efflux of water during hyperglycemia. Water 17-22 aquaporin 1 (Colton blood group) Homo sapiens 0-4 34627746-6 2022 AQP1 is mainly a water channel and thus is thought to be involved in the response to hyper-osmotic stress by efflux of water during hyperglycemia. Water 119-124 aquaporin 1 (Colton blood group) Homo sapiens 0-4 34686053-0 2021 Influence of water models on water movement through AQP1. Water 13-18 aquaporin 1 (Colton blood group) Homo sapiens 52-56 34830416-0 2021 Aquaporin-1 Facilitates Transmesothelial Water Permeability: In Vitro and Ex Vivo Evidence and Possible Implications in Peritoneal Dialysis. Water 41-46 aquaporin 1 (Colton blood group) Homo sapiens 0-11 34830416-1 2021 We previously showed that mesothelial cells in human peritoneum express the water channel aquaporin 1 (AQP1) at the plasma membrane, suggesting that, although in a non-physiological context, it may facilitate osmotic water exchange during peritoneal dialysis (PD). Water 76-81 aquaporin 1 (Colton blood group) Homo sapiens 103-107 34830416-1 2021 We previously showed that mesothelial cells in human peritoneum express the water channel aquaporin 1 (AQP1) at the plasma membrane, suggesting that, although in a non-physiological context, it may facilitate osmotic water exchange during peritoneal dialysis (PD). Water 217-222 aquaporin 1 (Colton blood group) Homo sapiens 103-107 34830416-8 2021 Real-time transmesothelial water flux, in response to an increase of osmolarity in the apical solution, indicated that, in the presence of AQP1, the rate of TEA+ dilution was up to four-fold higher than in its absence. Water 27-32 aquaporin 1 (Colton blood group) Homo sapiens 139-143 34914911-3 2022 In this study, we made an attempt to elucidate the molecular mechanism of water transportation in AQP1 from walking catfish (Clarias batrachus), a model species capable of breathing in air and inhabits in challenging environments. Water 74-79 aquaporin 1 (Colton blood group) Homo sapiens 98-102 34686053-0 2021 Influence of water models on water movement through AQP1. Water 29-34 aquaporin 1 (Colton blood group) Homo sapiens 52-56 34686053-6 2021 We present a numerical study of water diffusion through AQP1 comparing three water models: TIP3P, OPC, and TIP4P/2005. Water 32-37 aquaporin 1 (Colton blood group) Homo sapiens 56-60 34686053-6 2021 We present a numerical study of water diffusion through AQP1 comparing three water models: TIP3P, OPC, and TIP4P/2005. Water 77-82 aquaporin 1 (Colton blood group) Homo sapiens 56-60 35151337-13 2022 CONCLUSIONS: Apoptotic changes and altered AQP-1 expression may contribute to CPEC dysfunction and subsequently reduce cerebrospinal fluid production, affecting the water homeostasis in the brains of patients with CM. Water 165-170 aquaporin 1 (Colton blood group) Homo sapiens 43-48 34670044-2 2021 Variants in AQP1, the gene that encodes the archetypal water channel aquaporin-1, may contribute to that variability. Water 55-60 aquaporin 1 (Colton blood group) Homo sapiens 12-16 35453560-0 2022 Oxidative Stress-Induced Alterations of Cellular Localization and Expression of Aquaporin 1 Lead to Defected Water Transport upon Peritoneal Fibrosis. Water 109-114 aquaporin 1 (Colton blood group) Homo sapiens 80-91 35453560-6 2022 Functional interference of aquaporin 1 on free water transport would result in PD failure in patients. Water 47-52 aquaporin 1 (Colton blood group) Homo sapiens 27-38 34532317-8 2021 The IL-6-mediated enhanced osmotic sensitivity of RA-FLS likely involves NKCC1 and aquaporin-1, which mainly constitute the volume-associated ion transporter and water channel elements. Water 162-167 aquaporin 1 (Colton blood group) Homo sapiens 83-94 34532317-9 2021 These results suggest that RA-FLS provide enhanced electrolytes and concomitant water movement through NKCC1 and aquaporin-1, thereby inducing cellular swelling ultimately resulting in cytotoxic edema. Water 80-85 aquaporin 1 (Colton blood group) Homo sapiens 113-124 33558238-5 2021 Proteomics analysis was used to reveal propranolol-mediated protein alteration correlating with tumor growth inhibition, and Aquaporin-1 (AQP1), a water channel modulated in tumor cell migration and invasion, was identified. Water 147-152 aquaporin 1 (Colton blood group) Homo sapiens 125-136 34017100-4 2021 We report a class of biomimetic, helically folded pore-forming polymeric foldamers that can serve as long-sought-after highly selective ultrafast water-conducting channels with performance exceeding those of AQPs (1.1 x 1010 water molecules per second for AQP1), with high water-over-monovalent-ion transport selectivity (~108 water molecules over Cl- ion) conferred by the modularly tunable hydrophobicity of the interior pore surface. Water 146-151 aquaporin 1 (Colton blood group) Homo sapiens 256-260 34017100-4 2021 We report a class of biomimetic, helically folded pore-forming polymeric foldamers that can serve as long-sought-after highly selective ultrafast water-conducting channels with performance exceeding those of AQPs (1.1 x 1010 water molecules per second for AQP1), with high water-over-monovalent-ion transport selectivity (~108 water molecules over Cl- ion) conferred by the modularly tunable hydrophobicity of the interior pore surface. Water 225-230 aquaporin 1 (Colton blood group) Homo sapiens 256-260 34017100-4 2021 We report a class of biomimetic, helically folded pore-forming polymeric foldamers that can serve as long-sought-after highly selective ultrafast water-conducting channels with performance exceeding those of AQPs (1.1 x 1010 water molecules per second for AQP1), with high water-over-monovalent-ion transport selectivity (~108 water molecules over Cl- ion) conferred by the modularly tunable hydrophobicity of the interior pore surface. Water 225-230 aquaporin 1 (Colton blood group) Homo sapiens 256-260 34017100-4 2021 We report a class of biomimetic, helically folded pore-forming polymeric foldamers that can serve as long-sought-after highly selective ultrafast water-conducting channels with performance exceeding those of AQPs (1.1 x 1010 water molecules per second for AQP1), with high water-over-monovalent-ion transport selectivity (~108 water molecules over Cl- ion) conferred by the modularly tunable hydrophobicity of the interior pore surface. Water 225-230 aquaporin 1 (Colton blood group) Homo sapiens 256-260 34017100-5 2021 The best-performing AWC reported here delivers water transport at an exceptionally high rate, namely, 2.5 times that of AQP1, while concurrently rejecting salts (NaCl and KCl) and even protons. Water 47-52 aquaporin 1 (Colton blood group) Homo sapiens 120-124 33980862-2 2021 In TNBC, Aquaporin 1 (AQP1), a water-transporting transmembrane protein, is aberrantly enriched in cytoplasm and causes tumor cell death evasion. Water 31-36 aquaporin 1 (Colton blood group) Homo sapiens 9-20 33980862-2 2021 In TNBC, Aquaporin 1 (AQP1), a water-transporting transmembrane protein, is aberrantly enriched in cytoplasm and causes tumor cell death evasion. Water 31-36 aquaporin 1 (Colton blood group) Homo sapiens 22-26 33558238-5 2021 Proteomics analysis was used to reveal propranolol-mediated protein alteration correlating with tumor growth inhibition, and Aquaporin-1 (AQP1), a water channel modulated in tumor cell migration and invasion, was identified. Water 147-152 aquaporin 1 (Colton blood group) Homo sapiens 138-142 33644043-0 2021 AQP1 Is Up-Regulated by Hypoxia and Leads to Increased Cell Water Permeability, Motility, and Migration in Neuroblastoma. Water 60-65 aquaporin 1 (Colton blood group) Homo sapiens 0-4 33644043-1 2021 The water channel aquaporin 1 (AQP1) has been implicated in tumor progression and metastasis. Water 4-9 aquaporin 1 (Colton blood group) Homo sapiens 31-35 33644043-2 2021 It is hypothesized that AQP1 expression can facilitate the transmembrane water transport leading to changes in cell structure that promote migration. Water 73-78 aquaporin 1 (Colton blood group) Homo sapiens 24-28 33361042-7 2020 The results of the reverse transcriptase polymerase chain reaction, Western blot, and immunohistochemical staining confirmed the expression of AQP-1, a kind of transmembrane protein that mainly distributed in the membranes of pulmonary cells and contributed to maintain water balance in the body by interacting with tumor necrosis factor-alpha (TNF-alpha), is negatively associated with APALI. Water 270-275 aquaporin 1 (Colton blood group) Homo sapiens 143-148 32154567-2 2021 Aquaporin 1 (AQP1) is a membrane water channel protein belonging to the AQP family. Water 33-38 aquaporin 1 (Colton blood group) Homo sapiens 0-11 32154567-2 2021 Aquaporin 1 (AQP1) is a membrane water channel protein belonging to the AQP family. Water 33-38 aquaporin 1 (Colton blood group) Homo sapiens 13-17 33125833-2 2021 AQP1 helps mediate the cellular response to osmotic stress and tissue water permeability. Water 70-75 aquaporin 1 (Colton blood group) Homo sapiens 0-4 33911740-1 2020 Background: Aquaporin 1 (AQP1) is a transmembrane channel protein that allows rapid transposition of water and gases, in recent discoveries of AQP1 function involve cell proliferation, differentiation, wound healing, inflammation and infection in different cell types, suggesting that AQP1 plays key roles in diverse biologic process. Water 101-106 aquaporin 1 (Colton blood group) Homo sapiens 12-23 32275985-5 2020 (2015) showed that aortic ECs express the water channel protein aquaporin-1 (AQP1) and the transEC (deltaP) portion of the transmural (DeltaP) pressure difference drives, in parallel, water across AQP1s and plasma across interEC junctions. Water 42-47 aquaporin 1 (Colton blood group) Homo sapiens 64-75 32275985-5 2020 (2015) showed that aortic ECs express the water channel protein aquaporin-1 (AQP1) and the transEC (deltaP) portion of the transmural (DeltaP) pressure difference drives, in parallel, water across AQP1s and plasma across interEC junctions. Water 42-47 aquaporin 1 (Colton blood group) Homo sapiens 77-81 32275985-5 2020 (2015) showed that aortic ECs express the water channel protein aquaporin-1 (AQP1) and the transEC (deltaP) portion of the transmural (DeltaP) pressure difference drives, in parallel, water across AQP1s and plasma across interEC junctions. Water 184-189 aquaporin 1 (Colton blood group) Homo sapiens 64-75 32275985-5 2020 (2015) showed that aortic ECs express the water channel protein aquaporin-1 (AQP1) and the transEC (deltaP) portion of the transmural (DeltaP) pressure difference drives, in parallel, water across AQP1s and plasma across interEC junctions. Water 184-189 aquaporin 1 (Colton blood group) Homo sapiens 77-81 32275985-6 2020 Since the lumen is isotonic, selective AQP1-mediated water flow should quickly render the ECs" lumen side hypertonic and the SI hypotonic; resulting transEC oncotic pressure differences, deltapi, should oppose deltaP and quickly halt transEC flow. Water 53-58 aquaporin 1 (Colton blood group) Homo sapiens 39-43 32434851-1 2020 Aquaporin-1 (AQP1) dual water and ion channels enhance migration and invasion when upregulated in leading edges of certain classes of cancer cells. Water 24-29 aquaporin 1 (Colton blood group) Homo sapiens 0-11 32434851-1 2020 Aquaporin-1 (AQP1) dual water and ion channels enhance migration and invasion when upregulated in leading edges of certain classes of cancer cells. Water 24-29 aquaporin 1 (Colton blood group) Homo sapiens 13-17 32576929-1 2020 Aquaporins (AQP) are not only water channel protein, but also potential prognostic indicator and therapeutic target for rectal cancer. Water 30-35 aquaporin 1 (Colton blood group) Homo sapiens 12-15 33077138-2 2020 AQP1, AQP3 and AQP5 are isoforms of aquaporin known to aid in transepithelial water movement. Water 78-83 aquaporin 1 (Colton blood group) Homo sapiens 0-4 33911740-1 2020 Background: Aquaporin 1 (AQP1) is a transmembrane channel protein that allows rapid transposition of water and gases, in recent discoveries of AQP1 function involve cell proliferation, differentiation, wound healing, inflammation and infection in different cell types, suggesting that AQP1 plays key roles in diverse biologic process. Water 101-106 aquaporin 1 (Colton blood group) Homo sapiens 25-29 33911740-1 2020 Background: Aquaporin 1 (AQP1) is a transmembrane channel protein that allows rapid transposition of water and gases, in recent discoveries of AQP1 function involve cell proliferation, differentiation, wound healing, inflammation and infection in different cell types, suggesting that AQP1 plays key roles in diverse biologic process. Water 101-106 aquaporin 1 (Colton blood group) Homo sapiens 143-147 33911740-1 2020 Background: Aquaporin 1 (AQP1) is a transmembrane channel protein that allows rapid transposition of water and gases, in recent discoveries of AQP1 function involve cell proliferation, differentiation, wound healing, inflammation and infection in different cell types, suggesting that AQP1 plays key roles in diverse biologic process. Water 101-106 aquaporin 1 (Colton blood group) Homo sapiens 143-147 32063362-4 2020 Human lens epithelial cells expressing AQP1, AQP5 and AQP8, when treated with 50 muM HgCl2 water channel inhibitor showed a significant reduction in H2O2 transport. Water 91-96 aquaporin 1 (Colton blood group) Homo sapiens 39-43 32373535-1 2020 Background: Aquaporin 1 (AQP-1), a transmembrane water channel protein, has been proven to involve in many diseases" progression and prognosis. Water 49-54 aquaporin 1 (Colton blood group) Homo sapiens 12-23 32373535-1 2020 Background: Aquaporin 1 (AQP-1), a transmembrane water channel protein, has been proven to involve in many diseases" progression and prognosis. Water 49-54 aquaporin 1 (Colton blood group) Homo sapiens 25-30 33997172-3 2021 The expression of AQP-1, -3, -4, -5, -8 and -9 were found in the digestive system, where these six AQP isoforms serve essential roles including mediating the transmembrane water transport and regulating the secretion of gastrointestinal (GI) fluids, consequently facilitating the digestion and absorption of GI contents. Water 172-177 aquaporin 1 (Colton blood group) Homo sapiens 18-46 32242084-7 2020 Water efflux through aquaporin 1 and activation of protein kinase C via specific G protein-coupled receptors are essential to the pressure-induced transient activation of the Ras/ERK pathway. Water 0-5 aquaporin 1 (Colton blood group) Homo sapiens 21-32 31521632-7 2020 Overall, we conclude that AtPIP2;4, SoPIP2;1 and hAQP1 are all transporters of both H2O and H2O2, but have different efficiencies for various specificities. Water 84-87 aquaporin 1 (Colton blood group) Homo sapiens 49-54 32612811-2 2020 In this study, we examined the accuracies of two popular water models, TIP3P and TIP4P, in the molecular dynamics simulations of erythrocyte aquaporins (AQP1 and AQP3). Water 57-62 aquaporin 1 (Colton blood group) Homo sapiens 153-157 32066904-6 2020 Furthermore, water permeation through aquaporin-1 mediates the EV deformability, which further supports EV transport in hydrogels and a decellularized matrix. Water 13-18 aquaporin 1 (Colton blood group) Homo sapiens 38-49 31682170-2 2020 In human kidneys, nine aquaporins (AQPs), including AQP1-8 and AQP11, have been found and are differentially expressed along the renal tubules and collecting ducts with distinct and critical roles in the regulation of body water homeostasis and urine concentration. Water 223-228 aquaporin 1 (Colton blood group) Homo sapiens 52-58 31676353-1 2020 Water influx through aquaporin-1 (AQP-1) has been linked to the ability of different cell types to migrate, and therefore plays an important part in processes like metastasis and angiogenesis. Water 0-5 aquaporin 1 (Colton blood group) Homo sapiens 21-32 31676353-1 2020 Water influx through aquaporin-1 (AQP-1) has been linked to the ability of different cell types to migrate, and therefore plays an important part in processes like metastasis and angiogenesis. Water 0-5 aquaporin 1 (Colton blood group) Homo sapiens 34-39 31477744-1 2019 Aquaporin-1 (AQP1) has been proposed as a dual water and cation channel that when upregulated in cancers enhances cell migration rates; however, the mechanism remains unknown. Water 47-52 aquaporin 1 (Colton blood group) Homo sapiens 0-11 31411472-1 2019 Human aquaporin 1 (hAQP1) is the first discovered selective water channel present in lipid membranes of multiple types of cells. Water 60-65 aquaporin 1 (Colton blood group) Homo sapiens 6-17 31411472-1 2019 Human aquaporin 1 (hAQP1) is the first discovered selective water channel present in lipid membranes of multiple types of cells. Water 60-65 aquaporin 1 (Colton blood group) Homo sapiens 19-24 31411472-2 2019 Several structures of hAQP1 and its bovine homolog have been obtained by electron microscopy and X-ray crystallography, giving a consistent picture of the transmembrane domain with the water-conducting pore. Water 185-190 aquaporin 1 (Colton blood group) Homo sapiens 22-27 31400345-0 2019 Temperature-dependent viscosity dominated transport control through AQP1 water channel. Water 73-78 aquaporin 1 (Colton blood group) Homo sapiens 68-72 31400345-4 2019 Otherwise, proton or hydronium (ion) transport through AQP1 at room temperature manifests like a molecular fluid with a correspondingly lower viscosity, such as water (H2O), and then exclusion of proton or hydronium (ion) through AQP1 will not occur. Water 161-166 aquaporin 1 (Colton blood group) Homo sapiens 55-59 31400345-4 2019 Otherwise, proton or hydronium (ion) transport through AQP1 at room temperature manifests like a molecular fluid with a correspondingly lower viscosity, such as water (H2O), and then exclusion of proton or hydronium (ion) through AQP1 will not occur. Water 168-171 aquaporin 1 (Colton blood group) Homo sapiens 55-59 31477744-1 2019 Aquaporin-1 (AQP1) has been proposed as a dual water and cation channel that when upregulated in cancers enhances cell migration rates; however, the mechanism remains unknown. Water 47-52 aquaporin 1 (Colton blood group) Homo sapiens 13-17 31477744-2 2019 Previous work identified AqB011 as an inhibitor of the gated human AQP1 cation conductance, and bacopaside II as a blocker of AQP1 water pores. Water 131-136 aquaporin 1 (Colton blood group) Homo sapiens 126-130 31477744-13 2019 Results here are the first to demonstrate that combined block of the AQP1 ion channel and water pores is more potent in impairing motility across diverse classes of colon cancer cells than single agents alone. Water 90-95 aquaporin 1 (Colton blood group) Homo sapiens 69-73 31254364-0 2019 MEF2C/miR-133a-3p.1 circuit-stabilized AQP1 expression maintains endothelial water homeostasis. Water 77-82 aquaporin 1 (Colton blood group) Homo sapiens 39-43 31254364-2 2019 However, how AQP1 level is stabilized to maintain endothelial water homeostasis is still not clear. Water 62-67 aquaporin 1 (Colton blood group) Homo sapiens 13-17 31374984-3 2019 Molecular docking showed that Rg3 interacted with the aquaporin 1 (AQP1) water channel (binding score -9.4 kJ mol-1). Water 73-78 aquaporin 1 (Colton blood group) Homo sapiens 54-65 31251110-2 2019 Water channel aquaporin-1 (AQP1) enhances water flux across cell membranes, which is highly expressed and associated with cell migration, metastasis and angiogenesis in some human cancers. Water 0-5 aquaporin 1 (Colton blood group) Homo sapiens 27-31 31251110-2 2019 Water channel aquaporin-1 (AQP1) enhances water flux across cell membranes, which is highly expressed