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Volumn 18, Issue 1, 2016, Pages 79-89

Quantitative Impact of Plasma Clearance and Down-regulation on GLP-1 Receptor Molecular Imaging

Author keywords

Exendin; Glucagon like peptide 1 receptor; Type 1 diabetes imaging

Indexed keywords

ALBUMIN; DIMER; EXENDIN 4; FLUORESCENT DYE; GLUCAGON LIKE PEPTIDE 1 RECEPTOR; MONOMER; BENZENESULFONIC ACID DERIVATIVE; GREEN FLUORESCENT PROTEIN; INDOLE DERIVATIVE; IRDYE 800CW; PEPTIDE; VENOM;

EID: 84955672165     PISSN: 15361632     EISSN: 18602002     Source Type: Journal    
DOI: 10.1007/s11307-015-0880-2     Document Type: Article
Times cited : (16)

References (82)
  • 1
    • 77954883105 scopus 로고    scopus 로고
    • Near-infrared fluorescent probe for imaging of pancreatic beta cells
    • COI: 1:CAS:528:DC%2BC3cXotVeku74%3D, PID: 20583828
    • Reiner T, Kohler RH, Liew CW et al (2010) Near-infrared fluorescent probe for imaging of pancreatic beta cells. Bioconjug Chem 21:1362–1368
    • (2010) Bioconjug Chem , vol.21 , pp. 1362-1368
    • Reiner, T.1    Kohler, R.H.2    Liew, C.W.3
  • 2
    • 85017695158 scopus 로고    scopus 로고
    • Evaluation of Cu-64 and Ga-68 radiolabeled glucagon-like peptide-1 receptor agonists as PET tracers for pancreatic beta cell imaging
    • Bandara N, Zheleznyak A, Cherukuri K, et al. (2015) Evaluation of Cu-64 and Ga-68 radiolabeled glucagon-like peptide-1 receptor agonists as PET tracers for pancreatic beta cell imaging. Mol Imaging Biol
    • (2015) Mol Imaging Biol
    • Bandara, N.1    Zheleznyak, A.2    Cherukuri, K.3
  • 3
    • 77956212073 scopus 로고    scopus 로고
    • What are the potential benefits of clinical beta-cell imaging in diabetes mellitus?
    • PID: 20146664
    • Goke B (2010) What are the potential benefits of clinical beta-cell imaging in diabetes mellitus? Curr Pharm Des 16:1547–1549
    • (2010) Curr Pharm Des , vol.16 , pp. 1547-1549
    • Goke, B.1
  • 4
    • 55649108628 scopus 로고    scopus 로고
    • Imaging the pancreas: from ex vivo to non-invasive technology
    • COI: 1:STN:280:DC%2BD1cjhvFKgug%3D%3D, PID: 18777169
    • Holmberg D, Ahlgren U (2008) Imaging the pancreas: from ex vivo to non-invasive technology. Diabetologia 51:2148–2154
    • (2008) Diabetologia , vol.51 , pp. 2148-2154
    • Holmberg, D.1    Ahlgren, U.2
  • 5
  • 6
    • 77954988574 scopus 로고    scopus 로고
    • Imaging of beta-cell mass and function
    • COI: 1:CAS:528:DC%2BC3cXhtVWmu73J, PID: 20554742
    • Ichise M, Harris PE (2010) Imaging of beta-cell mass and function. J Nucl Med 51:1001–1004
    • (2010) J Nucl Med , vol.51 , pp. 1001-1004
    • Ichise, M.1    Harris, P.E.2
  • 7
    • 84859640488 scopus 로고    scopus 로고
    • F-18-Labelled exendin to image GLP-1 receptor-expressing tissues: from niche to blockbuster?
    • PID: 22170323
    • Boerman OC, Gotthardt M (2012) F-18-Labelled exendin to image GLP-1 receptor-expressing tissues: from niche to blockbuster? Eur J Nucl Med Mol Imaging 39:461–462
    • (2012) Eur J Nucl Med Mol Imaging , vol.39 , pp. 461-462
    • Boerman, O.C.1    Gotthardt, M.2
  • 8
    • 0022475906 scopus 로고
    • The histopathology of the pancreas in type 1 (insulin-dependent) diabetes mellitus: a 25-year review of deaths in patients under 20 years of age in the United Kingdom
    • COI: 1:STN:280:DyaL283kvVCgtw%3D%3D, PID: 3522324
    • Foulis AK, Liddle CN, Farquharson MA, Richmond JA, Weir RS (1986) The histopathology of the pancreas in type 1 (insulin-dependent) diabetes mellitus: a 25-year review of deaths in patients under 20 years of age in the United Kingdom. Diabetologia 29:267–274
    • (1986) Diabetologia , vol.29 , pp. 267-274
    • Foulis, A.K.1    Liddle, C.N.2    Farquharson, M.A.3    Richmond, J.A.4    Weir, R.S.5
  • 9
    • 84940105815 scopus 로고    scopus 로고
    • Distinct roles of beta cell mass and function during type 1 diabetes onset and remission
    • COI: 1:CAS:528:DC%2BC2MXhtVSiu7fO, PID: 25605805
    • Chmelova H, Cohrs CM, Chouinard JA et al (2015) Distinct roles of beta cell mass and function during type 1 diabetes onset and remission. Diabetes 64:2148–2160
    • (2015) Diabetes , vol.64 , pp. 2148-2160
    • Chmelova, H.1    Cohrs, C.M.2    Chouinard, J.A.3
  • 10
    • 52949128064 scopus 로고    scopus 로고
    • Imaging the beta-cell mass: why and how
    • PID: 18548165
    • Saudek F, Brogren CH, Manohar S (2008) Imaging the beta-cell mass: why and how. Rev Diabet Stud 5:6–12
    • (2008) Rev Diabet Stud , vol.5 , pp. 6-12
    • Saudek, F.1    Brogren, C.H.2    Manohar, S.3
  • 11
    • 77953388365 scopus 로고    scopus 로고
    • Pancreatic islet plasticity interspecies comparison of islet architecture and composition
    • PID: 20657742
    • Steiner DJ, Kim A, Miller K, Hara M (2010) Pancreatic islet plasticity interspecies comparison of islet architecture and composition. Islets 2:135–145