and associated with cell migration, metastasis and angiogenesis in some human cancers. Water 42-47 aquaporin 1 (Colton blood group) Homo sapiens 27-31 31039249-2 2019 Aquaporin-1 (AQP1) is the water channel directly implicated in CSF production and a potential therapeutic target in the management of CSF circulation disorders. Water 26-31 aquaporin 1 (Colton blood group) Homo sapiens 0-11 31039249-2 2019 Aquaporin-1 (AQP1) is the water channel directly implicated in CSF production and a potential therapeutic target in the management of CSF circulation disorders. Water 26-31 aquaporin 1 (Colton blood group) Homo sapiens 13-17 30768550-1 2019 INTRODUCTION: Physical exercise or hypoxic exposure influences erythrocyte susceptibility to osmotic stress, and the aquaporin 1 (AQP1) facilitates the transport of water in erythrocytes. Water 165-170 aquaporin 1 (Colton blood group) Homo sapiens 117-128 30768550-1 2019 INTRODUCTION: Physical exercise or hypoxic exposure influences erythrocyte susceptibility to osmotic stress, and the aquaporin 1 (AQP1) facilitates the transport of water in erythrocytes. Water 165-170 aquaporin 1 (Colton blood group) Homo sapiens 130-134 31374984-3 2019 Molecular docking showed that Rg3 interacted with the aquaporin 1 (AQP1) water channel (binding score -9.4 kJ mol-1). Water 73-78 aquaporin 1 (Colton blood group) Homo sapiens 67-71 31374984-6 2019 The results showed that only SRg3 inhibited the AQP1 water flux and inhibited the proliferation of MDA-MB-231 (100 muM), due to cell cycle arrest at G0/G1. Water 53-58 aquaporin 1 (Colton blood group) Homo sapiens 48-52 31185935-2 2019 Aquaporin (AQP) 1 and AQP2, important proteins for renal water reabsorption, have been identified in urinary extracellular vesicles (uEV-AQP1 and -AQP2), and experimental studies have shown that the presence of uEV-AQP1 and -AQP2 may be an indicator of their levels of expression in the kidney. Water 57-62 aquaporin 1 (Colton blood group) Homo sapiens 0-17 31185935-2 2019 Aquaporin (AQP) 1 and AQP2, important proteins for renal water reabsorption, have been identified in urinary extracellular vesicles (uEV-AQP1 and -AQP2), and experimental studies have shown that the presence of uEV-AQP1 and -AQP2 may be an indicator of their levels of expression in the kidney. Water 57-62 aquaporin 1 (Colton blood group) Homo sapiens 137-141 30739527-1 2019 Aquaporin-1 (AQP1) is a homo-tetrameric transmembrane protein that facilitates rapid movement of water and ions across cell membranes. Water 97-102 aquaporin 1 (Colton blood group) Homo sapiens 0-11 30802427-5 2019 Our simulations allowed us to characterize the dynamics of the key structural elements that modulate the diffusion of water single-files through the AQP0 and AQP1 pores. Water 118-123 aquaporin 1 (Colton blood group) Homo sapiens 158-162 30858164-3 2019 AQP1 is a dual water and cyclic-nucleotide-gated cation channel located in lamellipodia and is essential for rapid cell migration in a subset of aggressive cancers. Water 15-20 aquaporin 1 (Colton blood group) Homo sapiens 0-4 31013775-1 2019 AqB013 and AqB050 compounds inhibit aquaporin 1 (AQP1), a dual water and ion channel implicated in tumour angiogenesis. Water 63-68 aquaporin 1 (Colton blood group) Homo sapiens 36-47 31013775-1 2019 AqB013 and AqB050 compounds inhibit aquaporin 1 (AQP1), a dual water and ion channel implicated in tumour angiogenesis. Water 63-68 aquaporin 1 (Colton blood group) Homo sapiens 49-53 30970608-1 2019 The water channel Aquaporin 1 (AQP1) plays a fundamental role in water ultrafiltration during peritoneal dialysis (PD) and its reduced expression or function may be responsible for ultrafiltration failure (UFF). Water 4-9 aquaporin 1 (Colton blood group) Homo sapiens 31-35 30970608-1 2019 The water channel Aquaporin 1 (AQP1) plays a fundamental role in water ultrafiltration during peritoneal dialysis (PD) and its reduced expression or function may be responsible for ultrafiltration failure (UFF). Water 65-70 aquaporin 1 (Colton blood group) Homo sapiens 31-35 30659792-6 2019 Using these computed values along with the data from the latest literature on AQP1 and on erythrocyte proteomics, we estimated the water and glycerol transport rates across the membrane of an entire erythrocyte. Water 131-136 aquaporin 1 (Colton blood group) Homo sapiens 78-82 30470864-1 2019 Major intrinsic protein (MIP) superfamily contains water-transporting AQP1 and glycerol-specific GlpF belonging to two major phylogenetic groups, namely aquaporins (AQPs) and aquaglyceroporins (AQGPs). Water 51-56 aquaporin 1 (Colton blood group) Homo sapiens 70-74 30470864-8 2019 In contrast, the introduction of IHSB in the two AQP1 mutants has increased water transport. Water 76-81 aquaporin 1 (Colton blood group) Homo sapiens 49-53 30739527-1 2019 Aquaporin-1 (AQP1) is a homo-tetrameric transmembrane protein that facilitates rapid movement of water and ions across cell membranes. Water 97-102 aquaporin 1 (Colton blood group) Homo sapiens 13-17 30270117-1 2019 BACKGROUND: Aquaporin-1 (AQP1), a water channel protein controlling the water contents of cells and tissues, exerts pleiotropic effects on various biological activities, including inflammation, angiogenesis, and extracellular matrix remodeling, by regulating cell behaviors and tissue water balance. Water 34-39 aquaporin 1 (Colton blood group) Homo sapiens 12-23 30270117-1 2019 BACKGROUND: Aquaporin-1 (AQP1), a water channel protein controlling the water contents of cells and tissues, exerts pleiotropic effects on various biological activities, including inflammation, angiogenesis, and extracellular matrix remodeling, by regulating cell behaviors and tissue water balance. Water 34-39 aquaporin 1 (Colton blood group) Homo sapiens 25-29 29772789-6 2018 Moreover, it enhanced the expression of aquaporin 1, which is an important water channel that is expressed in the proximal tubules, and reverted aquaporin 1 downregulation induced by IL-1beta/TNFalpha. Water 75-80 aquaporin 1 (Colton blood group) Homo sapiens 40-51 30042826-1 2018 Aquaporin 1 (AQP1) is a membrane protein whose main function is to transfer water across cellular membranes. Water 76-81 aquaporin 1 (Colton blood group) Homo sapiens 0-11 30042826-1 2018 Aquaporin 1 (AQP1) is a membrane protein whose main function is to transfer water across cellular membranes. Water 76-81 aquaporin 1 (Colton blood group) Homo sapiens 13-17 29971013-11 2018 Research in this area is complicated by the fact that the H2O/CO2-transporting function of AQP1 is replaceable by other erythrocyte channels/transporters (e.g., UT-B/GLUT1 for H2O; RhAG for CO2). Water 58-61 aquaporin 1 (Colton blood group) Homo sapiens 91-95 29971013-11 2018 Research in this area is complicated by the fact that the H2O/CO2-transporting function of AQP1 is replaceable by other erythrocyte channels/transporters (e.g., UT-B/GLUT1 for H2O; RhAG for CO2). Water 176-179 aquaporin 1 (Colton blood group) Homo sapiens 91-95 29971013-12 2018 Recently, using carbonic anhydrase II (CAII)-filled erythrocyte vesicles, AQP1 has been demonstrated to transport water for the CAII-mediated reaction, CO2(g) + H2O HCO3-(aq) + H+(aq). Water 114-119 aquaporin 1 (Colton blood group) Homo sapiens 74-78 29971013-12 2018 Recently, using carbonic anhydrase II (CAII)-filled erythrocyte vesicles, AQP1 has been demonstrated to transport water for the CAII-mediated reaction, CO2(g) + H2O HCO3-(aq) + H+(aq). Water 161-164 aquaporin 1 (Colton blood group) Homo sapiens 74-78 28129470-0 2017 The water channel AQP1 is expressed in human atherosclerotic vascular lesions and AQP1 deficiency augments angiotensin II-induced atherosclerosis in mice. Water 4-9 aquaporin 1 (Colton blood group) Homo sapiens 18-22 29755973-2 2018 In addition to enabling water flux, mammalian Aquaporin-1 (AQP1) channels activated by cyclic GMP can carry non-selective monovalent cation currents, selectively blocked by arylsulfonamide compounds AqB007 (IC50 170 muM) and AqB011 (IC50 14 muM). Water 24-29 aquaporin 1 (Colton blood group) Homo sapiens 46-57 29755973-2 2018 In addition to enabling water flux, mammalian Aquaporin-1 (AQP1) channels activated by cyclic GMP can carry non-selective monovalent cation currents, selectively blocked by arylsulfonamide compounds AqB007 (IC50 170 muM) and AqB011 (IC50 14 muM). Water 24-29 aquaporin 1 (Colton blood group) Homo sapiens 59-63 29301341-7 2018 Subsequently, we found AQP1 and AQP3 to be the most predominant AQPs accounting for water and glycerol fluxes, respectively, in the healthy endothelium. Water 84-89 aquaporin 1 (Colton blood group) Homo sapiens 23-27 28762291-8 2017 Severity of appendicitis can be correlated with water permeability measured by AQP1 protein expression and increase of ganglia count in a progressive manner. Water 48-53 aquaporin 1 (Colton blood group) Homo sapiens 79-83 29393494-2 2018 Aquaporin 1 (AQP1) is a 28-kDa water channel formed of six transmembrane domains on the cell membrane. Water 31-36 aquaporin 1 (Colton blood group) Homo sapiens 0-11 29393494-2 2018 Aquaporin 1 (AQP1) is a 28-kDa water channel formed of six transmembrane domains on the cell membrane. Water 31-36 aquaporin 1 (Colton blood group) Homo sapiens 13-17 28632458-5 2018 AQP1, which is a water-selective channel, is expressed in the anterior chamber (cornea, ciliary body, trabecular meshwork) and posterior chamber (retina and microvessels in choroid), controlling the fluid homeostasis in the eye. Water 17-22 aquaporin 1 (Colton blood group) Homo sapiens 0-4 29267208-7 2017 It seems possible that AQP1 present in Gc and Tc cells may be implicated not only in the regulation of water homeostasis required for follicle development but also in cell proliferation and migration. Water 103-108 aquaporin 1 (Colton blood group) Homo sapiens 23-27 29340084-4 2017 More recently, salivary gland gene therapy utilizing the water-specific protein aquaporin 1 (AQP1) has been of great interest to potentially correct salivary dysfunction. Water 57-62 aquaporin 1 (Colton blood group) Homo sapiens 80-91 29340084-4 2017 More recently, salivary gland gene therapy utilizing the water-specific protein aquaporin 1 (AQP1) has been of great interest to potentially correct salivary dysfunction. Water 57-62 aquaporin 1 (Colton blood group) Homo sapiens 93-97 28596233-0 2017 Adaptable interaction between aquaporin-1 and band 3 reveals a potential role of water channel in blood CO2 transport. Water 81-86 aquaporin 1 (Colton blood group) Homo sapiens 30-41 28596233-8 2017 By demonstrating AQP1 as a mobile component of the CO2 transport metabolon, our results uncover a potential role of water channel in blood CO2 transport and respiration.-Hsu, K., Lee, T.-Y., Periasamy, A., Kao, F.-J., Li, L.-T., Lin, C.-Y., Lin, H.-J., Lin, M. Adaptable interaction between aquaporin-1 and band 3 reveals a potential role of water channel in blood CO2 transport. Water 116-121 aquaporin 1 (Colton blood group) Homo sapiens 17-21 28596233-8 2017 By demonstrating AQP1 as a mobile component of the CO2 transport metabolon, our results uncover a potential role of water channel in blood CO2 transport and respiration.-Hsu, K., Lee, T.-Y., Periasamy, A., Kao, F.-J., Li, L.-T., Lin, C.-Y., Lin, H.-J., Lin, M. Adaptable interaction between aquaporin-1 and band 3 reveals a potential role of water channel in blood CO2 transport. Water 116-121 aquaporin 1 (Colton blood group) Homo sapiens 291-302 28596233-8 2017 By demonstrating AQP1 as a mobile component of the CO2 transport metabolon, our results uncover a potential role of water channel in blood CO2 transport and respiration.-Hsu, K., Lee, T.-Y., Periasamy, A., Kao, F.-J., Li, L.-T., Lin, C.-Y., Lin, H.-J., Lin, M. Adaptable interaction between aquaporin-1 and band 3 reveals a potential role of water channel in blood CO2 transport. Water 342-347 aquaporin 1 (Colton blood group) Homo sapiens 17-21 28111028-7 2017 In addition to small pores, the peritoneal membrane contains a specialized water channel, aquaporin 1, which is also present in capillaries of the peritoneal membrane. Water 75-80 aquaporin 1 (Colton blood group) Homo sapiens 90-101 27143047-3 2017 Aquaporin 1 is a cell membrane channel involved in water transport, cell motility, and proliferation. Water 51-56 aquaporin 1 (Colton blood group) Homo sapiens 0-11 28373558-6 2017 This is confirmed by the distribution of the AQP1 water channel within endothelial membranes. Water 50-55 aquaporin 1 (Colton blood group) Homo sapiens 45-49 28146084-3 2017 Aquaporin 1 (AQP1) is a small hydrophobic integral transmembrane protein with a predominant role in trans-cellular water transport. Water 115-120 aquaporin 1 (Colton blood group) Homo sapiens 0-11 28128570-5 2017 In this study, we calculated potentials of mean force for water, ammonia, urea, molecular oxygen, and methanol across the urea transporter B (UT-B) and aquaporin-1 (AQP1), using 3D-RISM, as well as using MD simulations and umbrella sampling. Water 58-63 aquaporin 1 (Colton blood group) Homo sapiens 152-163 28128570-5 2017 In this study, we calculated potentials of mean force for water, ammonia, urea, molecular oxygen, and methanol across the urea transporter B (UT-B) and aquaporin-1 (AQP1), using 3D-RISM, as well as using MD simulations and umbrella sampling. Water 58-63 aquaporin 1 (Colton blood group) Homo sapiens 165-169 27932503-9 2017 The final scenario has AQP1 primarily in the proximal duct cells which secrete water under baseline conditions. Water 79-84 aquaporin 1 (Colton blood group) Homo sapiens 23-27 26919570-1 2017 The astrocytic water channel proteins aquaporin 1 (AQP1) and aquaporin 4 (AQP4) are known to be altered in brains affected by several neurodegenerative disorders, including Alzheimer"s disease. Water 15-20 aquaporin 1 (Colton blood group) Homo sapiens 38-49 26919570-1 2017 The astrocytic water channel proteins aquaporin 1 (AQP1) and aquaporin 4 (AQP4) are known to be altered in brains affected by several neurodegenerative disorders, including Alzheimer"s disease. Water 15-20 aquaporin 1 (Colton blood group) Homo sapiens 51-55 27090529-1 2017 In peritoneal dialysis (PD), ultrafiltration (UF) volume is the sum of solute-free- and solute-coupled-water removal, a dynamic process throughout the entire dwell exerted via aquaporin-1 (AQP1) and small pores, respectively. Water 103-108 aquaporin 1 (Colton blood group) Homo sapiens 176-187 28146084-3 2017 Aquaporin 1 (AQP1) is a small hydrophobic integral transmembrane protein with a predominant role in trans-cellular water transport. Water 115-120 aquaporin 1 (Colton blood group) Homo sapiens 13-17 28614812-5 2017 This "first" water channel was originally named CHIP28 and is now known as aquaporin 1. Water 13-18 aquaporin 1 (Colton blood group) Homo sapiens 48-54 28614812-5 2017 This "first" water channel was originally named CHIP28 and is now known as aquaporin 1. Water 13-18 aquaporin 1 (Colton blood group) Homo sapiens 75-86 27465156-4 2016 The effect of AQP1 inhibitors was evaluated through water flow-based tests: osmotic fragility and hypertonic cryohemolysis. Water 52-57 aquaporin 1 (Colton blood group) Homo sapiens 14-18 27622909-1 2017 INTRODUCTION: Since the discovery of aquaporin-1 (AQP1) as a water channel, more than 2,000 articles, reviews and chapters have been published. Water 61-66 aquaporin 1 (Colton blood group) Homo sapiens 37-48 27622909-1 2017 INTRODUCTION: Since the discovery of aquaporin-1 (AQP1) as a water channel, more than 2,000 articles, reviews and chapters have been published. Water 61-66 aquaporin 1 (Colton blood group) Homo sapiens 50-54 27799072-3 2016 Aquaporin, AQP1, allows water transfer across the apical surface of the choroid epithelium; another protein, perhaps GLUT1, is important on the basolateral surface. Water 24-29 aquaporin 1 (Colton blood group) Homo sapiens 11-15 28036023-4 2016 AQP1 and AQP4, the two primary aquaporin molecules of the central nervous system, regulate brain water and CSF movement and contribute to cytotoxic and vasogenic edema, where they control the size of the intracellular and extracellular fluid volumes, respectively. Water 97-102 aquaporin 1 (Colton blood group) Homo sapiens 0-4 27465156-11 2016 The finding of AQP1 expression induced by Epo in a model of erythroid cells may be interpreted as a mechanism to restore the balance of red cell water fluxes. Water 145-150 aquaporin 1 (Colton blood group) Homo sapiens 15-19 27465156-8 2016 Accordingly, red blood cells from HS subjects were less sensitive to cryohemolysis than normal erythrocytes after inhibition of the AQP1 water channel. Water 137-142 aquaporin 1 (Colton blood group) Homo sapiens 132-136 27409610-4 2016 We analyzed the function of aquaporin 1 (AQP1), a water channel known to promote metastasis and neoangiogenes. Water 50-55 aquaporin 1 (Colton blood group) Homo sapiens 28-39 27474162-4 2016 Results showed bacopaside I blocked both the water (IC50 117 muM) and ion channel activities of AQP1 but did not alter AQP4 activity, whereas bacopaside II selectively blocked the AQP1 water channel (IC50 18 muM) without impairing the ionic conductance. Water 185-190 aquaporin 1 (Colton blood group) Homo sapiens 180-184 27474162-1 2016 Aquaporin-1 (AQP1) is a major intrinsic protein that facilitates flux of water and other small solutes across cell membranes. Water 73-78 aquaporin 1 (Colton blood group) Homo sapiens 0-11 27474162-1 2016 Aquaporin-1 (AQP1) is a major intrinsic protein that facilitates flux of water and other small solutes across cell membranes. Water 73-78 aquaporin 1 (Colton blood group) Homo sapiens 13-17 27583975-1 2016 Multiple moderate-resolution crystal structures of human aquaporin-1 have provided a foundation for understanding the molecular mechanism of selective water translocation in human cells. Water 151-156 aquaporin 1 (Colton blood group) Homo sapiens 57-68 27583975-6 2016 The simulations reveal loop stabilizing interactions that alter the extracellular surface of human AQP1, with possible implications for water transport regulation through the channel. Water 136-141 aquaporin 1 (Colton blood group) Homo sapiens 99-103 27583975-7 2016 Modulation of water permeation may occur as a result of rearrangement of side chains from loop C in the extracellular vestibule of hAQP1, affecting the aromatic arginine selectivity filter. Water 14-19 aquaporin 1 (Colton blood group) Homo sapiens 131-136 26999313-1 2016 UNLABELLED: The adenoviral gene transfer of human aquaporin-1 (hAQP1) water channels to the liver of 17alpha-ethinylestradiol-induced cholestatic rats improves bile flow, in part by enhancing canalicular hAQP1-mediated osmotic water secretion. Water 70-75 aquaporin 1 (Colton blood group) Homo sapiens 50-61 26999313-1 2016 UNLABELLED: The adenoviral gene transfer of human aquaporin-1 (hAQP1) water channels to the liver of 17alpha-ethinylestradiol-induced cholestatic rats improves bile flow, in part by enhancing canalicular hAQP1-mediated osmotic water secretion. Water 70-75 aquaporin 1 (Colton blood group) Homo sapiens 63-68 26999313-1 2016 UNLABELLED: The adenoviral gene transfer of human aquaporin-1 (hAQP1) water channels to the liver of 17alpha-ethinylestradiol-induced cholestatic rats improves bile flow, in part by enhancing canalicular hAQP1-mediated osmotic water secretion. Water 70-75 aquaporin 1 (Colton blood group) Homo sapiens 204-209 26999313-1 2016 UNLABELLED: The adenoviral gene transfer of human aquaporin-1 (hAQP1) water channels to the liver of 17alpha-ethinylestradiol-induced cholestatic rats improves bile