    • (2010) Islets , vol.2 , pp. 135-145
    • Steiner, D.J.1    Kim, A.2    Miller, K.3    Hara, M.4
  • 12
    • 84872035827 scopus 로고    scopus 로고
    • Beta-cell mass and turnover in humans effects of obesity and aging
    • PID: 22875233
    • Saisho Y, Butler AE, Manesso E et al (2013) Beta-cell mass and turnover in humans effects of obesity and aging. Diabetes Care 36:111–117
    • (2013) Diabetes Care , vol.36 , pp. 111-117
    • Saisho, Y.1    Butler, A.E.2    Manesso, E.3
  • 13
    • 34250618363 scopus 로고    scopus 로고
    • In vivo multimodal imaging of transplanted pancreatic islets
    • COI: 1:CAS:528:DC%2BD28XhtFOitbnJ, PID: 17406265
    • Medarova Z, Evgenov NV, Dai G et al (2006) In vivo multimodal imaging of transplanted pancreatic islets. Nat Protoc 1:429–435
    • (2006) Nat Protoc , vol.1 , pp. 429-435
    • Medarova, Z.1    Evgenov, N.V.2    Dai, G.3
  • 14
    • 0025778295 scopus 로고
    • Correlations of in vivo beta-cell function tests with beta-cell mass and pancreatic insulin content in streptozocin-administered baboons
    • COI: 1:CAS:528:DyaK3MXkt1OjtLc%3D, PID: 2040383
    • McCulloch DK, Koerker DJ, Kahn SE et al (1991) Correlations of in vivo beta-cell function tests with beta-cell mass and pancreatic insulin content in streptozocin-administered baboons. Diabetes 40:673–679
    • (1991) Diabetes , vol.40 , pp. 673-679
    • McCulloch, D.K.1    Koerker, D.J.2    Kahn, S.E.3
  • 15
    • 77956221358 scopus 로고    scopus 로고
    • Development of radiotracers for the determination of the beta-cell mass in vivo
    • COI: 1:CAS:528:DC%2BC3cXmvFCnt7g%3D, PID: 20146667
    • Brom M, Andraojc K, Oyen WJG et al (2010) Development of radiotracers for the determination of the beta-cell mass in vivo. Curr Pharm Des 16:1561–1567
    • (2010) Curr Pharm Des , vol.16 , pp. 1561-1567
    • Brom, M.1    Andraojc, K.2    Oyen, W.J.G.3
  • 16
    • 62449183526 scopus 로고    scopus 로고
    • 11C-dihydrotetrabenazine PET of the pancreas in subjects with long-standing type 1 diabetes and in healthy controls
    • COI: 1:CAS:528:DC%2BD1MXktVynsr4%3D, PID: 19223416
    • 11C-dihydrotetrabenazine PET of the pancreas in subjects with long-standing type 1 diabetes and in healthy controls. J Nucl Med 50:382–389
    • (2009) J Nucl Med , vol.50 , pp. 382-389
    • Goland, R.1    Freeby, M.2    Parsey, R.3
  • 17
    • 0019400455 scopus 로고
    • The pancreatic islets in diabetes
    • COI: 1:STN:280:DyaL3M7gs1KlsQ%3D%3D, PID: 7006384
    • Gepts W, Lecompte PM (1981) The pancreatic islets in diabetes. Am J Med 70:105–115
    • (1981) Am J Med , vol.70 , pp. 105-115
    • Gepts, W.1    Lecompte, P.M.2
  • 18
    • 0942289897 scopus 로고    scopus 로고
    • Systematic screening of potential beta-cell imaging agents
    • COI: 1:CAS:528:DC%2BD2cXntVGgtg%3D%3D, PID: 14751228
    • Sweet IR, Cook DL, Lernmark A et al (2004) Systematic screening of potential beta-cell imaging agents. Biochem Biophys Res Commun 314:976–983
    • (2004) Biochem Biophys Res Commun , vol.314 , pp. 976-983
    • Sweet, I.R.1    Cook, D.L.2    Lernmark, A.3
  • 19
    • 0035487329 scopus 로고    scopus 로고
    • Noninvasive in vivo measurement of beta-cell mass in mouse model of diabetes
    • COI: 1:CAS:528:DC%2BD3MXntlGhur0%3D, PID: 11574403
    • Moore A, Bonner-Weir S, Weissleder R (2001) Noninvasive in vivo measurement of beta-cell mass in mouse model of diabetes. Diabetes 50:2231–2236
    • (2001) Diabetes , vol.50 , pp. 2231-2236
    • Moore, A.1    Bonner-Weir, S.2    Weissleder, R.3
  • 20
    • 23044456342 scopus 로고    scopus 로고
    • In vitro and in vivo evaluation of novel glibenclamide derivatives as imaging agents for the non-invasive assessment of the pancreatic islet cell mass in animals and humans
    • COI: 1:CAS:528:DC%2BD2MXmslCmsb4%3D, PID: 16025400
    • Schneider S, Feilen PJ, Schreckenberger M et al (2005) In vitro and in vivo evaluation of novel glibenclamide derivatives as imaging agents for the non-invasive assessment of the pancreatic islet cell mass in animals and humans. Exp Clin Endocrinol Diabetes 113:388–395
    • (2005) Exp Clin Endocrinol Diabetes , vol.113 , pp. 388-395
    • Schneider, S.1    Feilen, P.J.2    Schreckenberger, M.3
  • 21
    • 38349073954 scopus 로고    scopus 로고
    • VMAT2 gene expression and function as it applies to imaging beta-cell mass
    • COI: 1:CAS:528:DC%2BD1cXlt1amtg%3D%3D, PID: 17665159
    • Harris PE, Ferrara C, Barba P et al (2008) VMAT2 gene expression and function as it applies to imaging beta-cell mass. J Mol Med 86:5–16
    • (2008) J Mol Med , vol.86 , pp. 5-16
    • Harris, P.E.1    Ferrara, C.2    Barba, P.3
  • 22
    • 33745221211 scopus 로고    scopus 로고