flow, in part by enhancing canalicular hAQP1-mediated osmotic water secretion. Water 227-232 aquaporin 1 (Colton blood group) Homo sapiens 50-61 26999313-1 2016 UNLABELLED: The adenoviral gene transfer of human aquaporin-1 (hAQP1) water channels to the liver of 17alpha-ethinylestradiol-induced cholestatic rats improves bile flow, in part by enhancing canalicular hAQP1-mediated osmotic water secretion. Water 227-232 aquaporin 1 (Colton blood group) Homo sapiens 63-68 27409610-4 2016 We analyzed the function of aquaporin 1 (AQP1), a water channel known to promote metastasis and neoangiogenes. Water 50-55 aquaporin 1 (Colton blood group) Homo sapiens 41-45 27261598-10 2016 Cardiac membrane vesicles expressing AQP1 presented a high water permeability coefficient and pretreatment with SNP decreased water transport. Water 59-64 aquaporin 1 (Colton blood group) Homo sapiens 37-41 27261598-11 2016 Age-related influence of NO system on AQP1 abundance and localization in the heart may affect cardiac water homeostasis during hypovolemic state. Water 102-107 aquaporin 1 (Colton blood group) Homo sapiens 38-42 27261598-12 2016 Increased AQP1 S-nitrosylation in the youngest group may decrease osmotic water permeability of cardiac membranes, having a negative impact on cardiac water balance. Water 74-79 aquaporin 1 (Colton blood group) Homo sapiens 10-14 26966862-10 2016 Altogether, the data suggest that expression of hAQP1 increases the water permeability of acinar cells, which underlies the recovery of fluid secretion in the salivary glands functionally compromised post IR. Water 68-73 aquaporin 1 (Colton blood group) Homo sapiens 48-53 27229103-1 2016 Aquaporin 1(AQP1) and AQP5 have an important role in eliminating extravascular lung water, an increase of which contributes to lung injury in patients with sepsis and its consequent mortality. Water 84-89 aquaporin 1 (Colton blood group) Homo sapiens 0-11 26993802-0 2016 Experimental Evaluation of Proposed Small-Molecule Inhibitors of Water Channel Aquaporin-1. Water 65-70 aquaporin 1 (Colton blood group) Homo sapiens 79-90 26993802-1 2016 The aquaporin-1 (AQP1) water channel is a potentially important drug target, as AQP1 inhibition is predicted to have therapeutic action in edema, tumor growth, glaucoma, and other conditions. Water 23-28 aquaporin 1 (Colton blood group) Homo sapiens 4-15 26993802-1 2016 The aquaporin-1 (AQP1) water channel is a potentially important drug target, as AQP1 inhibition is predicted to have therapeutic action in edema, tumor growth, glaucoma, and other conditions. Water 23-28 aquaporin 1 (Colton blood group) Homo sapiens 17-21 26993802-1 2016 The aquaporin-1 (AQP1) water channel is a potentially important drug target, as AQP1 inhibition is predicted to have therapeutic action in edema, tumor growth, glaucoma, and other conditions. Water 23-28 aquaporin 1 (Colton blood group) Homo sapiens 80-84 26993802-4 2016 As a positive control, 0.3 mM HgCl2 inhibited AQP1 water permeability by >95%. Water 51-56 aquaporin 1 (Colton blood group) Homo sapiens 46-50 27229103-1 2016 Aquaporin 1(AQP1) and AQP5 have an important role in eliminating extravascular lung water, an increase of which contributes to lung injury in patients with sepsis and its consequent mortality. Water 84-89 aquaporin 1 (Colton blood group) Homo sapiens 12-16 27006441-2 2016 At that time, AQP1 dysfunction was suggested as the cause of impaired free-water transport. Water 75-80 aquaporin 1 (Colton blood group) Homo sapiens 14-18 26685080-3 2016 Selective inhibition of the AQP1 water channel may provide a new approach for the treatment of several disorders including ocular hypertension/glaucoma, congestive heart failure, brain swelling associated with a stroke, corneal and macular edema, pulmonary edema, and otic disorders such as hearing loss and vertigo. Water 33-38 aquaporin 1 (Colton blood group) Homo sapiens 28-32 26685080-6 2016 These selected compounds directly inhibited water transport in AQP1-enriched stripped erythrocyte ghosts and in proteoliposomes reconstituted with purified AQP1. Water 44-49 aquaporin 1 (Colton blood group) Homo sapiens 63-67 26685080-6 2016 These selected compounds directly inhibited water transport in AQP1-enriched stripped erythrocyte ghosts and in proteoliposomes reconstituted with purified AQP1. Water 44-49 aquaporin 1 (Colton blood group) Homo sapiens 156-160 26924063-2 2016 On the other hand, free-water transport takes place through aquaporin-1 channels, but leads to sodium retention and over hydration. Water 24-29 aquaporin 1 (Colton blood group) Homo sapiens 60-71 26475849-2 2016 This dilutional phenomenon is caused by free water transport through the water channel aquaporin-1. Water 45-50 aquaporin 1 (Colton blood group) Homo sapiens 87-98 26475849-2 2016 This dilutional phenomenon is caused by free water transport through the water channel aquaporin-1. Water 73-78 aquaporin 1 (Colton blood group) Homo sapiens 87-98 26467039-2 2016 AQP1 is a water channel, and under permissive conditions, a nonselective cation channel gated by cGMP. Water 10-15 aquaporin 1 (Colton blood group) Homo sapiens 0-4 26912239-0 2016 Pharmacological blockade of aquaporin-1 water channel by AqB013 restricts migration and invasiveness of colon cancer cells and prevents endothelial tube formation in vitro. Water 40-45 aquaporin 1 (Colton blood group) Homo sapiens 28-39 26812884-1 2016 Aquaporin1 (AQP1) belongs to a highly conserved family of aquaporin proteins which facilitate water flux across cell membranes. Water 94-99 aquaporin 1 (Colton blood group) Homo sapiens 0-10 26812884-1 2016 Aquaporin1 (AQP1) belongs to a highly conserved family of aquaporin proteins which facilitate water flux across cell membranes. Water 94-99 aquaporin 1 (Colton blood group) Homo sapiens 12-16 26549133-0 2016 Inhibition of the expression of aquaporin-1 by RNA interference in pulmonary epithelial cells and its effects on water transport. Water 113-118 aquaporin 1 (Colton blood group) Homo sapiens 32-43 26549133-7 2016 The osmotic water permeability of the AQP1-silenced cells was reduced in the air control and hyperoxia exposure groups, compared with the negative control group 48 and 72 h following exposure. Water 12-17 aquaporin 1 (Colton blood group) Homo sapiens 38-42 26549133-8 2016 The volume and cell membrane osmotic water permeability of the A549 cells were reduced, compared with those in the control group following AQP1-silencing, which indicated that the downregulation of AQP1 impedes extracellular to intracellular fluid transportation. Water 37-42 aquaporin 1 (Colton blood group) Homo sapiens 198-202 26178576-6 2015 PBEF also inhibited the expression of aquaporin 1 (AQP1), which caused a dysfunction and imbalance in water transport. Water 102-107 aquaporin 1 (Colton blood group) Homo sapiens 38-49 26342025-9 2015 Further, we found that the water content of the tissue was positively correlated with the levels of plasma 5-hydroxyindoleacetic acid or tissue aquaporin-1 but not with CD31. Water 27-32 aquaporin 1 (Colton blood group) Homo sapiens 144-155 26197201-4 2015 Pharmacologic regulation of AQP1, either through increased expression or gating, is associated with increased water transport in rodent models of peritoneal dialysis. Water 110-115 aquaporin 1 (Colton blood group) Homo sapiens 28-32 26178576-6 2015 PBEF also inhibited the expression of aquaporin 1 (AQP1), which caused a dysfunction and imbalance in water transport. Water 102-107 aquaporin 1 (Colton blood group) Homo sapiens 51-55 26178576-9 2015 Taken together, these results demonstrate that the increase in intracellular PBEF expression promoted the apoptosis of HPMECs and the expression of inflammatory factors and thus enhanced the inflammatory response and inhibited the expression of AQP1, which resulted in abnormal water transport, diminishing the regulatory effects of AQP1 on water transport. Water 278-283 aquaporin 1 (Colton blood group) Homo sapiens 245-249 26075674-11 2015 Our study suggests that the presence of AQP 1, 3, and 5 in the middle ear cavity may be to have an important role for water transportation. Water 118-123 aquaporin 1 (Colton blood group) Homo sapiens 40-45 26045060-1 2015 INTRODUCTION: The aquaporins (AQP1, 3, 8, 9 and 11) are known to be expressed, and involved in the transport of water and small molecules through fetal membranes. Water 112-117 aquaporin 1 (Colton blood group) Homo sapiens 30-50 24990857-6 2014 Quantitative PCR analysis revealed the presence of major proteins involved in water absorption; the NKCC2beta and AQP1 genes whose expression was markedly upregulated after seawater acclimation. Water 78-83 aquaporin 1 (Colton blood group) Homo sapiens 114-118 26279619-3 2015 Aquaporin-1 (AQP1) and aquaporin-4 (AQP4) are water transport proteins that are highly expressed in primary glial-derived tumors. Water 46-51 aquaporin 1 (Colton blood group) Homo sapiens 0-11 26279619-3 2015 Aquaporin-1 (AQP1) and aquaporin-4 (AQP4) are water transport proteins that are highly expressed in primary glial-derived tumors. Water 46-51 aquaporin 1 (Colton blood group) Homo sapiens 13-17 25797519-11 2015 Molecular dynamics simulations on glycerol-specific GlpF, water-transporting AQP1, its mutant and a fungal AQP channel confirm these predictions. Water 58-63 aquaporin 1 (Colton blood group) Homo sapiens 77-81 26176849-1 2015 Aquaporin 1 (AQP1), a member of water channel proteins, functions as a water-selective transporting protein in cell membranes. Water 32-37 aquaporin 1 (Colton blood group) Homo sapiens 0-11 26176849-1 2015 Aquaporin 1 (AQP1), a member of water channel proteins, functions as a water-selective transporting protein in cell membranes. Water 32-37 aquaporin 1 (Colton blood group) Homo sapiens 13-17 25208977-9 2014 Our data suggest that the adenoviral transfer of hAQP1 gene to the livers of EE-induced cholestatic rats improves bile flow by enhancing the AQP-mediated bile salt-induced canalicular water secretion. Water 184-189 aquaporin 1 (Colton blood group) Homo sapiens 49-54 24120524-3 2014 SCOPE OF REVIEW: The AQP1 structure determined by electron crystallography provided the first insights into the proton exclusion mechanism despite fast water permeation. Water 152-157 aquaporin 1 (Colton blood group) Homo sapiens 21-25 23802191-4 2014 Several lines of evidence have demonstrated that the water channel aquaporin-1 (AQP1) corresponds to the ultrasmall pore located in endothelial cells. Water 53-58 aquaporin 1 (Colton blood group) Homo sapiens 80-84 23802191-6 2014 Haploinsufficiency in AQP1 is also reflected by a significant attenuation of water transport. Water 77-82 aquaporin 1 (Colton blood group) Homo sapiens 22-26 23802191-7 2014 Conversely, studies in a rat model and in PD patients have shown that the induction of AQP1 in peritoneal capillaries by corticosteroids is reflected by increased water transport and ultrafiltration, without affecting the osmotic gradient and small-solute transport. Water 163-168 aquaporin 1 (Colton blood group) Homo sapiens 87-91 23802191-8 2014 Recent data have demonstrated that a novel agonist of AQP1, predicted to stabilize the open-state conformation of the channel, modulates water transport and improves ultrafiltration. Water 137-142 aquaporin 1 (Colton blood group) Homo sapiens 54-58 24333057-1 2014 BACKGROUND: The Colton blood group antigens Co(a), Co(b) and Co3 are encoded by the AQP1 gene which produces a water channel forming integral protein. Water 111-116 aquaporin 1 (Colton blood group) Homo sapiens 84-88 25353519-0 2014 1/ f Fluctuations of amino acids regulate water transportation in aquaporin 1. Water 42-47 aquaporin 1 (Colton blood group) Homo sapiens 66-77 25353519-8 2014 As a result, we confirm that 1/f fluctuations of amino acids contribute to water transportation in AQP1. Water 75-80 aquaporin 1 (Colton blood group) Homo sapiens 99-103 24286224-6 2014 We confirmed high H2O2 permeability of the human aquaammoniaporin AQP8 and found intermediate H2O2 permeability of the prototypical orthodox water channel AQP1 from the rat. Water 141-146 aquaporin 1 (Colton blood group) Homo sapiens 155-159 24169407-4 2013 Both corticosteroids and vitamin A derivatives have been shown to upregulate the expression of aquaporin 1, a water channel protein. Water 110-115 aquaporin 1 (Colton blood group) Homo sapiens 95-106 24169407-5 2013 Aquaporin 1 is widely distributed in the human brain and is associated with water secretion into the subarachnoid space. Water 76-81 aquaporin 1 (Colton blood group) Homo sapiens 0-11 22252122-2 2012 AQP1-4 are localized in plasma membranes of renal epithelial cells and are intimately involved in water reabsorption by the kidney. Water 98-103 aquaporin 1 (Colton blood group) Homo sapiens 0-4 23813972-8 2013 Localization of AQP1 and SLC4A11 in human and murine corneal (apical and basolateral, respectively) suggests a cooperative role in mediating trans-endothelial water reabsorption. Water 159-164 aquaporin 1 (Colton blood group) Homo sapiens 16-20 23549977-3 2013 Water channel proteins known as aquaporins (AQP)s, notably AQP-1, appear to be involved in the arterial capillary proliferation in the cirrhotic liver. Water 0-5 aquaporin 1 (Colton blood group) Homo sapiens 59-64 23164158-3 2013 Aquaporin 1 (AQP1) is a specific protein channels for water transport; it is expressed in articular chondrocytes, human synovitis, in chondrocytes of patients with rheumatoid arthritis or OA and in chondrocyte-like cells of human intervertebral disc. Water 54-59 aquaporin 1 (Colton blood group) Homo sapiens 0-11 23164158-3 2013 Aquaporin 1 (AQP1) is a specific protein channels for water transport; it is expressed in articular chondrocytes, human synovitis, in chondrocytes of patients with rheumatoid arthritis or OA and in chondrocyte-like cells of human intervertebral disc. Water 54-59 aquaporin 1 (Colton blood group) Homo sapiens 13-17 23219802-5 2013 Mass spectrometry of the isolated, high molecular, cross-linked stomatin complexes revealed the major interaction partners as glucose transporter-1 (GLUT1), anion exchanger (band 3), and water channel (aquaporin-1). Water 187-192 aquaporin 1 (Colton blood group) Homo sapiens 202-213 23332061-9 2013 Predicted pressure, volume, and permeability changes indicate that hAQP1 water channels can transit from a high-water-permeability state to a closed state. Water 73-78 aquaporin 1 (Colton blood group) Homo sapiens 67-72 23332061-9 2013 Predicted pressure, volume, and permeability changes indicate that hAQP1 water channels can transit from a high-water-permeability state to a closed state. Water 112-117 aquaporin 1 (Colton blood group) Homo sapiens 67-72 23468265-1 2013 BACKGROUND: In peritoneal dialysis (PD) approximately 40% of ultrafiltration (UF) during hypertonic dwell (mini-PET test) occurs as free water transport (FWT) through water channels, mainly aquaporin-1. Water 137-142 aquaporin 1 (Colton blood group) Homo sapiens 190-201 23468265-1 2013 BACKGROUND: In peritoneal dialysis (PD) approximately 40% of ultrafiltration (UF) during hypertonic dwell (mini-PET test) occurs as free water transport (FWT) through water channels, mainly aquaporin-1. Water 167-172 aquaporin 1 (Colton blood group) Homo sapiens 190-201 23948641-0 2013 AQP1 expression alterations affect morphology and water transport in Schwann cells and hypoxia-induced up-regulation of AQP1 occurs in a HIF-1alpha-dependent manner. Water 50-55 aquaporin 1 (Colton blood group) Homo sapiens 0-4 23948641-1 2013 Aquaporin-1 (AQP1) is the principle water channel in the peripheral nervous system (PNS) and is specifically localized to Schwann cells in the PNS. Water 36-41 aquaporin 1 (Colton blood group) Homo sapiens 0-11 23948641-1 2013 Aquaporin-1 (AQP1) is the principle water channel in the peripheral nervous system (PNS) and is specifically localized to Schwann cells in the PNS. Water 36-41 aquaporin 1 (Colton blood group) Homo sapiens 13-17 23948641-8 2013 Taken together, these results indicate that (1) AQP1 is an important factor responsible for the fast water transport of cultured Schwann cells and is involved in cell plasticity; (2) AQP1 alterations may be a primary factor in hypoxia-induced peripheral nerve edema; (3) HIF-1alpha participates in the hypoxic induction of the AQP1 gene; (4) AQP1 inhibition might provide a new therapeutic alternative for the treatment of some forms of peripheral nerve edema. Water 101-106 aquaporin 1 (Colton blood group) Homo sapiens 48-52 24086369-3 2013 We hypothesized that seronegative NMOsd patients might have autoantibodies against aquaporin-1 (AQP1), another water channel in CNS astrocytes. Water 111-116 aquaporin 1 (Colton blood group) Homo sapiens 83-94 24086369-3 2013 We hypothesized that seronegative NMOsd patients might have autoantibodies against aquaporin-1 (AQP1), another water channel in CNS astrocytes. Water 111-116 aquaporin 1 (Colton blood group) Homo sapiens 96-100 23690341-9 2013 Functional expression of aquaporin-1 tyrosine phosphorylation on red blood cell membranes increased significantly at 25 and 50 minutes after subjects ingested 500 mL of water compared with that before water ingestion. Water 169-174 aquaporin 1 (Colton blood group) Homo sapiens 25-36 23690341-9 2013 Functional expression of aquaporin-1 tyrosine phosphorylation on red blood cell membranes increased significantly at 25 and 50 minutes after subjects ingested 500 mL of water compared with that before water ingestion. Water 201-206 aquaporin 1 (Colton blood group) Homo sapiens 25-36 23690341-10 2013 This study concludes that water ingestion produces upregulation of aquaporin-1 tyrosine phosphorylation on red blood cell, which presents as a novel biological marker that occurs simultaneously with the osmopressor response. Water 26-31 aquaporin 1 (Colton blood group) Homo sapiens 67-78 23113556-1 2013 Human aquaporin-1 (hAQP1) is a water channel found in many tissues and potentially involved in several human pathologies. Water 31-36 aquaporin 1 (Colton blood group) Homo sapiens 6-17 23113556-1 2013 Human aquaporin-1 (hAQP1) is a water channel found in many tissues and potentially involved in several human pathologies. Water 31-36 aquaporin 1 (Colton blood group) Homo sapiens 19-24 23113556-4 2013 In this study we present three novel hAQP1 blockers that have been identified by virtual screening and inhibit water flux through hAQP1 in Xenopus laevis oocyte swelling assays at low micromolar concentrations. Water 111-116 aquaporin 1 (Colton blood group) Homo sapiens 37-42 23113556-4 2013 In this study we present three novel hAQP1 blockers that have been identified by virtual screening and inhibit water flux through hAQP1 in Xenopus laevis oocyte swelling assays at low micromolar concentrations. Water 111-116 aquaporin 1 (Colton blood group) Homo sapiens 130-135 22705445-4 2012 In 1992 the Agre group identified CHIP28"s water transport property. Water 43-48 aquaporin 1 (Colton blood group) Homo sapiens 34-40 22705445-7 2012 In the natural or model membranes AQP1 is in the form of a homotetramer, however, each monomer has an independent water channel (pore). Water 114-119 aquaporin 1 (Colton blood group) Homo sapiens 34-38 22705445-8 2012 The three-dimensional structure of AQP1 is described, with a detailed description of the channel (pore), the molecular mechanisms of permeation through the channel of water molecules and exclusion of protons. Water 167-172 aquaporin 1 (Colton blood group) Homo sapiens 35-39 22705445-12 2012 The role of AQP1 in red blood cells is discussed based on our comparative studies of water permeability in over 30 species. Water 85-90 aquaporin 1 (Colton blood group) Homo sapiens 12-16 22554013-3 2012 METHODS: We investigated the expression pattern and localization of aquaporin-1, an important channel protein involved in plasma membrane water permeability, in patients with anterior disc displacement (both with and without reduction), with a view to assessing the characteristics of local tissue responses to the microenvironmental changes induced by abnormal mechanical loading of the displaced disc. Water 138-143 aquaporin 1 (Colton blood group) Homo sapiens 68-79 22805778-2 2012 The water channel proteins astrocytic aquaporin 1 (AQP1) and aquaporin 4 (AQP4) are known to be abnormally expressed in AD brains, but the expression of AQPs surrounding SPs and cerebral amyloid angiopathy has not been described in detail. Water 4-9 aquaporin 1 (Colton blood group) Homo sapiens 38-49 22947940-5 2012 Applications to T4 lysozyme, the Trp-cage, the aquaporin channels Aqy1 and hAQP1, and the CLC-ec1 chloride antiporter are presented in which the active site geometry, the hydrophobic solvent-accessible surface, channel gating dynamics, water permeability (p(f)), and a dihedral angle are defined as functional order parameters. Water 236-241 aquaporin 1 (Colton blood group) Homo sapiens 75-80 22820194-2 2012 The aquaporin (AQP) water channels, in particular AQP1 and -4, have been suggested to play an important role in fluid homeostasis of the myocardium. Water 20-25 aquaporin 1 (Colton blood group) Homo sapiens 50-61 22805778-2 2012 The water channel proteins astrocytic aquaporin 1 (AQP1) and aquaporin 4 (AQP4) are known to be abnormally expressed in AD brains, but the expression of AQPs surrounding SPs and cerebral amyloid angiopathy has not been described in detail. Water 4-9 aquaporin 1 (Colton blood group) Homo sapiens 51-55 22348807-1 2012 BACKGROUND AND OBJECTIVES: The Colton blood group antigens are carried by the AQP1 water channel. Water 83-88 aquaporin 1 (Colton blood group) Homo sapiens 78-82 22334691-0 2012 Rapid aquaporin translocation regulates cellular water flow: mechanism of hypotonicity-induced subcellular localization of aquaporin 1 water channel. Water 49-54 aquaporin 1 (Colton blood group) Homo sapiens 123-134 22426160-5 2012 Simultaneously, exposure to Rg3 suppressed expression of the aquaporin 1 (AQP1) water channel protein, which has previously been reported to be involved in cell migration. Water 80-85 aquaporin 1 (Colton blood group) Homo sapiens 61-72 22426160-5 2012 Simultaneously, exposure to Rg3 suppressed expression of the aquaporin 1 (AQP1) water channel protein, which has previously been reported to be involved in cell migration. Water 80-85 aquaporin 1 (Colton blood group) Homo sapiens 74-78 22020536-6 2012 Aquaporin 1 (AQP1) is a cell membrane channel involved in water transport, cell motility, and proliferation. Water 58-63 aquaporin 1 (Colton blood group) Homo sapiens 0-11 22020536-6 2012 Aquaporin 1 (AQP1) is a cell membrane channel involved in water transport, cell motility, and proliferation. Water 58-63 aquaporin 1 (Colton blood group) Homo sapiens 13-17 22020536-14 2012 RESULTS: We demonstrated expression of AQP1 in normal and neoplastic mesothelium at the apical aspect of the cell, in keeping with a role in water transport. Water 141-146 aquaporin 1 (Colton blood group) Homo sapiens 39-43 22334691-0 2012 Rapid aquaporin translocation regulates cellular water flow: mechanism of hypotonicity-induced subcellular localization of aquaporin 1 water channel. Water 135-140 aquaporin 1 (Colton blood group) Homo sapiens 123-134 22334691-7 2012 This translocation, which has a direct role in cell volume regulation, occurs within 30 s and is dependent on calmodulin activation and phosphorylation of AQP1 at two threonine residues by protein kinase C. This direct mechanism provides a rationale for the changes in water transport that are required in response to constantly changing local cellular water availability. Water 269-274 aquaporin 1 (Colton blood group) Homo sapiens 155-159 22334691-7 2012 This translocation, which has a direct role in cell volume regulation, occurs within 30 s and is dependent on calmodulin activation and phosphorylation of AQP1 at two threonine residues by protein kinase C. This direct mechanism provides a rationale for the changes in water transport that are required in response to constantly changing local cellular water availability. Water 353-358 aquaporin 1 (Colton blood group) Homo sapiens 155-159 22116423-3 2012 Aquaporin-1 (AQP1) is a water channel located mainly at the choroid plexus epithelium and plays an active role in CSF production. Water 24-29 aquaporin 1 (Colton blood group) Homo sapiens 0-11 22116423-3 2012 Aquaporin-1 (AQP1) is a water channel located mainly at the choroid plexus epithelium and plays an active role in CSF production. Water 24-29 aquaporin 1 (Colton blood group) Homo sapiens 13-17 23123479-1 2012 Recently, we have found that pressure-induced hemolysis is enhanced by inhibiting water transport via aquaporin-1 (AQP1), as seen in p-chloromercuribenzoate (pCMB)-treated erythrocytes. Water 82-87 aquaporin 1 (Colton blood group) Homo sapiens 102-113 23123479-1 2012 Recently, we have found that pressure-induced hemolysis is enhanced by inhibiting water transport via aquaporin-1 (AQP1), as seen in p-chloromercuribenzoate (pCMB)-treated erythrocytes. Water 82-87 aquaporin 1 (Colton blood group) Homo sapiens 115-119 22200949-2 2012 Here, we applied chromophore-assisted light inactivation (CALI) to inhibit the water permeability of AQP1, and of two AQP4 isoforms (M1 and M23), one of which (M23) forms aggregates at the cell plasma membrane. Water 79-84 aquaporin 1 (Colton blood group) Homo sapiens 101-105 22415096-1 2012 BACKGROUND/AIMS: Aquaporin-1 (AQP1) is a glycoprotein that mediates osmotic water transport, its expression has been found to correlate with tumour stage in some tumours. Water 76-81 aquaporin 1 (Colton blood group) Homo sapiens 17-28 22415096-1 2012 BACKGROUND/AIMS: Aquaporin-1 (AQP1) is a glycoprotein that mediates osmotic water transport, its expression has been found to correlate with tumour stage in some tumours. Water 76-81 aquaporin 1 (Colton blood group) Homo sapiens 30-34 22200949-6 2012 After KR bleaching, KR-AQP1 water permeability was reduced by up to 80% for the chimera with the shortest linker. Water 28-33 aquaporin 1 (Colton blood group) Homo sapiens 23-27 23029502-1 2012 Previous studies reported that a subpopulation of mouse and rat trigeminal neurons express water channel aquaporin-1 (AQP1). Water 91-96 aquaporin 1 (Colton blood group) Homo sapiens 105-116 22310126-1 2012 BACKGROUND: Aquaporin (AQP)-1 is expressed in most microvasculature endothelial cells forming water channels that play major roles in a variety of physiologic processes. Water 94-99 aquaporin 1 (Colton blood group) Homo sapiens 23-29 21157000-4 2010 These are, respectively, enhancement of the intracellular water proton intrinsic NMR relaxation rate 1/T(2a) by paramagnetism of NO subsequently bonded to iron atoms of intracellular deoxyhemoglobin, and suppression of diffusional water permeability P(d) as a consequence of nitrosylation of aquaporin-1 (AQP1) channel Cys189, either by direct reaction with NO or with one of the NO oxidation products, such as N2O3. Water 58-63 aquaporin 1 (Colton blood group) Homo sapiens 293-304 21793635-0 2011 Influence of aquaporin-1 gene polymorphism on water retention in liver cirrhosis. Water 46-51 aquaporin 1 (Colton blood group) Homo sapiens 13-24 21793635-13 2011 CONCLUSIONS: Our results suggest that the rs1049305 (C/G, UTR3) AQP1 polymorphism could be involved in the genetic susceptibility to develop water retention in patients with liver cirrhosis. Water 141-146 aquaporin 1 (Colton blood group) Homo sapiens 64-68 21525850-5 2011 About half of the ultrafiltration generated by L-carnitine reflected facilitated water transport by aquaporin-1 (AQP1) water channels of endothelial cells. Water 81-86 aquaporin 1 (Colton blood group) Homo sapiens 100-111 21525850-5 2011 About half of the ultrafiltration generated by L-carnitine reflected facilitated water transport by aquaporin-1 (AQP1) water channels of endothelial cells. Water 81-86 aquaporin 1 (Colton blood group) Homo sapiens 113-117 21525850-5 2011 About half of the ultrafiltration generated by L-carnitine reflected facilitated water transport by aquaporin-1 (AQP1) water channels of endothelial cells. Water 119-124 aquaporin 1 (Colton blood group) Homo sapiens 100-111 21525850-5 2011 About half of the ultrafiltration generated by L-carnitine reflected facilitated water transport by aquaporin-1 (AQP1) water channels of endothelial cells. Water 119-124 aquaporin 1 (Colton blood group) Homo sapiens 113-117 21373963-0 2011 Water flux through human aquaporin 1: inhibition by intracellular furosemide and maximal response with high osmotic gradients. Water 0-5 aquaporin 1 (Colton blood group) Homo sapiens 25-36 21373963-1 2011 This work studies water permeability properties of human aquaporin 1 (hAQP1) expressed in Xenopus laevis oocyte membranes, applying a technique where cellular content is replaced with a known medium, with the possibility of measuring intracellular pressure. Water 18-23 aquaporin 1 (Colton blood group) Homo sapiens 57-68 21373963-1 2011 This work studies water permeability properties of human aquaporin 1 (hAQP1) expressed in Xenopus laevis oocyte membranes, applying a technique where cellular content is replaced with a known medium, with the possibility of measuring intracellular pressure. Water 18-23 aquaporin 1 (Colton blood group) Homo sapiens 70-75 21373963-5 2011 These results would indicate that the passage of water molecules through hAQP1 may have a maximum rate. Water 49-54 aquaporin 1 (Colton blood group) Homo sapiens 73-78 21360438-1 2011 Aquaporin-1 (AQP1) is the main water channel responsible for water transport through many epithelia and endothelia. Water 31-36 aquaporin 1 (Colton blood group) Homo sapiens 0-11 21360438-1 2011 Aquaporin-1 (AQP1) is the main water channel responsible for water transport through many epithelia and endothelia. Water 31-36 aquaporin 1 (Colton blood group) Homo sapiens 13-17 21360438-1 2011 Aquaporin-1 (AQP1) is the main water channel responsible for water transport through many epithelia and endothelia. Water 61-66 aquaporin 1 (Colton blood group) Homo sapiens 0-11 21360438-1 2011 Aquaporin-1 (AQP1) is the main water channel responsible for water transport through many epithelia and endothelia. Water 61-66 aquaporin 1 (Colton blood group) Homo sapiens 13-17 20851859-6 2010 Our preliminary AQP1 data suggest that all the NH3 and less than half of the CO2 move along with H2O through the four monomeric aquapores. Water 97-100 aquaporin 1 (Colton blood group) Homo sapiens 16-20 21940485-1 2011 The water channel aquaporin-1 (AQP1) is the molecular counterpart of the ultrasmall pore that mediates free water transport during peritoneal dialysis (PD). Water 4-9 aquaporin 1 (Colton blood group) Homo sapiens 31-35 21940485-1 2011 The water channel aquaporin-1 (AQP1) is the molecular counterpart of the ultrasmall pore that mediates free water transport during peritoneal dialysis (PD). Water 108-113 aquaporin 1 (Colton blood group) Homo sapiens 31-35 21157000-4 2010 These are, respectively, enhancement of the intracellular water proton intrinsic NMR relaxation rate 1/T(2a) by paramagnetism of NO subsequently bonded to iron atoms of intracellular deoxyhemoglobin, and suppression of diffusional water permeability P(d) as a consequence of nitrosylation of aquaporin-1 (AQP1) channel Cys189, either by direct reaction with NO or with one of the NO oxidation products, such as N2O3. Water 58-63 aquaporin 1 (Colton blood group) Homo sapiens 306-310 21157000-5 2010 The bound NO on the Cys189 thiol residue appears to impose a less efficient barrier to water permeation through AQP1 than the larger carboxyphenylmercuryl residue from p-chloromercuribenzoate. Water 88-93 aquaporin 1 (Colton blood group) Homo sapiens 113-117 20492605-2 2010 The latter is only absent in the extremely rare individuals of the Colton "null" phenotype, usually referred to as Co(a-b-), which lack the water channel AQP1 that carries the Colton antigens. Water 140-145 aquaporin 1 (Colton blood group) Homo sapiens 154-158 21055716-5 2010 Furthermore, we show that the mutation has a dominant-negative effect on KLF1 transcriptional activity and unexpectedly abolishes the expression of the water channel AQP1 and the adhesion molecule CD44. Water 152-157 aquaporin 1 (Colton blood group) Homo sapiens 166-170 20739606-0 2010 Cloning and characterization of a zebrafish homologue of human AQP1: a bifunctional water and gas channel. Water 84-89 aquaporin 1 (Colton blood group) Homo sapiens 63-67 20739606-1 2010 The mammalian aquaporins AQP1, AQP4, and AQP5 have been shown to function not only as water channels but also as gas channels. Water 86-91 aquaporin 1 (Colton blood group) Homo sapiens 25-29 20853510-5 2010 Here we provide evidence through anatomical colocalization studies that OEG express the water channel aquaporin 1 (AQP1), both in vivo and in vitro. Water 88-93 aquaporin 1 (Colton blood group) Homo sapiens 102-113 20853510-5 2010 Here we provide evidence through anatomical colocalization studies that OEG express the water channel aquaporin 1 (AQP1), both in vivo and in vitro. Water 88-93 aquaporin 1 (Colton blood group) Homo sapiens 115-119 20969805-3 2010 Water channel proteins, known as aquaporins (AQPs), notably AQP-1 and AQP-4, appears to be involved in the pathophysiology of several neurological diseases. Water 0-5 aquaporin 1 (Colton blood group) Homo sapiens 60-65 19761816-5 2010 Using D54MG glioma cells stably transfected with either AQP1 or AQP4, we show that PKC activity regulates water permeability through phosphorylation of AQP4. Water 106-111 aquaporin 1 (Colton blood group) Homo sapiens 56-60 20607193-6 2010 Our simulations show that the PfAQP, the human aquaporin 1 (hAQP1) and the Escherichia coli glycerol facilitator (GlpF) have nearly identical water permeabilities. Water 142-147 aquaporin 1 (Colton blood group) Homo sapiens 47-58 20607193-6 2010 Our simulations show that the PfAQP, the human aquaporin 1 (hAQP1) and the Escherichia coli glycerol facilitator (GlpF) have nearly identical water permeabilities. Water 142-147 aquaporin 1 (Colton blood group) Homo sapiens 60-65 20149606-3 2010 We have recently shown that human chondrocytes and synoviocytes express aquaporin 1 (AQP1) water channels and that AQP1 is upregulated in RA cartilage. Water 91-96 aquaporin 1 (Colton blood group) Homo sapiens 72-83 20578142-11 2010 Additionally, AQP-1 localizes to plasma membrane blebs, where it increases osmotic water permeability and locally facilitates the rapid, trans-membrane flux of water. Water 83-88 aquaporin 1 (Colton blood group) Homo sapiens 14-19 20578142-11 2010 Additionally, AQP-1 localizes to plasma membrane blebs, where it increases osmotic water permeability and locally facilitates the rapid, trans-membrane flux of water. Water 160-165 aquaporin 1 (Colton blood group) Homo sapiens 14-19 20578142-12 2010 CONCLUSION: AQP-1 enhances osmotic water permeability and FGF-induced dynamic membrane blebbing in LEC and thereby drives invasion and pathological angiogenesis during cirrhosis. Water 35-40 aquaporin 1 (Colton blood group) Homo sapiens 12-17 20409716-1 2010 Aquaporin 1 (AQP1) is a molecular water channel expressed in many anatomical locations, particularly in epithelial barriers specialized in water transport. Water 34-39 aquaporin 1 (Colton blood group) Homo sapiens 0-11 20409716-1 2010 Aquaporin 1 (AQP1) is a molecular water channel expressed in many anatomical locations, particularly in epithelial barriers specialized in water transport. Water 34-39 aquaporin 1 (Colton blood group) Homo sapiens 13-17 20409716-1 2010 Aquaporin 1 (AQP1) is a molecular water channel expressed in many anatomical locations, particularly in epithelial barriers specialized in water transport. Water 139-144 aquaporin 1 (Colton blood group) Homo sapiens 0-11 20409716-1 2010 Aquaporin 1 (AQP1) is a molecular water channel expressed in many anatomical locations, particularly in epithelial barriers specialized in water transport. Water 139-144 aquaporin 1 (Colton blood group) Homo sapiens 13-17 20149606-3 2010 We have recently shown that human chondrocytes and synoviocytes express aquaporin 1 (AQP1) water channels and that AQP1 is upregulated in RA cartilage. Water 91-96 aquaporin 1 (Colton blood group) Homo sapiens 85-89 20168076-0 2010 AQP1 is not only a water channel: It contributes to cell migration through Lin7/beta-catenin. Water 19-24 aquaporin 1 (Colton blood group) Homo sapiens 0-4 20409470-0 2010 Molecular mechanisms of how mercury inhibits water permeation through aquaporin-1: understanding by molecular dynamics simulation. Water 45-50 aquaporin 1 (Colton blood group) Homo sapiens 70-81 20409470-3 2010 Although site-directed mutagenesis has shown that mercury binds to Cys189 during the inhibition process, it is not fully understood how this inhibits the water permeation through AQP1. Water 154-159 aquaporin 1 (Colton blood group) Homo sapiens 179-183 20409470-6 2010 During each last 10 ns, we observed water permeation events occurred 23 times in Free AQP1 and never in Hg-AQP1. Water 36-41 aquaporin 1 (Colton blood group) Homo sapiens 86-90 20409470-8 2010 In Free AQP1, backbone oxygen atoms of Gly190, Cys191, and Gly192 lined, and were oriented to, the surface of the water pore channel. Water 114-119 aquaporin 1 (Colton blood group) Homo sapiens 8-12 20409470-9 2010 In Hg-AQP1, however, the SHg+ of Cys191-SHg+ was oriented toward the outside of the water pore. Water 84-89 aquaporin 1 (Colton blood group) Homo sapiens 6-10 20409470-11 2010 We suggest that mercury disrupts the water pore of AQP1 through local conformational changes in the ar/R region. Water 37-42 aquaporin 1 (Colton blood group) Homo sapiens 51-55 20168076-4 2010 Investigating the possible connection between AQP1 and cytoskeleton, our group showed that such a water channel through Lin7/beta-catenin affects the organization of the cytoskeleton and proposed a model. Water 98-103 aquaporin 1 (Colton blood group) Homo sapiens 46-50 20049482-0 2010 AQP1 mediates water transport in the carotid body. Water 14-19 aquaporin 1 (Colton blood group) Homo sapiens 0-4 20049482-5 2010 We have also shown that inhibition of AQP1 expression clearly reduced type I cell swelling after a hyposmotic shock, demonstrating that AQP1 has a major contribution in transmembrane water movement in these chemoreceptor cells. Water 183-188 aquaporin 1 (Colton blood group) Homo sapiens 38-42 20049482-5 2010 We have also shown that inhibition of AQP1 expression clearly reduced type I cell swelling after a hyposmotic shock, demonstrating that AQP1 has a major contribution in transmembrane water movement in these chemoreceptor cells. Water 183-188 aquaporin 1 (Colton blood group) Homo sapiens 136-140 20049482-8 2010 We also show that AQP1 mediates water transport across the cell membrane of type I cells, supporting the contribution of this protein to the osmoreception function of the CB. Water 32-37 aquaporin 1 (Colton blood group) Homo sapiens 18-22 20738681-5 2009 The Aqp1b belongs to a teleost-specific subfamily of water-selective aquaporins, similar to mammalian aquaporin-1 (AQP1) that has