    • Longitudinal noninvasive PET-based beta cell mass estimates in a spontaneous diabetes rat model
    • COI: 1:CAS:528:DC%2BD28XlsFWrtLg%3D, PID: 16710474
    • Souza F, Simpson N, Raffo A et al (2006) Longitudinal noninvasive PET-based beta cell mass estimates in a spontaneous diabetes rat model. J Clin Invest 116:1506–1513
    • (2006) J Clin Invest , vol.116 , pp. 1506-1513
    • Souza, F.1    Simpson, N.2    Raffo, A.3
  • 23
    • 84855473709 scopus 로고    scopus 로고
    • Multimodal image coregistration and inducible selective cell ablation to evaluate imaging ligands
    • COI: 1:CAS:528:DC%2BC38Xkt1KqtA%3D%3D, PID: 22143775
    • Virostko J, Henske J, Vinet L et al (2011) Multimodal image coregistration and inducible selective cell ablation to evaluate imaging ligands. Proc Natl Acad Sci U S A 108:20719–20724
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 20719-20724
    • Virostko, J.1    Henske, J.2    Vinet, L.3
  • 24
    • 79961244260 scopus 로고    scopus 로고
    • Accurate measurement of pancreatic islet beta-cell mass using a second-generation fluorescent exendin-4 analog
    • COI: 1:CAS:528:DC%2BC3MXhtVenu7fI, PID: 21768367
    • Reiner T, Thurber G, Gaglia J et al (2011) Accurate measurement of pancreatic islet beta-cell mass using a second-generation fluorescent exendin-4 analog. Proc Natl Acad Sci U S A 108:12815–12820
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 12815-12820
    • Reiner, T.1    Thurber, G.2    Gaglia, J.3
  • 25
    • 84870985165 scopus 로고    scopus 로고
    • Imaging of beta-cell mass and insulitis in insulin-dependent (type 1) diabetes mellitus
    • PID: 22889646
    • Di Gialleonardo V, de Vries EF, Di Girolamo M et al (2012) Imaging of beta-cell mass and insulitis in insulin-dependent (type 1) diabetes mellitus. Endocr Rev 33:892–919
    • (2012) Endocr Rev , vol.33 , pp. 892-919
    • Di Gialleonardo, V.1    de Vries, E.F.2    Di Girolamo, M.3
  • 26
    • 34748871424 scopus 로고    scopus 로고
    • Partial volume correction of standardized uptake values and the dual time point in FDG-PET imaging: should these be routinely employed in assessing patients with cancer?
    • PID: 17522857
    • Basu S, Alavi A (2007) Partial volume correction of standardized uptake values and the dual time point in FDG-PET imaging: should these be routinely employed in assessing patients with cancer? Eur J Nucl Med Mol Imaging 34:1527–1529
    • (2007) Eur J Nucl Med Mol Imaging , vol.34 , pp. 1527-1529
    • Basu, S.1    Alavi, A.2
  • 27
    • 34047192093 scopus 로고    scopus 로고
    • Novel quantitative techniques for assessing regional and global function and structure based on modern imaging modalities: implications for normal variation, aging and diseased states
    • PID: 17418154
    • Basu S, Zaidi H, Houseni M et al (2007) Novel quantitative techniques for assessing regional and global function and structure based on modern imaging modalities: implications for normal variation, aging and diseased states. Semin Nucl Med 37:223–239
    • (2007) Semin Nucl Med , vol.37 , pp. 223-239
    • Basu, S.1    Zaidi, H.2    Houseni, M.3
  • 28
    • 0023223873 scopus 로고
    • Positron emission tomography in aging and dementia: effect of cerebral atrophy
    • COI: 1:STN:280:DyaL2s7pslKisA%3D%3D, PID: 3494824
    • Chawluk JB, Alavi A, Dann R et al (1987) Positron emission tomography in aging and dementia: effect of cerebral atrophy. J Nucl Med 28:431–437
    • (1987) J Nucl Med , vol.28 , pp. 431-437
    • Chawluk, J.B.1    Alavi, A.2    Dann, R.3
  • 29
    • 0036454017 scopus 로고    scopus 로고
    • Use of a corrected standardized uptake value based on the lesion size on CT permits accurate characterization of lung nodules on FDG-PET
    • PID: 12458399
    • Hickeson M, Yun MJ, Matthies A et al (2002) Use of a corrected standardized uptake value based on the lesion size on CT permits accurate characterization of lung nodules on FDG-PET. Eur J Nucl Med Mol Imaging 29:1639–1647
    • (2002) Eur J Nucl Med Mol Imaging , vol.29 , pp. 1639-1647
    • Hickeson, M.1    Yun, M.J.2    Matthies, A.3
  • 30
    • 67651177441 scopus 로고    scopus 로고
    • A recovery coefficient method for partial volume correction of PET images
    • PID: 19367446
    • Srinivas SM, Dhurairaj T, Basu S et al (2009) A recovery coefficient method for partial volume correction of PET images. Ann Nucl Med 23:341–348
    • (2009) Ann Nucl Med , vol.23 , pp. 341-348
    • Srinivas, S.M.1    Dhurairaj, T.2    Basu, S.3
  • 31
    • 0025957221 scopus 로고
    • Analysis of brain and cerebrospinal-fluid volumes with MR imaging: impact on PET data correction for atrophy. Part II. Aging and Alzheimer dementia
    • COI: 1:STN:280:DyaK3M%2FnsV2ltg%3D%3D, PID: 1984290