possibly evolved by duplication of a common ancestor and further neofunctionalization in oocytes of marine teleosts for water uptake. Water 53-58 aquaporin 1 (Colton blood group) Homo sapiens 102-113 19961829-2 2010 Using molecular dynamics simulations of AQP0 and AQP1, we find that there is a sudden decrease in the distribution profile of water density along the pore of AQP0 in the region of residue Tyr23, which significantly disrupts the single file water chain by forming hydrogen bond with permeating water molecules. Water 126-131 aquaporin 1 (Colton blood group) Homo sapiens 49-53 19961829-2 2010 Using molecular dynamics simulations of AQP0 and AQP1, we find that there is a sudden decrease in the distribution profile of water density along the pore of AQP0 in the region of residue Tyr23, which significantly disrupts the single file water chain by forming hydrogen bond with permeating water molecules. Water 240-245 aquaporin 1 (Colton blood group) Homo sapiens 49-53 19961829-2 2010 Using molecular dynamics simulations of AQP0 and AQP1, we find that there is a sudden decrease in the distribution profile of water density along the pore of AQP0 in the region of residue Tyr23, which significantly disrupts the single file water chain by forming hydrogen bond with permeating water molecules. Water 240-245 aquaporin 1 (Colton blood group) Homo sapiens 49-53 19961829-3 2010 Comparisons of free-energy and interaction-energy profiles for water conduction between AQP0 and AQP1 indicate that this interruption of the water chain causes a huge energy barrier opposing water translocation through AQP0. Water 63-68 aquaporin 1 (Colton blood group) Homo sapiens 97-101 19961829-3 2010 Comparisons of free-energy and interaction-energy profiles for water conduction between AQP0 and AQP1 indicate that this interruption of the water chain causes a huge energy barrier opposing water translocation through AQP0. Water 141-146 aquaporin 1 (Colton blood group) Homo sapiens 97-101 19961829-3 2010 Comparisons of free-energy and interaction-energy profiles for water conduction between AQP0 and AQP1 indicate that this interruption of the water chain causes a huge energy barrier opposing water translocation through AQP0. Water 141-146 aquaporin 1 (Colton blood group) Homo sapiens 97-101 19306058-1 2010 Aquaporin1 (AQP1) is a water channel protein that facilitates water flux across cell membranes. Water 23-28 aquaporin 1 (Colton blood group) Homo sapiens 12-16 20063900-5 2010 This suggests that the increased level of water transport following osmotic change may be due a phosphorylation-dependent increase in the level of AQP1 trafficking resulting in membrane localization. Water 42-47 aquaporin 1 (Colton blood group) Homo sapiens 147-151 19306058-1 2010 Aquaporin1 (AQP1) is a water channel protein that facilitates water flux across cell membranes. Water 23-28 aquaporin 1 (Colton blood group) Homo sapiens 0-10 19796672-10 2010 Furthermore, such a distribution of AQP-2, -3, and V2-R suggests that VP-AQP-2 mediated water transport might work actively in the basal cells from perilymph towards endolymph containing AQP-1, -7 and -9. Water 88-93 aquaporin 1 (Colton blood group) Homo sapiens 187-203 19610096-3 2010 In response to injury, two additional aquaporins, AQP1 and AQP9, can be detected in astrocytes, yet neither is found in cultured astrocytes, and therefore their contribution to astrocyte water uptake and biology is poorly investigated. Water 187-192 aquaporin 1 (Colton blood group) Homo sapiens 50-54 20738681-5 2009 The Aqp1b belongs to a teleost-specific subfamily of water-selective aquaporins, similar to mammalian aquaporin-1 (AQP1) that has possibly evolved by duplication of a common ancestor and further neofunctionalization in oocytes of marine teleosts for water uptake. Water 53-58 aquaporin 1 (Colton blood group) Homo sapiens 115-119 20738681-5 2009 The Aqp1b belongs to a teleost-specific subfamily of water-selective aquaporins, similar to mammalian aquaporin-1 (AQP1) that has possibly evolved by duplication of a common ancestor and further neofunctionalization in oocytes of marine teleosts for water uptake. Water 250-255 aquaporin 1 (Colton blood group) Homo sapiens 102-113 20738681-5 2009 The Aqp1b belongs to a teleost-specific subfamily of water-selective aquaporins, similar to mammalian aquaporin-1 (AQP1) that has possibly evolved by duplication of a common ancestor and further neofunctionalization in oocytes of marine teleosts for water uptake. Water 250-255 aquaporin 1 (Colton blood group) Homo sapiens 115-119 19787701-8 2009 Adenovirus-mediated high expression of AQP1 in HT20 cells increased relative plasma membrane water permeability and migration rate in both wound healing and invasive transwell migration assays. Water 93-98 aquaporin 1 (Colton blood group) Homo sapiens 39-43 18930582-1 2009 BACKGROUND: Aquaporin 1 (AQP1) is a water channel expressed in many epithelial tissues and endothelium, including the proximal nephron of the kidney. Water 36-41 aquaporin 1 (Colton blood group) Homo sapiens 12-23 18930582-1 2009 BACKGROUND: Aquaporin 1 (AQP1) is a water channel expressed in many epithelial tissues and endothelium, including the proximal nephron of the kidney. Water 36-41 aquaporin 1 (Colton blood group) Homo sapiens 25-29 19701945-7 2009 Fusion of this motif to aquaporin-1 also resulted in missorting of that water channel, indicating that this retention motif is transferable. Water 72-77 aquaporin 1 (Colton blood group) Homo sapiens 24-35 19787701-9 2009 In contrary, RNA interference vector-mediated low expression of AQP1 in HT20 cells reduced relative plasma membrane water permeability and migration rate. Water 116-121 aquaporin 1 (Colton blood group) Homo sapiens 64-68 19484468-5 2009 However, pCMBS, which inhibits AQP1, the major water exchange pathway, inhibited flickering in all cells, and yet it was restored by the membrane intercalating species dibutyl phthalate (DBP). Water 47-52 aquaporin 1 (Colton blood group) Homo sapiens 31-35 19584911-0 2009 AQP1 is not only a water channel: it contributes to cell migration through Lin7/beta-catenin. Water 19-24 aquaporin 1 (Colton blood group) Homo sapiens 0-4 19574955-4 2009 We report that three point mutations turned the water-specific AQP1 into a proton/alkali cation channel with reduced water permeability and the permeability sequence: H(+) >>K(+) >Rb(+) >Na(+) >Cs(+) >Li(+). Water 48-53 aquaporin 1 (Colton blood group) Homo sapiens 63-67 19574955-4 2009 We report that three point mutations turned the water-specific AQP1 into a proton/alkali cation channel with reduced water permeability and the permeability sequence: H(+) >>K(+) >Rb(+) >Na(+) >Cs(+) >Li(+). Water 117-122 aquaporin 1 (Colton blood group) Homo sapiens 63-67 19424603-5 2009 UV and H2O2 as well as AQP1-specific siRNA knockdown impaired water permeability of ARPE-19 cells. Water 62-67 aquaporin 1 (Colton blood group) Homo sapiens 23-27 19406128-2 2009 Based on the electron crystallographic structure of AQP1, the hydrogen-bond isolation mechanism was proposed to explain why AQPs are impermeable to protons despite their very fast water conduction. Water 180-185 aquaporin 1 (Colton blood group) Homo sapiens 52-56 19383790-4 2009 Unlike the case in the structures of water-selective AQPs AqpZ and AQP1, the asparagines of the 2 Asn-Pro-Ala motifs do not hydrogen bond to the same water molecule; instead, they bond to 2 different water molecules in the center of the channel. Water 37-42 aquaporin 1 (Colton blood group) Homo sapiens 67-71 19472194-4 2009 Plasma membrane osmotic water permeability analysis, measured by YFP-based fluorescence quenching method and Xenopus oocyte expression assays, demonstrated that NPA1 or NPA2 deletion significantly reduced human AQP1 water permeability nearly 50% compared to wild-type AQP1, while NPA1,2 double deletion had little effect on human AQP1 water permeability. Water 216-221 aquaporin 1 (Colton blood group) Homo sapiens 211-215 19472194-4 2009 Plasma membrane osmotic water permeability analysis, measured by YFP-based fluorescence quenching method and Xenopus oocyte expression assays, demonstrated that NPA1 or NPA2 deletion significantly reduced human AQP1 water permeability nearly 50% compared to wild-type AQP1, while NPA1,2 double deletion had little effect on human AQP1 water permeability. Water 216-221 aquaporin 1 (Colton blood group) Homo sapiens 211-215 19096773-8 2009 We also summarize data on the modification of pore selectivity of the prototypical water-specific mammalian aquaporin-1. Water 83-88 aquaporin 1 (Colton blood group) Homo sapiens 108-119 19270200-9 2009 During PD, AQP1 plays an essential role in water permeability and ultrafiltration (UF), modulating processes such as endothelial permeability and angiogenesis. Water 43-48 aquaporin 1 (Colton blood group) Homo sapiens 11-15 19114109-3 2009 Here, we report the effect of inhibitors on water conduction by AQP4 and AQP1 reconstituted into liposomes. Water 44-49 aquaporin 1 (Colton blood group) Homo sapiens 73-77 19096784-4 2009 AQP1 is present in both apical and basolateral membranes of proximal tubules, and in descending limbs of Henle"s loop where 70% of filtrated water is isoosmotically reabsorbed (King and Agre 1996). Water 141-146 aquaporin 1 (Colton blood group) Homo sapiens 0-4 18811940-0 2008 Structural and functional divergence of two fish aquaporin-1 water channels following teleost-specific gene duplication. Water 61-66 aquaporin 1 (Colton blood group) Homo sapiens 49-60 20224214-0 2009 Aquaporin 1 water channel is overexpressed in the plasma membranes of pancreatic ducts in patients with autoimmune pancreatitis. Water 12-17 aquaporin 1 (Colton blood group) Homo sapiens 0-11 20224214-4 2009 Among them aquaporin 1 (AQP1) is a predominant water channel expressed in the plasma membranes of human pancreatic ducts. Water 47-52 aquaporin 1 (Colton blood group) Homo sapiens 11-22 20224214-4 2009 Among them aquaporin 1 (AQP1) is a predominant water channel expressed in the plasma membranes of human pancreatic ducts. Water 47-52 aquaporin 1 (Colton blood group) Homo sapiens 24-28 18841368-1 2008 Aquaporin1 (AQP1) is a water channel protein which facilitates water flux across cell membranes. Water 23-28 aquaporin 1 (Colton blood group) Homo sapiens 0-10 18841368-1 2008 Aquaporin1 (AQP1) is a water channel protein which facilitates water flux across cell membranes. Water 23-28 aquaporin 1 (Colton blood group) Homo sapiens 12-16 18509662-0 2008 Close association of water channel AQP1 with amyloid-beta deposition in Alzheimer disease brains. Water 21-26 aquaporin 1 (Colton blood group) Homo sapiens 35-39 18509662-1 2008 Aquaporin-1 (AQP1), a membrane water channel protein, is expressed exclusively in the choroid plexus epithelium in the central nervous system under physiological conditions. Water 31-36 aquaporin 1 (Colton blood group) Homo sapiens 0-11 18509662-1 2008 Aquaporin-1 (AQP1), a membrane water channel protein, is expressed exclusively in the choroid plexus epithelium in the central nervous system under physiological conditions. Water 31-36 aquaporin 1 (Colton blood group) Homo sapiens 13-17 18509662-2 2008 However, AQP1 expression is enhanced in reactive astrocytes, accumulating in brain lesions of Creutzfeldt-Jakob disease and multiple sclerosis, suggesting a role of AQP1-expressing astrocytes in brain water homeostasis under pathological conditions. Water 201-206 aquaporin 1 (Colton blood group) Homo sapiens 9-13 18392839-1 2008 Transmembrane water transport is mediated by aquaporins (AQPs), of which AQP1 and AQP4 are expressed in skeletal muscle. Water 14-19 aquaporin 1 (Colton blood group) Homo sapiens 73-77 18509662-2 2008 However, AQP1 expression is enhanced in reactive astrocytes, accumulating in brain lesions of Creutzfeldt-Jakob disease and multiple sclerosis, suggesting a role of AQP1-expressing astrocytes in brain water homeostasis under pathological conditions. Water 201-206 aquaporin 1 (Colton blood group) Homo sapiens 165-169 18196268-3 2008 In this paper, we identified the binding site for tetraethylammonium (TEA) of the membrane water channel aquaporin-1 by a combined molecular docking and molecular dynamics simulation approach. Water 91-96 aquaporin 1 (Colton blood group) Homo sapiens 105-116 18538351-10 2008 Thus, modulation of AQP1 expression by maternal hormones may regulate invasion and fetal-placental-amnion water homeostasis during gestation. Water 106-111 aquaporin 1 (Colton blood group) Homo sapiens 20-24 18280225-2 2008 AQP1 and AQP5 expressed in lung provide the principal route for osmotically driven water transport. Water 83-88 aquaporin 1 (Colton blood group) Homo sapiens 0-4 18544259-1 2008 OBJECTIVE: Aquaporin-1 (AQP1), the osmotic water channel, is located in choroidal plexus, which facilitates the cerebrospinal fluid formation in central nervous system (CNS). Water 43-48 aquaporin 1 (Colton blood group) Homo sapiens 11-22 18544259-1 2008 OBJECTIVE: Aquaporin-1 (AQP1), the osmotic water channel, is located in choroidal plexus, which facilitates the cerebrospinal fluid formation in central nervous system (CNS). Water 43-48 aquaporin 1 (Colton blood group) Homo sapiens 24-28 18544259-2 2008 AQP1 has been speculated to maintain the homeostasis of intracellular and extracellular water in the brain, while the intractable epilepsy (IE) may be related to the imbalance in water and ion homeostasis. Water 88-93 aquaporin 1 (Colton blood group) Homo sapiens 0-4 18544259-6 2008 CONCLUSION: For the first time, we showed high expression of AQP1 water channels in IE cases and suggest two mechanisms to explain this finding. Water 66-71 aquaporin 1 (Colton blood group) Homo sapiens 61-65 17894331-6 2008 It is also found that the number of water molecules hydrating the ions is reduced as the ions enter the pore, implying that the energetic cost for detaching water molecules from a permeating ion also contributes to the free energy barriers of ion transport in AQP1. Water 36-41 aquaporin 1 (Colton blood group) Homo sapiens 260-264 18275976-1 2008 Aquaporin 1 (AQP1) was first purified from red blood cell membranes and is now known to be an osmolarity-driven water transporter that is widely expressed in many epithelial and endothelial cells outside the brain. Water 112-117 aquaporin 1 (Colton blood group) Homo sapiens 0-11 18275976-1 2008 Aquaporin 1 (AQP1) was first purified from red blood cell membranes and is now known to be an osmolarity-driven water transporter that is widely expressed in many epithelial and endothelial cells outside the brain. Water 112-117 aquaporin 1 (Colton blood group) Homo sapiens 13-17 17894331-6 2008 It is also found that the number of water molecules hydrating the ions is reduced as the ions enter the pore, implying that the energetic cost for detaching water molecules from a permeating ion also contributes to the free energy barriers of ion transport in AQP1. Water 157-162 aquaporin 1 (Colton blood group) Homo sapiens 260-264 18282122-2 2008 Currently, 13 human AQPs are known and they are divided into two subgroups according to their ability to transport only water molecules, such as AQP1, or also glycerol and other small solutes. Water 120-125 aquaporin 1 (Colton blood group) Homo sapiens 145-149 18202181-2 2008 We studied the selectivity of aquaporin-1 (AQP1) and the bacterial glycerol facilitator, GlpF, for O(2), CO(2), NH(3), glycerol, urea, and water. Water 139-144 aquaporin 1 (Colton blood group) Homo sapiens 30-41 17942963-1 2007 In mammalian kidneys, aquaporin-1 is responsible for water reabsorption along the proximal tubule and is also thought to be involved in the concentration of urine that occurs in the medulla. Water 53-58 aquaporin 1 (Colton blood group) Homo sapiens 22-33 17941896-2 2008 Recent studies indicate that the aquaporin-1 (AQP1) water channel is expressed in human and equine articular chondrocytes. Water 52-57 aquaporin 1 (Colton blood group) Homo sapiens 33-44 17941896-2 2008 Recent studies indicate that the aquaporin-1 (AQP1) water channel is expressed in human and equine articular chondrocytes. Water 52-57 aquaporin 1 (Colton blood group) Homo sapiens 46-50 17941896-8 2008 Relative plasma membrane water permeability of AQP1(+/+) chondrocytes was approximately 1.6-fold higher than that of AQP1(-/-) chondrocytes. Water 25-30 aquaporin 1 (Colton blood group) Homo sapiens 47-51 17941896-14 2008 The results provided direct evidence that AQP1-mediated plasma membrane water permeability plays an important role in chondrocyte migration and adhesion. Water 72-77 aquaporin 1 (Colton blood group) Homo sapiens 42-46 17638023-6 2008 An insufficient function of the water-selective aquaporin 1 (AQP-1) channel may also be causative for inadequate ultrafiltration. Water 32-37 aquaporin 1 (Colton blood group) Homo sapiens 48-59 17638023-6 2008 An insufficient function of the water-selective aquaporin 1 (AQP-1) channel may also be causative for inadequate ultrafiltration. Water 32-37 aquaporin 1 (Colton blood group) Homo sapiens 61-66 17664179-1 2007 BACKGROUND: Aquaporin-1 (AQP-1) dysfunction is one of the valid theories for decreased free water transport (FWT) in long-term peritoneal dialysis (PD) ultrafiltration failure (UFF). Water 92-97 aquaporin 1 (Colton blood group) Homo sapiens 12-23 17664179-1 2007 BACKGROUND: Aquaporin-1 (AQP-1) dysfunction is one of the valid theories for decreased free water transport (FWT) in long-term peritoneal dialysis (PD) ultrafiltration failure (UFF). Water 92-97 aquaporin 1 (Colton blood group) Homo sapiens 25-30 17331768-6 2007 AQP 1 was localized in the endothelium of subepidermal capillaries and serves as a pathway for water absorption in series with the apical and basolateral membranes of the epithelium. Water 95-100 aquaporin 1 (Colton blood group) Homo sapiens 0-5 17869538-5 2007 Water channel activity of this purified hAQP1 was verified by reconstitution into proteoliposomes and performing stopped-flow vesicle shrinkage measurements. Water 0-5 aquaporin 1 (Colton blood group) Homo sapiens 40-45 17618150-6 2007 AQP1 may have a major osmoregulatory role in water transport in kidney and gut in SW-acclimated fish, whereas AQP3 could be implicated in gill water transport in FW-acclimated fish. Water 45-50 aquaporin 1 (Colton blood group) Homo sapiens 0-4 17320442-10 2007 As AQP-1 functions to allow water movement across mammalian cell membranes, its presence in water-permeable cells in a bird suggests it may have a similar function. Water 28-33 aquaporin 1 (Colton blood group) Homo sapiens 3-8 17449664-6 2007 The p(f) matrices from molecular dynamics simulations of five aquaporins (AQP0, AQP1, AQP4, AqpZ, and GlpF) indicated that the reduction in the water correlation across the Asn-Pro-Ala region, and the small local permeability around the ar/R region, characterize the transport efficiency of water. Water 144-149 aquaporin 1 (Colton blood group) Homo sapiens 80-84 17449664-7 2007 These structural determinants in water permeation were confirmed in molecular dynamics simulations of three mutants of AqpZ, which mimic AQP1. Water 33-38 aquaporin 1 (Colton blood group) Homo sapiens 137-141 17549682-9 2007 Reintroducing either AQP1 or AQP4 stably into glioma cell lines allowed us to show that each AQP is sufficient to restore water permeability. Water 122-127 aquaporin 1 (Colton blood group) Homo sapiens 21-25 17320442-10 2007 As AQP-1 functions to allow water movement across mammalian cell membranes, its presence in water-permeable cells in a