    • Tanna NK, Kohn MI, Horwich DN et al (1991) Analysis of brain and cerebrospinal-fluid volumes with MR imaging: impact on PET data correction for atrophy. Part II. Aging and Alzheimer dementia. Radiology 178:123–130
    • (1991) Radiology , vol.178 , pp. 123-130
    • Tanna, N.K.1    Kohn, M.I.2    Horwich, D.N.3
  • 32
    • 6044234743 scopus 로고    scopus 로고
    • Non-invasive imaging of beta cell mass: a quantitative analysis
    • PID: 15628819
    • Sweet IR, Cook DL, Lernmark A et al (2004) Non-invasive imaging of beta cell mass: a quantitative analysis. Diabetes Technol Ther 6:652–659
    • (2004) Diabetes Technol Ther , vol.6 , pp. 652-659
    • Sweet, I.R.1    Cook, D.L.2    Lernmark, A.3
  • 33
    • 84876721784 scopus 로고    scopus 로고
    • Efficient 18F-labeling of synthetic exendin-4 analogues for imaging beta cells
    • COI: 1:CAS:528:DC%2BC38Xht1KitL%2FE, PID: 23997998
    • Keliher EJ, Reiner T, Thurber GM et al (2012) Efficient 18F-labeling of synthetic exendin-4 analogues for imaging beta cells. ChemistryOpen 1:177–183
    • (2012) ChemistryOpen , vol.1 , pp. 177-183
    • Keliher, E.J.1    Reiner, T.2    Thurber, G.M.3
  • 34
    • 84904427412 scopus 로고    scopus 로고
    • In vivo imaging of GLP-1R with a targeted bimodal PET/fluorescence imaging agent
    • COI: 1:CAS:528:DC%2BC2cXosFait7Y%3D, PID: 24856928
    • Brand C, Abdel-Atti D, Zhang Y et al (2014) In vivo imaging of GLP-1R with a targeted bimodal PET/fluorescence imaging agent. Bioconjug Chem 25:1323–1330
    • (2014) Bioconjug Chem , vol.25 , pp. 1323-1330
    • Brand, C.1    Abdel-Atti, D.2    Zhang, Y.3
  • 35
    • 0026648961 scopus 로고
    • Isolation and characterization of exendin-4, an exendin-3 analog, from Heloderma suspectum venom. Further evidence for an exendin receptor on dispersed acini from guinea pig pancreas
    • COI: 1:CAS:528:DyaK38XktVantbw%3D, PID: 1313797
    • Eng J, Kleinman WA, Singh L et al (1992) Isolation and characterization of exendin-4, an exendin-3 analog, from Heloderma suspectum venom. Further evidence for an exendin receptor on dispersed acini from guinea pig pancreas. J Biol Chem 267:7402–7405
    • (1992) J Biol Chem , vol.267 , pp. 7402-7405
    • Eng, J.1    Kleinman, W.A.2    Singh, L.3
  • 36
    • 33751515577 scopus 로고    scopus 로고
    • A new technique for in vivo imaging of specific GLP-1 binding sites: first results in small rodents
    • COI: 1:CAS:528:DC%2BD28Xht12rsLjO, PID: 16930741
    • Gotthardt M, Lalyko G, van Eerd-Vismale J et al (2006) A new technique for in vivo imaging of specific GLP-1 binding sites: first results in small rodents. Regul Pept 137:162–167
    • (2006) Regul Pept , vol.137 , pp. 162-167
    • Gotthardt, M.1    Lalyko, G.2    van Eerd-Vismale, J.3
  • 37
    • 0027184119 scopus 로고
    • Exendin-4 is a high potency agonist and truncated exendin-(9–39)-amide an antagonist at the glucagon-like peptide 1-(7–36)-amide receptor of insulin-secreting beta-cells
    • COI: 1:STN:280:DyaK3sznsV2lsw%3D%3D, PID: 8396143
    • Goke R, Fehmann HC, Linn T et al (1993) Exendin-4 is a high potency agonist and truncated exendin-(9–39)-amide an antagonist at the glucagon-like peptide 1-(7–36)-amide receptor of insulin-secreting beta-cells. J Biol Chem 268:19650–19655
    • (1993) J Biol Chem , vol.268 , pp. 19650-19655
    • Goke, R.1    Fehmann, H.C.2    Linn, T.3
  • 38
    • 0028883257 scopus 로고
    • Reduction of the incretin effect in rats by the glucagon-like peptide-1 receptor antagonist exendin(9–39) amide
    • COI: 1:CAS:528:DyaK2MXivVyitLg%3D, PID: 7813808
    • Kolligs F, Fehmann HC, Goke R, Goke B (1995) Reduction of the incretin effect in rats by the glucagon-like peptide-1 receptor antagonist exendin(9–39) amide. Diabetes 44:16–19
    • (1995) Diabetes , vol.44 , pp. 16-19
    • Kolligs, F.1    Fehmann, H.C.2    Goke, R.3    Goke, B.4
  • 39
    • 0036232690 scopus 로고    scopus 로고
    • Use of the incretin hormone glucagon-like peptide-1 (GLP-1) for the detection of insulinomas: initial experimental results
    • COI: 1:CAS:528:DC%2BD38XkvFSns74%3D, PID: 11976797
    • Gotthardt M, Fischer M, Naeher I et al (2002) Use of the incretin hormone glucagon-like peptide-1 (GLP-1) for the detection of insulinomas: initial experimental results. Eur J Nucl Med Mol Imaging 29:597–606
    • (2002) Eur J Nucl Med Mol Imaging , vol.29 , pp. 597-606
    • Gotthardt, M.1    Fischer, M.2    Naeher, I.3
  • 40
    • 34250722229 scopus 로고    scopus 로고
    • [Lys(40)(Ahx-DTPA-In-111)NH2]-Exendin-4 is a highly efficient radiotherapeutic for glucagon-like peptide-1 receptor-targeted therapy for insulinoma
    • COI: 1:CAS:528:DC%2BD2sXmsFCqu70%3D, PID: 17575235
    • Wicki A, Wild D, Storch D et al (2007) [Lys(40)(Ahx-DTPA-In-111)NH2]-Exendin-4 is a highly efficient radiotherapeutic for glucagon-like peptide-1 receptor-targeted therapy for insulinoma. Clin Cancer Res 13:3696–3705