bird suggests it may have a similar function. Water 92-97 aquaporin 1 (Colton blood group) Homo sapiens 3-8 16935571-1 2007 The passage of water through the aquaporin-1 (AQP1) transmembrane channel protein of the human erythrocyte is known to be inhibited by organic mercurials such as p-chloromercuribenzoate (pCMB), which react with the free SH-group of the critical cysteine (Cys189) located near the constriction of the AQP1 water-specific channel. Water 15-20 aquaporin 1 (Colton blood group) Homo sapiens 33-44 17645239-7 2007 These immunohistochemical results indicate that the expression not only of AQP4 but also of AQP1 was enhanced in MS and ischemic brain lesions located predominantly in astrocytes, suggesting a pivotal role of astrocytic AQP in the maintenance of water homeostasis in the CNS under pathological conditions. Water 246-251 aquaporin 1 (Colton blood group) Homo sapiens 92-96 21136710-1 2007 Human aquaporin-1 (AQP1) is the most studied member of the aquaporin family, acting as molecular water channel. Water 97-102 aquaporin 1 (Colton blood group) Homo sapiens 6-17 21136710-1 2007 Human aquaporin-1 (AQP1) is the most studied member of the aquaporin family, acting as molecular water channel. Water 97-102 aquaporin 1 (Colton blood group) Homo sapiens 19-23 16935571-1 2007 The passage of water through the aquaporin-1 (AQP1) transmembrane channel protein of the human erythrocyte is known to be inhibited by organic mercurials such as p-chloromercuribenzoate (pCMB), which react with the free SH-group of the critical cysteine (Cys189) located near the constriction of the AQP1 water-specific channel. Water 15-20 aquaporin 1 (Colton blood group) Homo sapiens 46-50 16935571-1 2007 The passage of water through the aquaporin-1 (AQP1) transmembrane channel protein of the human erythrocyte is known to be inhibited by organic mercurials such as p-chloromercuribenzoate (pCMB), which react with the free SH-group of the critical cysteine (Cys189) located near the constriction of the AQP1 water-specific channel. Water 15-20 aquaporin 1 (Colton blood group) Homo sapiens 300-304 16935571-1 2007 The passage of water through the aquaporin-1 (AQP1) transmembrane channel protein of the human erythrocyte is known to be inhibited by organic mercurials such as p-chloromercuribenzoate (pCMB), which react with the free SH-group of the critical cysteine (Cys189) located near the constriction of the AQP1 water-specific channel. Water 305-310 aquaporin 1 (Colton blood group) Homo sapiens 33-44 16935571-1 2007 The passage of water through the aquaporin-1 (AQP1) transmembrane channel protein of the human erythrocyte is known to be inhibited by organic mercurials such as p-chloromercuribenzoate (pCMB), which react with the free SH-group of the critical cysteine (Cys189) located near the constriction of the AQP1 water-specific channel. Water 305-310 aquaporin 1 (Colton blood group) Homo sapiens 46-50 16935571-1 2007 The passage of water through the aquaporin-1 (AQP1) transmembrane channel protein of the human erythrocyte is known to be inhibited by organic mercurials such as p-chloromercuribenzoate (pCMB), which react with the free SH-group of the critical cysteine (Cys189) located near the constriction of the AQP1 water-specific channel. Water 305-310 aquaporin 1 (Colton blood group) Homo sapiens 300-304 17692010-3 2007 Since the molecular identification of the first water channel, AQP1, by Peter Agre"s group, 13 homologous members have been found in mammals with varying degree of homology. Water 48-53 aquaporin 1 (Colton blood group) Homo sapiens 63-67 18045170-5 2007 Recognizing that AQP1 is a water channel and, under permissive conditions, also a cGMP-gated cation channel, evidence in various tissues for a coupling of the cGMP signaling cascade to a physiological outcome that might involve AQP1 dual ion-and-water channel functions is of interest. Water 27-32 aquaporin 1 (Colton blood group) Homo sapiens 17-21 17120021-9 2007 Water molecules follow across the epithelium mainly through the water channel, AQP1, driven by the created ionic gradient. Water 0-5 aquaporin 1 (Colton blood group) Homo sapiens 79-83 17120021-9 2007 Water molecules follow across the epithelium mainly through the water channel, AQP1, driven by the created ionic gradient. Water 64-69 aquaporin 1 (Colton blood group) Homo sapiens 79-83 17123487-2 2007 Expression levels of the water channels aquaporin 1 and aquaporin 4 (AQP1, AQP4) were examined in AD cases by gel electrophoresis and Western blotting, and densitometric values normalized with beta-actin were compared with corresponding values in age-matched controls processed in parallel. Water 25-30 aquaporin 1 (Colton blood group) Homo sapiens 40-51 17123487-2 2007 Expression levels of the water channels aquaporin 1 and aquaporin 4 (AQP1, AQP4) were examined in AD cases by gel electrophoresis and Western blotting, and densitometric values normalized with beta-actin were compared with corresponding values in age-matched controls processed in parallel. Water 25-30 aquaporin 1 (Colton blood group) Homo sapiens 69-73 17123487-10 2007 These results indicate abnormal expression of AQP1 in astrocytes in AD, and they add support to the idea that abnormal regulation of mechanisms involved in the control of water fluxes occurs at early stages in AD. Water 171-176 aquaporin 1 (Colton blood group) Homo sapiens 46-50 18045170-5 2007 Recognizing that AQP1 is a water channel and, under permissive conditions, also a cGMP-gated cation channel, evidence in various tissues for a coupling of the cGMP signaling cascade to a physiological outcome that might involve AQP1 dual ion-and-water channel functions is of interest. Water 246-251 aquaporin 1 (Colton blood group) Homo sapiens 17-21 18045170-5 2007 Recognizing that AQP1 is a water channel and, under permissive conditions, also a cGMP-gated cation channel, evidence in various tissues for a coupling of the cGMP signaling cascade to a physiological outcome that might involve AQP1 dual ion-and-water channel functions is of interest. Water 246-251 aquaporin 1 (Colton blood group) Homo sapiens 228-232 16871401-3 2006 The present study examines, by gel electrophoresis and Western blotting, the expression levels of the water channels aquaporin 1 (AQP1) and aquaporin 4 (AQP4) in the frontal cortex (area 8) homogenates of sporadic CJD cases (six men, four women; seven cases with methionine/methionine at codon 129 and PrP type 1; two cases with valine/valine at codon 129 and PrP type 2, and one case methionine/valine at codon 129 and PrP type 1) compared with age-matched controls, and cases with Alzheimer"s disease (AD, stage VI of Braak and Braak) and diffuse Lewy body disease (DLB). Water 102-107 aquaporin 1 (Colton blood group) Homo sapiens 117-128 17222168-1 2007 The discovery of aquaporin-1 (AQP1) explained the long-standing biophysical question of how water specifically crosses biological membranes. Water 92-97 aquaporin 1 (Colton blood group) Homo sapiens 17-28 17222168-1 2007 The discovery of aquaporin-1 (AQP1) explained the long-standing biophysical question of how water specifically crosses biological membranes. Water 92-97 aquaporin 1 (Colton blood group) Homo sapiens 30-34 16871401-3 2006 The present study examines, by gel electrophoresis and Western blotting, the expression levels of the water channels aquaporin 1 (AQP1) and aquaporin 4 (AQP4) in the frontal cortex (area 8) homogenates of sporadic CJD cases (six men, four women; seven cases with methionine/methionine at codon 129 and PrP type 1; two cases with valine/valine at codon 129 and PrP type 2, and one case methionine/valine at codon 129 and PrP type 1) compared with age-matched controls, and cases with Alzheimer"s disease (AD, stage VI of Braak and Braak) and diffuse Lewy body disease (DLB). Water 102-107 aquaporin 1 (Colton blood group) Homo sapiens 130-134 16865795-0 2006 Comment on: cloning and characterization of porcine aquaporin 1 water channel expressed extensively in the gastrointestinal system. Water 64-69 aquaporin 1 (Colton blood group) Homo sapiens 52-63 17543213-1 2006 A critical analysis of the discovery of the first water channel protein (later called aquaporin 1) has been performed. Water 50-55 aquaporin 1 (Colton blood group) Homo sapiens 86-97 17543216-9 2006 We have thus a world priority in the discovery of the first water channel in the RBC membrane, that was re-discovered by chance by the group of Agre (Baltimore, USA) in 1988, when they isolated a new protein from the RBC membrane, nick-named CHIP28 (channel-forming integral membrane protein of 28 kDa). Water 60-65 aquaporin 1 (Colton blood group) Homo sapiens 242-248 17543216-9 2006 We have thus a world priority in the discovery of the first water channel in the RBC membrane, that was re-discovered by chance by the group of Agre (Baltimore, USA) in 1988, when they isolated a new protein from the RBC membrane, nick-named CHIP28 (channel-forming integral membrane protein of 28 kDa). Water 60-65 aquaporin 1 (Colton blood group) Homo sapiens 250-301 17543216-11 2006 Only in 1992 the Agre"s group suggested that "it is likely that CHIP28 is a functional unit of membrane water channels". Water 104-109 aquaporin 1 (Colton blood group) Homo sapiens 64-70 17012249-6 2006 2) pCMBS, an inhibitor of the AQP1 water channel, reduces P(CO2) of RBCs solely by action on AQP1 as it has no effect in AQP1-deficient RBCs. Water 35-40 aquaporin 1 (Colton blood group) Homo sapiens 30-34 17009073-7 2006 Abnormalities in water channels aquaporin (AQP)1 and AQP2, as well as in the vasopressin receptor V2R, are known to cause nephrogenic diabetes insipidus. Water 17-22 aquaporin 1 (Colton blood group) Homo sapiens 43-48 16872579-10 2006 AQP1, 5 are strictly water channels. Water 21-26 aquaporin 1 (Colton blood group) Homo sapiens 0-4 16814974-10 2006 These results in human fetal brain lend morphological support to the previous findings that aquaporin-1 and aquaporin-4 play different roles in the regulation of the water homeostasis of the brain. Water 166-171 aquaporin 1 (Colton blood group) Homo sapiens 92-103 18095114-11 2006 The fact that AQP-1 was highly expressed at the dural attachment and invading front of meningioma may indicate that dural invasion of the meningioma may be facilitated by AQP-1-induced water flow and neovascularization. Water 185-190 aquaporin 1 (Colton blood group) Homo sapiens 14-19 16756992-4 2006 The extracellular-side constriction region of this AQP0 structure was significantly larger than that of the EM-based model and similar to that of the highly water permeable AQP1. Water 157-162 aquaporin 1 (Colton blood group) Homo sapiens 173-177 16481371-5 2006 The water channel, aquaporin (AQP) 1, was predominantly situated in the apical plasma membrane domain, although distinct basolateral and endothelial immunoreactivity was also observed. Water 4-9 aquaporin 1 (Colton blood group) Homo sapiens 30-36 16551622-6 2006 TEA inhibition was lost upon a Tyr to Phe amino acid switch in the external water pore of AQP1/AQP2/AQP4, whereas the water permeability of AQP3 and AQP5, which lack a corresponding Tyr, was not blocked by TEA. Water 76-81 aquaporin 1 (Colton blood group) Homo sapiens 90-94 16551622-7 2006 Consistent with experimental data, multi-nanosecond molecular dynamics simulations showed one stable binding site for TEA, but not tetramethyl (TMA), in AQP1, resulting in a nearly 50% water permeability inhibition, which was reduced in AQP1-Y186F due to effects on the TEA inhibitory binding region. Water 185-190 aquaporin 1 (Colton blood group) Homo sapiens 153-157 16682607-3 2006 The water channel aquaporin-1 transports low molecular weight gases in addition to water and is expressed in cells that produce or are the targets of NO. Water 4-9 aquaporin 1 (Colton blood group) Homo sapiens 18-29 16682607-5 2006 In cells expressing aquaporin-1, NO permeability correlated with water permeability. Water 65-70 aquaporin 1 (Colton blood group) Homo sapiens 20-31 16534779-0 2006 Localization of aquaporin-1 water channel in glial cells of the human peripheral nervous system. Water 28-33 aquaporin 1 (Colton blood group) Homo sapiens 16-27 16534779-2 2006 AQP1, AQP4, and AQP9 have been identified in the central nervous system and demonstrated or proposed to play important roles in brain water homeostasis. Water 134-139 aquaporin 1 (Colton blood group) Homo sapiens 0-4 16534779-4 2006 Here we report that the AQP1 water channel is specifically localized to glial cells of the peripheral nervous system by immunohistochemistry, RT-PCR, and immunoblotting. Water 29-34 aquaporin 1 (Colton blood group) Homo sapiens 24-28 18095114-11 2006 The fact that AQP-1 was highly expressed at the dural attachment and invading front of meningioma may indicate that dural invasion of the meningioma may be facilitated by AQP-1-induced water flow and neovascularization. Water 185-190 aquaporin 1 (Colton blood group) Homo sapiens 171-176 16749244-8 2006 For example, the flow rate of water through AQP1 is an extraordinary three billion water molecules per second per aquaporin channel, while a relative trickle of water crosses the hydrophobic lipid bilayer of cell membranes devoid of AQPs. Water 30-35 aquaporin 1 (Colton blood group) Homo sapiens 44-48 16749244-8 2006 For example, the flow rate of water through AQP1 is an extraordinary three billion water molecules per second per aquaporin channel, while a relative trickle of water crosses the hydrophobic lipid bilayer of cell membranes devoid of AQPs. Water 83-88 aquaporin 1 (Colton blood group) Homo sapiens 44-48 16749244-8 2006 For example, the flow rate of water through AQP1 is an extraordinary three billion water molecules per second per aquaporin channel, while a relative trickle of water crosses the hydrophobic lipid bilayer of cell membranes devoid of AQPs. Water 83-88 aquaporin 1 (Colton blood group) Homo sapiens 44-48 16480680-0 2006 Acetazolamide inhibits osmotic water permeability by interaction with aquaporin-1. Water 31-36 aquaporin 1 (Colton blood group) Homo sapiens 70-81 16480680-6 2006 Acetazolamide, at concentrations of 1 and 10muM, inhibited the osmotic water permeability in HEK293 cells transfected with pEGFP/AQP1. Water 71-76 aquaporin 1 (Colton blood group) Homo sapiens 129-133 16480680-10 2006 This study demonstrated that acetazolamide inhibited osmotic water permeability through interaction with AQP1. Water 61-66 aquaporin 1 (Colton blood group) Homo sapiens 105-109 16522429-3 2006 Previous studies from our laboratory have shown that the water channel aquaporin 1 (AQP1) is expressed in human fetal membranes from term pregnancies with normal amniotic fluid (AF) volume. Water 57-62 aquaporin 1 (Colton blood group) Homo sapiens 71-82 16522429-3 2006 Previous studies from our laboratory have shown that the water channel aquaporin 1 (AQP1) is expressed in human fetal membranes from term pregnancies with normal amniotic fluid (AF) volume. Water 57-62 aquaporin 1 (Colton blood group) Homo sapiens 84-88 16225876-2 2005 The single-channel water permeability, pf, was evaluated to be GlpF approximately AQPZ > AQP1 >> AQP0, while their relative pore sizes were GlpF >> AQP1 > AQPZ >> AQP0. Water 19-24 aquaporin 1 (Colton blood group) Homo sapiens 92-96 16720988-6 2006 Aquaporin-1, water-only channels, are important for solute-free water transport from blood capillaries. Water 13-18 aquaporin 1 (Colton blood group) Homo sapiens 0-11 16720988-6 2006 Aquaporin-1, water-only channels, are important for solute-free water transport from blood capillaries. Water 64-69 aquaporin 1 (Colton blood group) Homo sapiens 0-11 16133142-4 2005 We describe the temporal expression and appearance of aquaporin-1 (AQP1) which is important for water transfer across adult choroid plexuses. Water 96-101 aquaporin 1 (Colton blood group) Homo sapiens 54-65 16133142-4 2005 We describe the temporal expression and appearance of aquaporin-1 (AQP1) which is important for water transfer across adult choroid plexuses. Water 96-101 aquaporin 1 (Colton blood group) Homo sapiens 67-71 16407156-1 2006 Water-specific aquaporins (AQP), such as the prototypical mammalian AQP1, stringently exclude the passage of solutes, ions, and even protons. Water 0-5 aquaporin 1 (Colton blood group) Homo sapiens 68-72 16539309-6 2006 CONCLUSION: We have established a high expression of AQP1 water channels in nasal polyp tissue and have suggested two mechanisms to explain this finding. Water 58-63 aquaporin 1 (Colton blood group) Homo sapiens 53-57 16719363-7 2006 Subsequently, our studies demonstrated that the water channel aquaporin-1 (AQP1) is also present at the zymogen granule membrane and participates in rapid GTP-induced and G(alphai3)-mediated vesicular water gating and swelling. Water 48-53 aquaporin 1 (Colton blood group) Homo sapiens 75-79 16225876-2 2005 The single-channel water permeability, pf, was evaluated to be GlpF approximately AQPZ > AQP1 >> AQP0, while their relative pore sizes were GlpF >> AQP1 > AQPZ >> AQP0. Water 19-24 aquaporin 1 (Colton blood group) Homo sapiens 163-167 15949534-3 2005 The necessarily high water permeability of the choroid plexus barrier is made possible by the abundant expression of a water channel, Aquaporin-1 (AQP1), on the apical side of the membrane from early stages of development through adulthood. Water 21-26 aquaporin 1 (Colton blood group) Homo sapiens 134-145 16179736-2 2005 A G alphai3-phospholipase A2 (PLA2)-mediated involvement of the water channel aquaporin-1 (AQP1) in the regulation of secretory vesicle swelling in the exocrine pancreas has been previously reported. Water 64-69 aquaporin 1 (Colton blood group) Homo sapiens 91-95 16179736-4 2005 Results from the study demonstrate that water channels AQP1 and AQP6, and the heterotrimeric Go protein are associated with SVs and participate in their swelling. Water 40-45 aquaporin 1 (Colton blood group) Homo sapiens 55-59 15964017-8 2005 Superposition of the SoPIP2;1 potential map with the atomic model of AQP1 demonstrates the generally well conserved overall structure of water channels. Water 137-142 aquaporin 1 (Colton blood group) Homo sapiens 69-73 15901245-1 2005 Following the discovery of the aquaporin-1 water channel over a decade ago, molecular techniques have been developed to examine the role of renal aquaporin water channels under numerous physiological and pathological conditions. Water 43-48 aquaporin 1 (Colton blood group) Homo sapiens 31-42 15958180-0 2005 Establishment of HEK293 cell line expressing green fluorescent protein-aquaporin-1 to determine osmotic water permeability. Water 104-109 aquaporin 1 (Colton blood group) Homo sapiens 71-82 15958180-2 2005 The present study aimed to establish a cell line stably transfected with AQP1 to measure osmotic water permeability. Water 97-102 aquaporin 1 (Colton blood group) Homo sapiens 73-77 15958180-7 2005 The typical AQP1 inhibitor, mercuric chloride, validated this osmotic water permeability assay. Water 70-75 aquaporin 1 (Colton blood group) Homo sapiens 12-16 15809704-0 2005 Heterogeneous expression of the aquaporin 1 (AQP1) water channel in tumors of the prostate, breast, ovary, colon and lung: a study using high density multiple human tumor tissue microarrays. Water 51-56 aquaporin 1 (Colton blood group) Homo sapiens 32-43 15809704-0 2005 Heterogeneous expression of the aquaporin 1 (AQP1) water channel in tumors of the prostate, breast, ovary, colon and lung: a study using high density multiple human tumor tissue microarrays. Water 51-56 aquaporin 1 (Colton blood group) Homo sapiens 45-49 15809704-1 2005 Aquaporin 1 (AQP1) water channels are membrane proteins that control the permeability of endothelial and epithelial barriers by facilitating water movement across cell membranes. Water 19-24 aquaporin 1 (Colton blood group) Homo sapiens 0-11 15809704-1 2005 Aquaporin 1 (AQP1) water channels are membrane proteins that control the permeability of endothelial and epithelial barriers by facilitating water movement across cell membranes. Water 19-24 aquaporin 1 (Colton blood group) Homo sapiens 13-17 15809704-1 2005 Aquaporin 1 (AQP1) water channels are membrane proteins that control the permeability of endothelial and epithelial barriers by facilitating water movement across cell membranes. Water 141-146 aquaporin 1 (Colton blood group) Homo sapiens 0-11 15809704-1 2005 Aquaporin 1 (AQP1) water channels are membrane proteins that control the permeability of endothelial and epithelial barriers by facilitating water movement across cell membranes. Water 141-146 aquaporin 1 (Colton blood group) Homo sapiens 13-17 15809704-9 2005 In conclusion, the AQP1 water channel is an excellent marker of microvasculature but it is heterogeneously expressed in different human tumors and not necessarily expressed in all neoplastic cells. Water 24-29 aquaporin 1 (Colton blood group) Homo sapiens 19-23 15949534-3 2005 The necessarily high water permeability of the choroid plexus barrier is made possible by the abundant expression of a water channel, Aquaporin-1 (AQP1), on the apical side of the membrane from early stages of development through adulthood. Water 21-26 aquaporin 1 (Colton blood group) Homo sapiens 147-151 15949534-3 2005 The necessarily high water permeability of the choroid plexus barrier is made possible by the abundant expression of a water channel, Aquaporin-1 (AQP1), on the apical side of the membrane from early stages of development through adulthood. Water 119-124 aquaporin 1 (Colton blood group) Homo sapiens 134-145 15949534-3 2005 The necessarily high water permeability of the choroid plexus barrier is made possible by the abundant expression of a water channel, Aquaporin-1 (AQP1), on the apical side of the membrane from early stages of development through adulthood. Water 119-124 aquaporin 1 (Colton blood group) Homo sapiens 147-151 15949534-12 2005 An appreciation of AQP1 as an ion channel in addition to its role as a water channel should offer new targets for therapeutic strategies in diseases involving water imbalance in the brain. Water 159-164 aquaporin 1 (Colton blood group) Homo sapiens 19-23 15557734-2 2004 The atomic structure of aquaporin-1 (AQP1) demonstrated how aquaporin is freely permeated by water but not protons and provided marked insight into several human disorders. Water 93-98 aquaporin 1 (Colton blood group) Homo sapiens 24-35 15667881-1 2005 OBJECTIVES: To investigate the immunoexpression of aquaporin-1 (AQP-1), a major transmembrane water channel, in high-grade varicocele testes, which are known to imply an unbalanced transmembrane water flow, in both tubular and extratubular compartments. Water 94-99 aquaporin 1 (Colton blood group) Homo sapiens 51-62 15667881-1 2005 OBJECTIVES: To investigate the immunoexpression of aquaporin-1 (AQP-1), a major transmembrane water channel, in high-grade varicocele testes, which are known to imply an unbalanced transmembrane water flow, in both tubular and extratubular compartments. Water 94-99 aquaporin 1 (Colton blood group) Homo sapiens 64-69 15770929-1 2005 BACKGROUND: In peritoneal dialysis, approximately 40% of the total osmotic ultrafiltration (UF) induced by glucose can be predicted to be due to "free" water transport across aquaporin-1 (APQ-1). Water 152-157 aquaporin 1 (Colton blood group) Homo sapiens 175-186 15667881-1 2005 OBJECTIVES: To investigate the immunoexpression of aquaporin-1 (AQP-1), a major transmembrane water channel, in high-grade varicocele testes, which are known to imply an unbalanced transmembrane water flow, in both tubular and extratubular compartments. Water 195-200 aquaporin 1 (Colton blood group) Homo sapiens 51-62 15667881-1 2005 OBJECTIVES: To investigate the immunoexpression of aquaporin-1 (AQP-1), a major transmembrane water channel, in high-grade varicocele testes, which are known to imply an unbalanced transmembrane water flow, in both tubular and extratubular compartments. Water 195-200 aquaporin 1 (Colton blood group) Homo sapiens 64-69 15557734-2 2004 The atomic structure of aquaporin-1 (AQP1) demonstrated how aquaporin is freely permeated by water but not protons and provided marked insight into several human disorders. Water 93-98 aquaporin 1 (Colton blood group) Homo sapiens 37-41 15135229-1 2004 Three water channel proteins, aquaporins, have been shown to be expressed in the placentae of humans and sheep-AQP1, 3, 8; AQP1 is in the vasculature, whereas AQP3, 8 are in the trophoblast cells. Water 6-11 aquaporin 1 (Colton blood group) Homo sapiens 111-115 15211447-1 2004 BACKGROUND: Aquaporin 1 (AQP-1) channels have been claimed to be responsible for osmotically driven free-water movement across the peritoneal membrane. Water 105-110 aquaporin 1 (Colton blood group) Homo sapiens 12-23 15211447-1 2004 BACKGROUND: Aquaporin 1 (AQP-1) channels have been claimed to be responsible for osmotically driven free-water movement across the peritoneal membrane. Water 105-110 aquaporin 1 (Colton blood group) Homo sapiens 25-30 15211447-2 2004 Data about AQP-1 expression and its location in the human peritoneum related to clinical findings concerning ultrafiltration (UF) and free-water transport are still lacking. Water 139-144 aquaporin 1 (Colton blood group) Homo sapiens 11-16 15211447-8 2004 Free-water transport through AQP-1 was 42% +/- 12% from total UF after 1 hour. Water 5-10 aquaporin 1 (Colton blood group) Homo sapiens 29-34 15211447-9 2004 There was a significant correlation between AQP-1 expression and free-water transport after 1 hour of equilibration with 3.86% glucose in the PET (r = 0.753; P < 0.001). Water 70-75 aquaporin 1 (Colton blood group) Homo sapiens 44-49 15211447-11 2004 AQP-1 expression correlated with free-water transport after 1 hour of equilibration, reaching a significant part from total UF at this time. Water 38-43 aquaporin 1 (Colton blood group) Homo sapiens 0-5 15071758-1 2004 The structures of the mammalian water transport protein Aqp1 and of its bacterial homologue GlpF enables us to test whether homology models can be used to explore relationships between structure, dynamics and function in mammalian transport proteins. Water 32-37 aquaporin 1 (Colton blood group) Homo sapiens 56-60 15071758-7 2004 The orientation of the dipoles of water molecules within the pore is of key importance in maintaining low proton permeability through Aqp1. Water 34-39 aquaporin 1 (Colton blood group) Homo sapiens 134-138 14592814-0 2004 Expression of the AQP-1 water channel in normal human tissues: a semiquantitative study using tissue microarray technology. Water 24-29 aquaporin 1 (Colton blood group) Homo sapiens 18-23 15024704-2 2004 The aim of the present investigation was to determine if human articular chondrocytes and synoviocytes express aquaporin 1 (AQP1) water channels and to establish if there are any alterations in AQP1 expression in osteoarticular disorders such as osteoarthritis (OA) and rheumatoid arthritis (RA). Water 130-135 aquaporin 1 (Colton blood group) Homo sapiens 124-128 15024704-12 2004 These findings suggest a potential role for AQP1 and possibly other members of the AQP gene family in the movement of extracellular matrix and metabolic water across the membranes of chondrocytes and synoviocytes for the purposes of chondrocyte volume regulation and synovial homeostasis. Water 153-158 aquaporin 1 (Colton blood group) Homo sapiens 44-48 14701836-1 2004 Aquaporin-1 (AQP1) is a membrane channel that allows rapid water movement driven by a transmembrane osmotic gradient. Water 59-64 aquaporin 1 (Colton blood group) Homo sapiens 0-11 14701836-1 2004 Aquaporin-1 (AQP1) is a membrane channel that allows rapid water movement driven by a transmembrane osmotic gradient. Water 59-64 aquaporin 1 (Colton blood group) Homo sapiens 13-17 14592814-2 2004 Aquaporin-1 (AQP-1) has been found to be important in osmotic water movement across cell membranes of epithelial and endothelial barriers. Water 62-67 aquaporin 1 (Colton blood group) Homo sapiens 0-11 14592814-2 2004 Aquaporin-1 (AQP-1) has been found to be important in osmotic water movement across cell membranes of epithelial and endothelial barriers. Water 62-67 aquaporin 1 (Colton blood group) Homo sapiens 13-18 14695248-0 2004 Theory and simulation of water permeation in aquaporin-1. Water 25-30 aquaporin 1 (Colton blood group) Homo sapiens 45-56 15561410-5 2004 Mercury inhibits the water permeability of AQP1 and AQP9, but not AQP4. Water 21-26 aquaporin 1 (Colton blood group) Homo sapiens 43-47 14759764-4 2004 AQP-1 and Galphai3 have been implicated in GTP-induced gating of water in zymogen granules (ZG), the secretory vesicles in exocrine pancreas. Water 65-70 aquaporin 1 (Colton blood group) Homo sapiens 0-5 15561411-8 2004 Aquaporin 1 mediates water transport at the apical membrane, but the route across the basolateral membrane is unknown. Water 21-26 aquaporin 1 (Colton blood group) Homo sapiens 0-11 15561408-1 2004 Each day, approximately 0.5-0.9 l of water diffuses through (primarily) aquaporin-1 (AQP1) channels in the human choroid plexus, into the cerebrospinal fluid of the brain ventricles and spinal cord central canal, through the ependymal cell lining, and into the parenchyma of the CNS. Water 37-42 aquaporin 1 (Colton blood group) Homo sapiens 72-83 15984652-7 2004 Half of the 2003 Nobel Prize in Chemistry was awarded to Peter Agre (Johns Hopkins University, Baltimore, USA) "for the discovery of water channels", actually the first water channel protein from the human red blood cell (RBC) membrane, known today as aquaporin 1 (AQP1). Water 133-138 aquaporin 1 (Colton blood group) Homo sapiens 252-263 15561408-1 2004 Each day, approximately 0.5-0.9 l of water diffuses through (primarily) aquaporin-1 (AQP1) channels in the human choroid plexus, into the cerebrospinal fluid of the brain ventricles and spinal cord central canal, through the ependymal cell lining, and into the parenchyma of the CNS. Water 37-42 aquaporin 1 (Colton blood group) Homo sapiens 85-89 15984652-7 2004 Half of the 2003 Nobel Prize in Chemistry was awarded to Peter Agre (Johns Hopkins University, Baltimore, USA) "for the discovery of water channels", actually the first water channel protein from the human red blood cell (RBC) membrane, known today as aquaporin 1 (AQP1). Water 133-138 aquaporin 1 (Colton blood group) Homo sapiens 265-269 15984652-7 2004 Half of the 2003 Nobel Prize in Chemistry was awarded to Peter Agre (Johns Hopkins University, Baltimore, USA) "for the discovery of water channels", actually the first water channel protein from the human red blood cell (RBC) membrane, known today as aquaporin 1 (AQP1). Water 169-174 aquaporin 1 (Colton blood group) Homo sapiens 252-263 14630322-2 2003 The atomic structure of mammalian AQP1 illustrates how this family of proteins is freely permeated by water but not protons (hydronium ions, H3O+). Water 102-107 aquaporin 1 (Colton blood group) Homo sapiens 34-38 12939380-10 2003 Preferential localization of AQP1 in the apical membrane of epithelial cells in the posterior intestine of seawater eel indicates that this region of the intestine is responsible for water absorption, and that AQP1 may act as a water entry site in the epithelial cells. Water 110-115 aquaporin 1 (Colton blood group) Homo sapiens 29-33 14561230-1 2003 BACKGROUND: Aquaporin-1 (AQP1) functions as an osmotic water channel and a gated cation channel. Water 55-60 aquaporin 1 (Colton blood group) Homo sapiens 12-23 14561230-1 2003 BACKGROUND: Aquaporin-1 (AQP1) functions as an osmotic water channel and a gated cation channel. Water 55-60 aquaporin 1 (Colton blood group) Homo sapiens 25-29 17986548-4 2003 Aquaporin-1 (AQP1) is constitutively expressed in the endothelial cells of the capillaries and venules that provide the ultrasmall pores predicted by the three-pore model of water movement during peritoneal dialysis. Water 174-179 aquaporin 1 (Colton blood group) Homo sapiens 0-11 17986548-4 2003 Aquaporin-1 (AQP1) is constitutively expressed in the endothelial cells of the capillaries and venules that provide the ultrasmall pores predicted by the three-pore model of water movement during peritoneal dialysis. Water 174-179 aquaporin 1 (Colton blood group) Homo sapiens 13-17 12824077-3 2003 However, by lowering transmural urea concentration gradients, UTB reduces water efflux from DVR through aquaporin-1 (AQP1) water channels, thereby decreasing plasma sodium concentration. Water 74-79 aquaporin 1 (Colton blood group) Homo sapiens 104-115 12824077-3 2003 However, by lowering transmural urea concentration gradients, UTB reduces water efflux from DVR through aquaporin-1 (AQP1) water channels, thereby decreasing plasma sodium concentration. Water 74-79 aquaporin 1 (Colton blood group) Homo sapiens 117-121 12824077-3 2003 However, by lowering transmural urea concentration gradients, UTB reduces water efflux from DVR through aquaporin-1 (AQP1) water channels, thereby decreasing plasma sodium concentration. Water 123-128 aquaporin 1 (Colton blood group) Homo sapiens 104-115 12824077-3 2003 However, by lowering transmural urea concentration gradients, UTB reduces water efflux from DVR through aquaporin-1 (AQP1) water channels, thereby decreasing plasma sodium concentration. Water 123-128 aquaporin 1 (Colton blood group) Homo sapiens 117-121 12939380-10 2003 Preferential localization of AQP1 in the apical membrane of epithelial cells in the posterior intestine of seawater eel indicates that this region of the intestine is responsible for water absorption, and that AQP1 may act as a water entry site in the epithelial cells. Water 183-188 aquaporin 1 (Colton blood group) Homo sapiens 29-33 12498798-0 2003 The structure of the aquaporin-1 water channel: a comparison between cryo-electron microscopy and X-ray crystallography. Water 33-38 aquaporin 1 (Colton blood group) Homo sapiens 21-32 12766090-0 2003 Aquaporin-1 channels in human retinal pigment epithelium: role in transepithelial water movement. Water 82-87 aquaporin 1 (Colton blood group) Homo sapiens 0-11 12766090-9 2003 In functional assays, AQP1 facilitated water movement across RPE monolayers in an expression-dependent manner in two complementary model systems. Water 39-44 aquaporin 1 (Colton blood group) Homo sapiens 22-26 12766090-10 2003 CONCLUSION: The expression of AQP1 by RPE in vivo probably contributes to the efficient transepithelial water transport across RPE, maintains retinal attachment, and prevents subretinal edema. Water 104-109 aquaporin 1 (Colton blood group) Homo sapiens 30-34 12676741-6 2003 The recent discoveries of aquaporin-1 (AQP1) water channels and the facilitated urea carrier UTB in DVR endothelia show that transcellular as well as paracellular pathways are involved in equilibration of DVR plasma with the interstitium. Water 45-50 aquaporin 1 (Colton blood group) Homo sapiens 26-37 12676741-6 2003 The recent discoveries of aquaporin-1 (AQP1) water channels and the facilitated urea carrier UTB in DVR endothelia show that transcellular as well as paracellular pathways are involved in equilibration of DVR plasma with the interstitium. Water 45-50 aquaporin 1 (Colton blood group) Homo sapiens 39-43 12676741-7 2003 Efflux of water across AQP1 excludes NaCl and urea, leading to the conclusion that both water abstraction and diffusion contribute to transmural equilibration. Water 10-15 aquaporin 1 (Colton blood group) Homo sapiens 23-27 12676741-7 2003 Efflux of water across AQP1 excludes NaCl and urea, leading to the conclusion that both water abstraction and diffusion contribute to transmural equilibration. Water 88-93 aquaporin 1 (Colton blood group) Homo sapiens 23-27 12529271-8 2003 In the hydropenic kidney, DVR plasma equilibrates with the interstitium both by diffusion and through water efflux across aquaporin-1. Water 102-107 aquaporin 1 (Colton blood group) Homo sapiens 122-133 12565698-1 2003 Following the discovery of the aquaporin-1 water channel in 1991, molecular techniques have been developed to examine the roles of renal aquaporins-1, -2, -3, and -4 in disorders of water balance. Water 43-48 aquaporin 1 (Colton blood group) Homo sapiens 31-42 12498798-1 2003 Three different medium-resolution structures of the human water channel aquaporin-1 (AQP1) have been solved by cryo-electron microscopy (cryo-EM) during the last two years. Water 58-63 aquaporin 1 (Colton blood group) Homo sapiens 72-83 12498798-1 2003 Three different medium-resolution structures of the human water channel aquaporin-1 (AQP1) have been solved by cryo-electron microscopy (cryo-EM) during the last two years. Water 58-63 aquaporin 1 (Colton blood group) Homo sapiens 85-89 12972274-8 2003 In 1992 Agre and coworkers suggested that CHIP28 is a functional unit of membrane water channels; by reconstitution in liposomes it was demonstrated that CHIP28 is a water channel itself rather than a water channel regulator. Water 82-87 aquaporin 1 (Colton blood group) Homo sapiens 42-48 12874954-1 2003 The discovery of aquaporin-1 (AQP1) by Agre and colleagues explained the long-standing biophysical question of how water specifically crosses biological membranes. Water 115-120 aquaporin 1 (Colton blood group) Homo sapiens 17-28 12874954-1 2003 The discovery of aquaporin-1 (AQP1) by Agre and colleagues explained the long-standing biophysical question of how water specifically crosses biological membranes. Water 115-120 aquaporin 1 (Colton blood group) Homo sapiens 30-34 12972274-8 2003 In 1992 Agre and coworkers suggested that CHIP28 is a functional unit of membrane water channels; by reconstitution in liposomes it was demonstrated that CHIP28 is a water channel itself rather than a water channel regulator. Water 82-87 aquaporin 1 (Colton blood group) Homo sapiens 154-160 12972274-8 2003 In 1992 Agre and coworkers suggested that CHIP28 is a functional unit of membrane water channels; by reconstitution in liposomes it was demonstrated that CHIP28 is a water channel itself rather than a water channel regulator. Water 166-171 aquaporin 1 (Colton blood group) Homo sapiens 42-48 12972274-8 2003 In 1992 Agre and coworkers suggested that CHIP28 is a functional unit of membrane water channels; by reconstitution in liposomes it was demonstrated that CHIP28 is a water channel itself rather than a water channel regulator. Water 166-171 aquaporin 1 (Colton blood group) Homo sapiens 154-160 12218304-1 2002 AIM: To determine whether glucose, NaCl and/or cholera toxin modify the expression of aquaporin-1 (AQP-1) water channel. Water 106-111 aquaporin 1 (Colton blood group) Homo sapiens 86-97 12457773-1 2002 Aquaporin-1 (AQP1) is a member of the diverse major intrinsic protein family of water and solute channels. Water 80-85 aquaporin 1 (Colton blood group) Homo sapiens 0-11 12457773-1 2002 Aquaporin-1 (AQP1) is a member of the diverse major intrinsic protein family of water and solute channels. Water 80-85 aquaporin 1 (Colton blood group) Homo sapiens 13-17 12457773-2 2002 AQP1 is known as an osmotic water channel in kidney, brain, vascular system and other tissues, and recently has been demonstrated