    • (2007) Clin Cancer Res , vol.13 , pp. 3696-3705
    • Wicki, A.1    Wild, D.2    Storch, D.3
  • 41
    • 84896395302 scopus 로고    scopus 로고
    • 64Cu- and 68Ga-labelled [Nle(14), Lys(40)(Ahx-NODAGA)NH2]-exendin-4 for pancreatic beta cell imaging in rats
    • PID: 24101374
    • Mikkola K, Yim CB, Fagerholm V et al (2014) 64Cu- and 68Ga-labelled [Nle(14), Lys(40)(Ahx-NODAGA)NH2]-exendin-4 for pancreatic beta cell imaging in rats. Mol Imaging Biol 16:255–263
    • (2014) Mol Imaging Biol , vol.16 , pp. 255-263
    • Mikkola, K.1    Yim, C.B.2    Fagerholm, V.3
  • 42
    • 77954986457 scopus 로고    scopus 로고
    • Exendin-4-based radiopharmaceuticals for glucagonlike peptide-1 receptor PET/CT and SPECT/CT
    • COI: 1:CAS:528:DC%2BC3cXhtVWmu73F, PID: 20595511
    • Wild D, Wicki A, Mansi R et al (2010) Exendin-4-based radiopharmaceuticals for glucagonlike peptide-1 receptor PET/CT and SPECT/CT. J Nucl Med 51:1059–1067
    • (2010) J Nucl Med , vol.51 , pp. 1059-1067
    • Wild, D.1    Wicki, A.2    Mansi, R.3
  • 43
    • 84923230371 scopus 로고    scopus 로고
    • Dual-purpose linker for alpha helix stabilization and imaging agent conjugation to glucagon-like peptide-1 receptor ligands
    • COI: 1:CAS:528:DC%2BC2MXovFGnsw%3D%3D, PID: 25594741
    • Zhang L, Navaratna T, Liao JS, Thurber GM (2015) Dual-purpose linker for alpha helix stabilization and imaging agent conjugation to glucagon-like peptide-1 receptor ligands. Bioconjug Chem 26:329–337
    • (2015) Bioconjug Chem , vol.26 , pp. 329-337
    • Zhang, L.1    Navaratna, T.2    Liao, J.S.3    Thurber, G.M.4
  • 44
    • 80053493999 scopus 로고    scopus 로고
    • PET of insulinoma using F-18-FBEM-EM3106B, a new GLP-1 analogue
    • COI: 1:CAS:528:DC%2BC3MXhtVemu73F, PID: 21800885
    • Gao HK, Niu G, Yang M et al (2011) PET of insulinoma using F-18-FBEM-EM3106B, a new GLP-1 analogue. Mol Pharm 8:1775–1782
    • (2011) Mol Pharm , vol.8 , pp. 1775-1782
    • Gao, H.K.1    Niu, G.2    Yang, M.3
  • 46
    • 79955014687 scopus 로고    scopus 로고
    • Mono-PEGylated dimeric exendin-4 as high receptor binding and long-acting conjugates for type 2 anti-diabetes therapeutics
    • COI: 1:CAS:528:DC%2BC3MXjtV2mu74%3D, PID: 21401109
    • Kim TH, Jiang HH, Lee S et al (2011) Mono-PEGylated dimeric exendin-4 as high receptor binding and long-acting conjugates for type 2 anti-diabetes therapeutics. Bioconjug Chem 22:625–632
    • (2011) Bioconjug Chem , vol.22 , pp. 625-632
    • Kim, T.H.1    Jiang, H.H.2    Lee, S.3
  • 47
    • 84869748023 scopus 로고    scopus 로고
    • Site-specific PEGylated exendin-4 modified with a high molecular weight trimeric PEG reduces steric hindrance and increases type 2 antidiabetic therapeutic effects
    • COI: 1:CAS:528:DC%2BC38Xhs1Wjt7bM, PID: 23116483
    • Kim TH, Jiang HH, Lim SM et al (2012) Site-specific PEGylated exendin-4 modified with a high molecular weight trimeric PEG reduces steric hindrance and increases type 2 antidiabetic therapeutic effects. Bioconjug Chem 23:2214–2220
    • (2012) Bioconjug Chem , vol.23 , pp. 2214-2220
    • Kim, T.H.1    Jiang, H.H.2    Lim, S.M.3
  • 48
    • 0029117847 scopus 로고
    • Agonist-induced internalization and recycling of the glucagon-like peptide-1 receptor in transfected fibroblasts and in insulinomas
    • COI: 1:CAS:528:DyaK2MXnsVyju7s%3D, PID: 7646446
    • Widmann C, Dolci W, Thorens B (1995) Agonist-induced internalization and recycling of the glucagon-like peptide-1 receptor in transfected fibroblasts and in insulinomas. Biochem J 310(Pt 1):203–214
    • (1995) Biochem J , vol.310 , pp. 203-214
    • Widmann, C.1    Dolci, W.2    Thorens, B.3
  • 49
    • 52549121490 scopus 로고    scopus 로고
    • Kinetics of anti-carcinoembryonic antigen antibody internalization: effects of affinity, bivalency, and stability
    • COI: 1:CAS:528:DC%2BD1cXhtFCgu7jI, PID: 18408925
    • Schmidt MM, Thurber GM, Wittrup KD (2008) Kinetics of anti-carcinoembryonic antigen antibody internalization: effects of affinity, bivalency, and stability. Cancer Immunol Immunother 57:1879–1890
    • (2008) Cancer Immunol Immunother , vol.57 , pp. 1879-1890
    • Schmidt, M.M.1    Thurber, G.M.2    Wittrup, K.D.3
  • 50
    • 84871717195 scopus 로고    scopus 로고
    • A novel method to quantify IRDye800CW fluorescent antibody probes ex vivo in tissue distribution studies
    • PID: 23009555
    • Oliveira S, Cohen R, Walsum MS et al (2012) A novel method to quantify IRDye800CW fluorescent antibody probes ex vivo in tissue distribution studies. EJNMMI Res 2:50
    • (2012) EJNMMI Res , vol.2 , pp. 50
    • Oliveira, S.1    Cohen, R.2    Walsum, M.S.3
  • 51
    • 45549086826 scopus 로고    scopus 로고
    • Crystal structure of the ligand-bound glucagon-like peptide-1 receptor extracellular domain