to function as a cation channel gated by cGMP. Water 28-33 aquaporin 1 (Colton blood group) Homo sapiens 0-4 12457773-5 2002 Distinct pathways for fluxes of water and ions in the tetrameric AQP1 channel indicate an intriguing multifunctional capacity. Water 32-37 aquaporin 1 (Colton blood group) Homo sapiens 65-69 12388974-2 2002 Specifically, aquaporin 1 (AQP1) and aquaporin 3 (AQP3) have been found to be important in osmotic water movement across membranes. Water 99-104 aquaporin 1 (Colton blood group) Homo sapiens 14-25 12388974-2 2002 Specifically, aquaporin 1 (AQP1) and aquaporin 3 (AQP3) have been found to be important in osmotic water movement across membranes. Water 99-104 aquaporin 1 (Colton blood group) Homo sapiens 27-31 12388974-13 2002 AQP1 may play a role in water movement from the amniotic cavity across the placenta into the fetal circulation. Water 24-29 aquaporin 1 (Colton blood group) Homo sapiens 0-4 12218304-1 2002 AIM: To determine whether glucose, NaCl and/or cholera toxin modify the expression of aquaporin-1 (AQP-1) water channel. Water 106-111 aquaporin 1 (Colton blood group) Homo sapiens 99-104 12218304-5 2002 Hyperosmolar Reno-60 and Hypaque-76 contrast agents at 500 mosm/kg.H(2)O and isomolar Visipaque at 25% (v/v) concentration(s) also increased AQP-1 expression 3.8- to 5.0-fold (p < 0.01) in HRPTE cells which also were inhibited by cholera toxin from 41% (p < 0.05) to 71% (p < 0.01). Water 67-72 aquaporin 1 (Colton blood group) Homo sapiens 141-146 12172703-0 2002 Transmembrane water influx via aquaporin-1 is inhibited by barbiturates and propofol in red blood cells. Water 14-19 aquaporin 1 (Colton blood group) Homo sapiens 31-42 12237771-1 2002 Aquaporin 1 is a water channel protein. Water 17-22 aquaporin 1 (Colton blood group) Homo sapiens 0-11 12172703-1 2002 Aquaporin-1 (AQP1) is known to be expressed at a high level in endothelial cell membranes and participates in water transfer into or across these cells. Water 110-115 aquaporin 1 (Colton blood group) Homo sapiens 0-11 12172703-1 2002 Aquaporin-1 (AQP1) is known to be expressed at a high level in endothelial cell membranes and participates in water transfer into or across these cells. Water 110-115 aquaporin 1 (Colton blood group) Homo sapiens 13-17 12172703-8 2002 Efflux of water (shrinking) was also inhibited by HgCl(2), confirming a significant role of AQP1 in this model. Water 10-15 aquaporin 1 (Colton blood group) Homo sapiens 92-96 11914159-2 2002 Tetraethylammonium chloride (TEA; 0.05 to 10 mM) was shown previously to inhibit the osmotic water permeability of human AQP1 channels expressed in Xenopus oocytes. Water 93-98 aquaporin 1 (Colton blood group) Homo sapiens 121-125 12137754-1 2002 Analysis of osmotic water permeability of aquaporin (AQP) 1, AQP3 and AQP4, which are expressed in human small intestine, in the presence or absence of cholera toxin (CT) was performed using a Xenopus oocyte expression system. Water 20-25 aquaporin 1 (Colton blood group) Homo sapiens 42-59 11917120-0 2002 Aquaporin 1 regulates GTP-induced rapid gating of water in secretory vesicles. Water 50-55 aquaporin 1 (Colton blood group) Homo sapiens 0-11 11917120-3 2002 Evidence is presented here that the water channel aquaporin-1 (AQP1) is present in the ZG membrane and participates in rapid GTP-induced vesicular water gating and swelling. Water 36-41 aquaporin 1 (Colton blood group) Homo sapiens 63-67 12002613-0 2002 Localization and expression of the aquaporin-1 water channel in mesangial cells in the human glomerulus. Water 47-52 aquaporin 1 (Colton blood group) Homo sapiens 35-46 12002613-1 2002 The expression and localization of the aquaporin-1 (AQP1) water channel were examined in the glomeruli of the human kidney. Water 58-63 aquaporin 1 (Colton blood group) Homo sapiens 39-50 12002613-1 2002 The expression and localization of the aquaporin-1 (AQP1) water channel were examined in the glomeruli of the human kidney. Water 58-63 aquaporin 1 (Colton blood group) Homo sapiens 52-56 12002613-9 2002 This study showed the distinct localization of AQP1 in the mesangial cells of human glomeruli, suggesting its role in water movement through these cells. Water 118-123 aquaporin 1 (Colton blood group) Homo sapiens 47-51 11788448-1 2002 Renal regulation of mammalian water homeostasis is mediated by the aquaporin-1 (AQP1) water channel, which is expressed in the apical and basolateral membranes of proximal tubules and descending limbs of Henle, and aquaporin-2 (AQP2), which is redistributed from intracellular vesicles to the apical membrane (AM) of collecting duct cells with vasopressin. Water 30-35 aquaporin 1 (Colton blood group) Homo sapiens 67-78 11788448-1 2002 Renal regulation of mammalian water homeostasis is mediated by the aquaporin-1 (AQP1) water channel, which is expressed in the apical and basolateral membranes of proximal tubules and descending limbs of Henle, and aquaporin-2 (AQP2), which is redistributed from intracellular vesicles to the apical membrane (AM) of collecting duct cells with vasopressin. Water 30-35 aquaporin 1 (Colton blood group) Homo sapiens 80-84 11788448-1 2002 Renal regulation of mammalian water homeostasis is mediated by the aquaporin-1 (AQP1) water channel, which is expressed in the apical and basolateral membranes of proximal tubules and descending limbs of Henle, and aquaporin-2 (AQP2), which is redistributed from intracellular vesicles to the apical membrane (AM) of collecting duct cells with vasopressin. Water 86-91 aquaporin 1 (Colton blood group) Homo sapiens 67-78 11788448-1 2002 Renal regulation of mammalian water homeostasis is mediated by the aquaporin-1 (AQP1) water channel, which is expressed in the apical and basolateral membranes of proximal tubules and descending limbs of Henle, and aquaporin-2 (AQP2), which is redistributed from intracellular vesicles to the apical membrane (AM) of collecting duct cells with vasopressin. Water 86-91 aquaporin 1 (Colton blood group) Homo sapiens 80-84 11914159-0 2002 Tetraethylammonium block of water flux in Aquaporin-1 channels expressed in kidney thin limbs of Henle"s loop and a kidney-derived cell line. Water 28-33 aquaporin 1 (Colton blood group) Homo sapiens 42-53 11914159-1 2002 BACKGROUND: Aquaporin-1 (AQP1) channels are constitutively active water channels that allow rapid transmembrane osmotic water flux, and also serve as cyclic-GMP-gated ion channels. Water 66-71 aquaporin 1 (Colton blood group) Homo sapiens 12-23 11914159-1 2002 BACKGROUND: Aquaporin-1 (AQP1) channels are constitutively active water channels that allow rapid transmembrane osmotic water flux, and also serve as cyclic-GMP-gated ion channels. Water 66-71 aquaporin 1 (Colton blood group) Homo sapiens 25-29 11914159-1 2002 BACKGROUND: Aquaporin-1 (AQP1) channels are constitutively active water channels that allow rapid transmembrane osmotic water flux, and also serve as cyclic-GMP-gated ion channels. Water 120-125 aquaporin 1 (Colton blood group) Homo sapiens 12-23 11914159-1 2002 BACKGROUND: Aquaporin-1 (AQP1) channels are constitutively active water channels that allow rapid transmembrane osmotic water flux, and also serve as cyclic-GMP-gated ion channels. Water 120-125 aquaporin 1 (Colton blood group) Homo sapiens 25-29 12096044-1 2002 The water permeability of biological membranes has been a longstanding problem in physiology, but the proteins responsible for this remained unknown until discovery of the aquaporin 1 (AQP1) water channel protein. Water 4-9 aquaporin 1 (Colton blood group) Homo sapiens 172-183 12096044-1 2002 The water permeability of biological membranes has been a longstanding problem in physiology, but the proteins responsible for this remained unknown until discovery of the aquaporin 1 (AQP1) water channel protein. Water 4-9 aquaporin 1 (Colton blood group) Homo sapiens 185-189 12096044-1 2002 The water permeability of biological membranes has been a longstanding problem in physiology, but the proteins responsible for this remained unknown until discovery of the aquaporin 1 (AQP1) water channel protein. Water 191-196 aquaporin 1 (Colton blood group) Homo sapiens 172-183 12096044-1 2002 The water permeability of biological membranes has been a longstanding problem in physiology, but the proteins responsible for this remained unknown until discovery of the aquaporin 1 (AQP1) water channel protein. Water 191-196 aquaporin 1 (Colton blood group) Homo sapiens 185-189 12096044-2 2002 AQP1 is selectively permeated by water driven by osmotic gradients. Water 33-38 aquaporin 1 (Colton blood group) Homo sapiens 0-4 12193876-17 2002 Water flows into principal cells from collecting duct lumen through AQP2 and flows out to interstitium through AQP3 and AQP4 and finally reachs blood circulation through AQP1 capillaries. Water 0-5 aquaporin 1 (Colton blood group) Homo sapiens 170-174 11891232-1 2002 Two aquaporin (AQP)-type water channels are expressed in mammalian cornea, AQP1 in endothelial cells and AQP5 in epithelial cells. Water 25-30 aquaporin 1 (Colton blood group) Homo sapiens 75-79 11917120-8 2002 Our results demonstrate that AQP1 associated at the ZG membrane is involved in basal as well as GTP-induced rapid gating of water in ZGs of the exocrine pancreas. Water 124-129 aquaporin 1 (Colton blood group) Homo sapiens 29-33 11914159-5 2002 RESULTS: TEA blocked water permeability of AQP1 channels in kidney and kidney-derived cells, demonstrating this effect is not limited to the oocyte expression system. Water 21-26 aquaporin 1 (Colton blood group) Homo sapiens 43-47 11914159-8 2002 CONCLUSIONS: TEA selectively inhibits osmotic water permeability through native and heterologously expressed AQP1 channels. Water 46-51 aquaporin 1 (Colton blood group) Homo sapiens 109-113 11914159-9 2002 The pathways for water and ions in AQP1 differ in pharmacological sensitivity to TEA, and are consistent with the idea of independent solute pathways within the channel structure. Water 17-22 aquaporin 1 (Colton blood group) Homo sapiens 35-39 11792767-7 2002 Low solute sieving across the peritoneal membrane was first identified in 1966, a phenomenon that is now attributed to the presence of water-only transport pathways mediated by aquaporin-1. Water 135-140 aquaporin 1 (Colton blood group) Homo sapiens 177-188 11952238-2 2002 Aquaporin-1, the water channel of human erythrocytes, is the first channel demonstrated to conduct water, by expression in Xenopus oocytes. Water 17-22 aquaporin 1 (Colton blood group) Homo sapiens 0-11 11952238-2 2002 Aquaporin-1, the water channel of human erythrocytes, is the first channel demonstrated to conduct water, by expression in Xenopus oocytes. Water 99-104 aquaporin 1 (Colton blood group) Homo sapiens 0-11 11743202-0 2001 Water permeation across biological membranes: mechanism and dynamics of aquaporin-1 and GlpF. Water 0-5 aquaporin 1 (Colton blood group) Homo sapiens 72-83 12027013-1 2002 The water-selective pathway through aquaporin 1 (AQP1) membrane channel has been visualized by fitting an atomic model to a 3.7 A resolution three-dimensional density map. Water 4-9 aquaporin 1 (Colton blood group) Homo sapiens 36-47 12027013-1 2002 The water-selective pathway through aquaporin 1 (AQP1) membrane channel has been visualized by fitting an atomic model to a 3.7 A resolution three-dimensional density map. Water 4-9 aquaporin 1 (Colton blood group) Homo sapiens 49-53 11780053-0 2001 Structural basis of water-specific transport through the AQP1 water channel. Water 20-25 aquaporin 1 (Colton blood group) Homo sapiens 57-61 11780053-0 2001 Structural basis of water-specific transport through the AQP1 water channel. Water 62-67 aquaporin 1 (Colton blood group) Homo sapiens 57-61 11780053-5 2001 Here we report the structure of the aquaporin 1 (AQP1) water channel to 2.2 A resolution. Water 55-60 aquaporin 1 (Colton blood group) Homo sapiens 36-47 11780053-5 2001 Here we report the structure of the aquaporin 1 (AQP1) water channel to 2.2 A resolution. Water 55-60 aquaporin 1 (Colton blood group) Homo sapiens 49-53 11773613-1 2002 The discovery of aquaporin-1 (AQP1) answered the long-standing biophysical question of how water specifically crosses biological membranes. Water 91-96 aquaporin 1 (Colton blood group) Homo sapiens 17-28 11773613-1 2002 The discovery of aquaporin-1 (AQP1) answered the long-standing biophysical question of how water specifically crosses biological membranes. Water 91-96 aquaporin 1 (Colton blood group) Homo sapiens 30-34 11743202-1 2001 "Real time" molecular dynamics simulations of water permeation through human aquaporin-1 (AQP1) and the bacterial glycerol facilitator GlpF are presented. Water 46-51 aquaporin 1 (Colton blood group) Homo sapiens 77-88 11743202-1 2001 "Real time" molecular dynamics simulations of water permeation through human aquaporin-1 (AQP1) and the bacterial glycerol facilitator GlpF are presented. Water 46-51 aquaporin 1 (Colton blood group) Homo sapiens 90-94 11743202-5 2001 In AQP1, a fine-tuned water dipole rotation during passage is essential for water selectivity. Water 22-27 aquaporin 1 (Colton blood group) Homo sapiens 3-7 11743202-5 2001 In AQP1, a fine-tuned water dipole rotation during passage is essential for water selectivity. Water 76-81 aquaporin 1 (Colton blood group) Homo sapiens 3-7 11532455-1 2001 A refined structure of the human water channel aquaporin-1 is presented. Water 33-38 aquaporin 1 (Colton blood group) Homo sapiens 47-58 11717407-1 2001 Molecular-dynamics simulations were performed on the structures of the water channel aquaporin-1. Water 71-76 aquaporin 1 (Colton blood group) Homo sapiens 85-96 11717407-8 2001 Moreover, mutations based on the simulation also have been suggested for further experimental investigation of the water-permeation mechanism of aquaporin-1. Water 115-120 aquaporin 1 (Colton blood group) Homo sapiens 145-156 11687943-4 2001 Furthermore, during glucose-induced osmosis during PD, nearly 40% of the total osmotic water flow occurs through molecular water channels, termed "aquaporin-1." Water 87-92 aquaporin 1 (Colton blood group) Homo sapiens 147-158 11606828-2 2001 The Colton blood group antigens are expressed by the water channel aquaporin 1 (aqp1; also known as channel-forming integral protein, CHIP-28), which is a highly conserved RBC integral membrane protein. Water 53-58 aquaporin 1 (Colton blood group) Homo sapiens 80-84 11606828-2 2001 The Colton blood group antigens are expressed by the water channel aquaporin 1 (aqp1; also known as channel-forming integral protein, CHIP-28), which is a highly conserved RBC integral membrane protein. Water 53-58 aquaporin 1 (Colton blood group) Homo sapiens 134-141 11532455-5 2001 Comparison with previous aquaporin-1 models shows significant differences, not only in the loop regions, but also in the core of the water channel. Water 133-138 aquaporin 1 (Colton blood group) Homo sapiens 25-36 11532456-0 2001 Molecular dynamics study of aquaporin-1 water channel in a lipid bilayer. Water 40-45 aquaporin 1 (Colton blood group) Homo sapiens 28-39 11532456-1 2001 The aquaporin-1 water channel was modeled in a palmitoyl-oleoyl-phosphatidyl-choline lipid bilayer, by means of molecular dynamics simulations. Water 16-21 aquaporin 1 (Colton blood group) Homo sapiens 4-15 11382807-1 2001 Several aquaporin-type water channels are expressed in mammalian airways and lung: AQP1 in microvascular endothelia, AQP3 in upper airway epithelia, AQP4 in upper and lower airway epithelia, and AQP5 in alveolar epithelia. Water 23-28 aquaporin 1 (Colton blood group) Homo sapiens 83-87 11410596-2 2001 The aquaporin-1 (AQP1) water channel protein is known to facilitate the rapid movement of water across cell membranes, but a proposed secondary role as an ion channel is still unsettled. Water 23-28 aquaporin 1 (Colton blood group) Homo sapiens 4-15 11410596-2 2001 The aquaporin-1 (AQP1) water channel protein is known to facilitate the rapid movement of water across cell membranes, but a proposed secondary role as an ion channel is still unsettled. Water 23-28 aquaporin 1 (Colton blood group) Homo sapiens 17-21 11410596-2 2001 The aquaporin-1 (AQP1) water channel protein is known to facilitate the rapid movement of water across cell membranes, but a proposed secondary role as an ion channel is still unsettled. Water 90-95 aquaporin 1 (Colton blood group) Homo sapiens 4-15 11410596-2 2001 The aquaporin-1 (AQP1) water channel protein is known to facilitate the rapid movement of water across cell membranes, but a proposed secondary role as an ion channel is still unsettled. Water 90-95 aquaporin 1 (Colton blood group) Homo sapiens 17-21 11410596-3 2001 Here we describe a method to simultaneously measure water permeability and ion conductance of purified human AQP1 after reconstitution into planar lipid bilayers. Water 52-57 aquaporin 1 (Colton blood group) Homo sapiens 109-113 11410596-5 2001 Comparisons with the known single channel water permeability of AQP1 indicate that the planar lipid bilayers contain from 10(6) to 10(7) water channels. Water 42-47 aquaporin 1 (Colton blood group) Homo sapiens 64-68 11410596-5 2001 Comparisons with the known single channel water permeability of AQP1 indicate that the planar lipid bilayers contain from 10(6) to 10(7) water channels. Water 137-142 aquaporin 1 (Colton blood group) Homo sapiens 64-68 11410596-10 2001 Deletion of the putative cGMP binding motif at the C terminus by introduction of a stop codon at position 237 yielded a truncated AQP1 protein that was still permeated by water but not by ions. Water 171-176 aquaporin 1 (Colton blood group) Homo sapiens 130-134 11431445-3 2001 Aquaporin (AQP)-1 is a hexahelical integral membrane protein that functions as a regulated channel for water and cations in fluid-secreting and -absorbing tissues. Water 103-108 aquaporin 1 (Colton blood group) Homo sapiens 11-17 11251046-17 2001 Coexpression of AQP1 with the SGLT1 increased the water permeability more than 10-fold and steady state isotonic transport was achieved after less than 2 s of sugar activation. Water 50-55 aquaporin 1 (Colton blood group) Homo sapiens 16-20 11320486-1 2001 The discovery of aquaporin-1 (AQP1) by Agre and associates answered the longstanding biophysical question of how water specifically crosses biological membranes. Water 113-118 aquaporin 1 (Colton blood group) Homo sapiens 17-28 11320486-1 2001 The discovery of aquaporin-1 (AQP1) by Agre and associates answered the longstanding biophysical question of how water specifically crosses biological membranes. Water 113-118 aquaporin 1 (Colton blood group) Homo sapiens 30-34 11239067-2 2001 At least two molecules might be involved in UF failure: aquaporin-1 (AQP1), a water channel thought to be the ultra small pore of the peritoneal membrane (PM), and nitric oxide (NO), which might regulate effective peritoneal surface area and microvascular permeability. Water 78-83 aquaporin 1 (Colton blood group) Homo sapiens 56-67 11239067-5 2001 RESULTS: AQP1 is located in the endothelium lining peritoneal capillaries, and its expression is remarkably stable in samples ranging from normal to highly inflamed peritoneum and even when transcellular water permeability is absent (loss of sodium sieving). Water 204-209 aquaporin 1 (Colton blood group) Homo sapiens 9-13 11171962-1 2001 The water-selective pathway through the aquaporin-1 membrane channel has been visualized by fitting an atomic model to a 3.7-A resolution three-dimensional density map. Water 4-9 aquaporin 1 (Colton blood group) Homo sapiens 40-51