    • COI: 1:CAS:528:DC%2BD1cXkvVSgtr4%3D, PID: 18287102
    • Runge S, Thogersen H, Madsen K et al (2008) Crystal structure of the ligand-bound glucagon-like peptide-1 receptor extracellular domain. J Biol Chem 283:11340–11347
    • (2008) J Biol Chem , vol.283 , pp. 11340-11347
    • Runge, S.1    Thogersen, H.2    Madsen, K.3
  • 52
    • 79953219749 scopus 로고    scopus 로고
    • Rational approach to select small peptide molecular probes labeled with fluorescent cyanine dyes for in vivo optical imaging
    • COI: 1:CAS:528:DC%2BC3MXivVChur4%3D, PID: 21329363
    • Berezin MY, Guo K, Akers W et al (2011) Rational approach to select small peptide molecular probes labeled with fluorescent cyanine dyes for in vivo optical imaging. Biochemistry 50:2691–2700
    • (2011) Biochemistry , vol.50 , pp. 2691-2700
    • Berezin, M.Y.1    Guo, K.2    Akers, W.3
  • 53
    • 80052841941 scopus 로고    scopus 로고
    • A systems approach for tumor pharmacokinetics
    • Thurber GM, Weissleder R (2011) A systems approach for tumor pharmacokinetics. PLoS ONE 6
    • (2011) PLoS ONE , pp. 6
    • Thurber, G.M.1    Weissleder, R.2
  • 54
    • 84930171216 scopus 로고    scopus 로고
    • Multichannel imaging to quantify four classes of pharmacokinetic distribution in tumors
    • COI: 1:CAS:528:DC%2BC2cXhtFygtrbI, PID: 25048378
    • Bhatnagar S, Deschenes E, Liao JS et al (2014) Multichannel imaging to quantify four classes of pharmacokinetic distribution in tumors. J Pharm Sci 103:3276–3286
    • (2014) J Pharm Sci , vol.103 , pp. 3276-3286
    • Bhatnagar, S.1    Deschenes, E.2    Liao, J.S.3
  • 55
    • 84895190840 scopus 로고    scopus 로고
    • The protective roles of GLP-1R signaling in diabetic nephropathy: possible mechanism and therapeutic potential
    • COI: 1:CAS:528:DC%2BC3sXhs1ykt73E, PID: 24152968
    • Fujita H, Morii T, Fujishima H et al (2014) The protective roles of GLP-1R signaling in diabetic nephropathy: possible mechanism and therapeutic potential. Kidney Int 85:579–589
    • (2014) Kidney Int , vol.85 , pp. 579-589
    • Fujita, H.1    Morii, T.2    Fujishima, H.3
  • 56
    • 84862944057 scopus 로고    scopus 로고
    • Dipeptidyl peptidase IV inhibitor attenuates kidney injury in streptozotocin-induced diabetic rats
    • COI: 1:CAS:528:DC%2BC38XjtVSltL0%3D, PID: 22025647
    • Liu WJ, Xie SH, Liu YN et al (2012) Dipeptidyl peptidase IV inhibitor attenuates kidney injury in streptozotocin-induced diabetic rats. J Pharmacol Exp Ther 340:248–255
    • (2012) J Pharmacol Exp Ther , vol.340 , pp. 248-255
    • Liu, W.J.1    Xie, S.H.2    Liu, Y.N.3
  • 57
    • 84897852105 scopus 로고    scopus 로고
    • GLP-1 receptor localization in monkey and human tissue: novel distribution revealed with extensively validated monoclonal antibody
    • PID: 24467746
    • Pyke C, Heller RS, Kirk RK et al (2014) GLP-1 receptor localization in monkey and human tissue: novel distribution revealed with extensively validated monoclonal antibody. Endocrinology 155:1280–1290
    • (2014) Endocrinology , vol.155 , pp. 1280-1290
    • Pyke, C.1    Heller, R.S.2    Kirk, R.K.3
  • 58
    • 84938414413 scopus 로고    scopus 로고
    • Glucagon-like-peptide-1 receptor expression in normal and diseased human thyroid and pancreas
    • PID: 25216224
    • Waser B, Blank A, Karamitopoulou E et al (2015) Glucagon-like-peptide-1 receptor expression in normal and diseased human thyroid and pancreas. Mod Pathol 28:391–402
    • (2015) Mod Pathol , vol.28 , pp. 391-402
    • Waser, B.1    Blank, A.2    Karamitopoulou, E.3
  • 59
    • 77958603882 scopus 로고    scopus 로고
    • Novel GLP-1 fusion chimera as potent long acting GLP-1 receptor agonist
    • Wang QH, Chen K, Liu R et al (2010) Novel GLP-1 fusion chimera as potent long acting GLP-1 receptor agonist. PLoS One 5:9
    • (2010) PLoS One , vol.5 , pp. 9
    • Wang, Q.H.1    Chen, K.2    Liu, R.3
  • 60
    • 84895198774 scopus 로고    scopus 로고
    • Novel exenatide analogs with peptidic albumin binding domains: potent anti-diabetic agents with extended duration of action
    • PID: 24503632
    • Levy OE, Jodka CM, Ren SS et al (2014) Novel exenatide analogs with peptidic albumin binding domains: potent anti-diabetic agents with extended duration of action. PLoS One 9:e87704
    • (2014) PLoS One , vol.9 , pp. 87704
    • Levy, O.E.1    Jodka, C.M.2    Ren, S.S.3
  • 61
    • 77952756104 scopus 로고    scopus 로고
    • Engineering and characterization of the long-acting glucagon-like peptide-1 analogue LY2189265, an Fc fusion protein
    • COI: 1:CAS:528:DC%2BC3cXoslyltbc%3D, PID: 20503261
    • Glaesner W, Vick AM, Millican R et al (2010) Engineering and characterization of the long-acting glucagon-like peptide-1 analogue LY2189265, an Fc fusion protein. Diabetes Metab Res Rev 26:287–296
    • (2010) Diabetes Metab Res Rev , vol.26 , pp. 287-296
    • Glaesner, W.1    Vick, A.M.2    Millican, R.3
  • 62
    • 38749139878 scopus 로고    scopus 로고
    • Factors determining antibody distribution in tumors
    • COI: 1:CAS:528:DC%2BD1cXhslOjsLw%3D, PID: 18179828
    • Thurber GM, Schmidt MM, Wittrup KD (2008) Factors determining antibody distribution in tumors. Trends Pharmacol Sci 29:57–61
    • (2008) Trends Pharmacol Sci , vol.29 , pp. 57-61
    • Thurber, G.M.1    Schmidt, M.M.2    Wittrup, K.D.3
  • 63
    • 84855322440 scopus 로고    scopus 로고
    • Techniques for molecular imaging probe design
    • COI: 1:CAS:528:DC%2BC38XitlGgu7c%3D, PID: 22201532
    • Reynolds F, Kelly KA (2011) Techniques for molecular imaging probe design. Mol Imaging 10:407–419
    • (2011) Mol Imaging , vol.10 , pp. 407-419
    • Reynolds, F.1    Kelly, K.A.2
  • 64
    • 0028117154 scopus 로고
    • Processing of antibody-radioisotope conjugates after binding to the surface of tumor cells
    • COI: 1:CAS:528:DyaK2cXltVeiurc%3D, PID: 8306261
    • Mattes MJ, Griffiths G, Diril H et al (1994) Processing of antibody-radioisotope conjugates after binding to the surface of tumor cells. Cancer 73:787–793
    • (1994) Cancer , vol.73 , pp. 787-793
    • Mattes, M.J.1    Griffiths, G.2    Diril, H.3
  • 65
    • 34250732525 scopus 로고    scopus 로고
    • [Lys(40) (Ahx-DTPA-In-111)NH2]exendin-4, a very promising ligand for glucagon-like peptide-1 (GLP-1) receptor targeting
    • COI: 1:CAS:528:DC%2BD2sXksFKntw%3D%3D, PID: 17138746
    • Wild D, Behe M, Wicki A et al (2006) [Lys(40) (Ahx-DTPA-In-111)NH2]exendin-4, a very promising ligand for glucagon-like peptide-1 (GLP-1) receptor targeting. J Nucl Med 47:2025–2033
    • (2006) J Nucl Med , vol.47 , pp. 2025-2033
    • Wild, D.1    Behe, M.2    Wicki, A.3
  • 66
    • 84890087174 scopus 로고    scopus 로고
    • Real-time trafficking and signaling of the glucagon-like peptide-1 receptor
    • COI: 1:CAS:528:DC%2BC2cXlt1ajtQ%3D%3D, PID: 24275181
    • Roed SN, Wismann P, Underwood CR et al (2014) Real-time trafficking and signaling of the glucagon-like peptide-1 receptor. Mol Cell Endocrinol 382:938–949
    • (2014) Mol Cell Endocrinol , vol.382 , pp. 938-949
    • Roed, S.N.1    Wismann, P.2    Underwood, C.R.3
  • 67
    • 71149111180 scopus 로고    scopus 로고
    • Functional characterization of N-terminally GFP-tagged GLP-1 receptor
    • Bavec A, Licar A (2009) Functional characterization of N-terminally GFP-tagged GLP-1 receptor. J Biomed Biotechnol
    • (2009) J Biomed Biotechnol
    • Bavec, A.1    Licar, A.2
  • 68
    • 70350234894 scopus 로고    scopus 로고
    • A modeling analysis of the effects of molecular size and binding affinity on tumor targeting
    • COI: 1:CAS:528:DC%2BD1MXht1Cqur7K, PID: 19825804
    • Schmidt MM, Wittrup KD (2009) A modeling analysis of the effects of molecular size and binding affinity on tumor targeting. Mol Cancer Ther 8:2861
    • (2009) Mol Cancer Ther , vol.8 , pp. 2861
    • Schmidt, M.M.1    Wittrup, K.D.2
  • 69
    • 79953708503 scopus 로고    scopus 로고
    • Renal uptake of different radiolabelled peptides is mediated by megalin: SPECT and biodistribution studies in megalin-deficient mice
    • COI: 1:CAS:528:DC%2BC3MXivFyksL0%3D, PID: 21170526
    • Vegt E, Melis M, Eek A et al (2011) Renal uptake of different radiolabelled peptides is mediated by megalin: SPECT and biodistribution studies in megalin-deficient mice. Eur J Nucl Med Mol Imaging 38:623–632
    • (2011) Eur J Nucl Med Mol Imaging , vol.38 , pp. 623-632
    • Vegt, E.1    Melis, M.2    Eek, A.3
  • 70
    • 34447336118 scopus 로고    scopus 로고
    • 64Cu-labeled tetrameric and octameric RGD peptides for small-animal PET of tumor alpha(v)beta(3) integrin expression
    • COI: 1:CAS:528:DC%2BD2sXhtVertL7F, PID: 17574975
    • Li ZB, Cai WB, Cao QZ et al (2007) 64Cu-labeled tetrameric and octameric RGD peptides for small-animal PET of tumor alpha(v)beta(3) integrin expression. J Nucl Med 48:1162–1171
    • (2007) J Nucl Med , vol.48 , pp. 1162-1171
    • Li, Z.B.1    Cai, W.B.2    Cao, Q.Z.3
  • 71
    • 27944452698 scopus 로고    scopus 로고
    • Near-infrared fluorescent RGD peptides for optical imaging of integrin alpha(v)beta 3 expression in living mice
    • COI: 1:CAS:528:DC%2BD2MXhtFGmtLjL, PID: 16287239
    • Cheng Z, Wu Y, Xiong ZM et al (2005) Near-infrared fluorescent RGD peptides for optical imaging of integrin alpha(v)beta 3 expression in living mice. Bioconjug Chem 16:1433–1441
    • (2005) Bioconjug Chem , vol.16 , pp. 1433-1441
    • Cheng, Z.1    Wu, Y.2    Xiong, Z.M.3
  • 72
    • 84899980586 scopus 로고    scopus 로고
    • Alternative non-antibody protein scaffolds for molecular imaging of cancer
    • Stern LA, Case BA, Hackel BJ (2013) Alternative non-antibody protein scaffolds for molecular imaging of cancer. Curr Opin Chem Eng 2
    • (2013) Curr Opin Chem Eng , pp. 2
    • Stern, L.A.1    Case, B.A.2    Hackel, B.J.3
  • 73
    • 84883442008 scopus 로고    scopus 로고
    • Engineered knottin peptide enables noninvasive optical imaging of intracranial medulloblastoma
    • COI: 1:CAS:528:DC%2BC3sXhsVKks7bF, PID: 23950221
    • Moore SJ, Gephart MGH, Bergen JM et al (2013) Engineered knottin peptide enables noninvasive optical imaging of intracranial medulloblastoma. Proc Natl Acad Sci U S A 110:14598–14603
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 14598-14603
    • Moore, S.J.1    Gephart, M.G.H.2    Bergen, J.M.3
  • 74
    • 84946569926 scopus 로고    scopus 로고
    • Residualization rates of near-infrared dyes for the rational design of molecular imaging agents, Mol Imaging Biol
    • Cilliers C, Liao J, Atangcho L, Thurber GM (2015) Residualization rates of near-infrared dyes for the rational design of molecular imaging agents. Mol Imaging Biol
    • (2015) Thurber GM
    • Cilliers, C.1    Liao, J.2    Atangcho, L.3
  • 75
    • 84901356899 scopus 로고    scopus 로고
    • Optimizing the bioavailability of small molecular optical imaging probes by conjugation to an albumin affinity tag
    • COI: 1:CAS:528:DC%2BC2cXpvFKis74%3D, PID: 24815420
    • Hahnenkamp A, Alsibai W, Bremer C, Holtke C (2014) Optimizing the bioavailability of small molecular optical imaging probes by conjugation to an albumin affinity tag. J Control Release 186:32–40
    • (2014) J Control Release , vol.186 , pp. 32-40
    • Hahnenkamp, A.1    Alsibai, W.2    Bremer, C.3    Holtke, C.4
  • 76
    • 84964285745 scopus 로고    scopus 로고
    • Bicyclic peptides conjugated to an albumin-binding tag diffuse efficiently into solid tumors
    • COI: 1:CAS:528:DC%2BC2MXnslWnsg%3D%3D, PID: 25381263
    • Pollaro L, Raghunathan S, Morales-Sanfrutos J et al (2015) Bicyclic peptides conjugated to an albumin-binding tag diffuse efficiently into solid tumors. Mol Cancer Ther 14:151–161
    • (2015) Mol Cancer Ther , vol.14 , pp. 151-161
    • Pollaro, L.1    Raghunathan, S.2    Morales-Sanfrutos, J.3
  • 77
    • 84914819810 scopus 로고    scopus 로고
    • Improving monoclonal antibody selection and engineering using measurements of colloidal protein interactions
    • COI: 1:CAS:528:DC%2BC2cXhsFWitrbO, PID: 25209466
    • Geng SB, Cheung JK, Narasimhan C et al (2014) Improving monoclonal antibody selection and engineering using measurements of colloidal protein interactions. J Pharm Sci 103:3356–3363
    • (2014) J Pharm Sci , vol.103 , pp. 3356-3363
    • Geng, S.B.1    Cheung, J.K.2    Narasimhan, C.3
  • 78
    • 84869840045 scopus 로고    scopus 로고
    • A strategy for risk mitigation of antibodies with fast clearance
    • PID: 23778268
    • Hotzel I, Theil FP, Bernstein LJ et al (2012) A strategy for risk mitigation of antibodies with fast clearance. MAbs 4:753–760
    • (2012) MAbs , vol.4 , pp. 753-760
    • Hotzel, I.1    Theil, F.P.2    Bernstein, L.J.3
  • 79
    • 84861861669 scopus 로고    scopus 로고
    • Tumor targeting using affibody molecules: interplay of affinity, target expression level, and binding site composition
    • COI: 1:CAS:528:DC%2BC38XhtVyntL3L, PID: 22586147
    • Tolmachev V, Tran TA, Rosik D et al (2012) Tumor targeting using affibody molecules: interplay of affinity, target expression level, and binding site composition. J Nucl Med 53:953–960
    • (2012) J Nucl Med , vol.53 , pp. 953-960
    • Tolmachev, V.1    Tran, T.A.2    Rosik, D.3
  • 80
    • 84918566063 scopus 로고    scopus 로고
    • Quantitative in vivo immunohistochemistry of epidermal growth factor receptor using a receptor concentration imaging approach
    • COI: 1:CAS:528:DC%2BC2cXitVOht7zN, PID: 25344226
    • Samkoe KS, Tichauer KM, Gunn JR et al (2014) Quantitative in vivo immunohistochemistry of epidermal growth factor receptor using a receptor concentration imaging approach. Cancer Res 74:7465–7474
    • (2014) Cancer Res , vol.74 , pp. 7465-7474
    • Samkoe, K.S.1    Tichauer, K.M.2    Gunn, J.R.3
  • 81
    • 23044438069 scopus 로고    scopus 로고
    • Quantitative evaluation of a monoclonal antibody and its fragment as potential markers for pancreatic beta cell mass
    • COI: 1:CAS:528:DC%2BD2MXmslCmsLc%3D, PID: 16025399
    • Hampe CS, Wallen AR, Schlosser M et al (2005) Quantitative evaluation of a monoclonal antibody and its fragment as potential markers for pancreatic beta cell mass. Exp Clin Endocrinol Diabetes 113:381–387
    • (2005) Exp Clin Endocrinol Diabetes , vol.113 , pp. 381-387
    • Hampe, C.S.1    Wallen, A.R.2    Schlosser, M.3
  • 82
    • 84888376674 scopus 로고    scopus 로고
    • Sphingomyelin patches on pancreatic beta-cells are indicative of insulin secretory capacity
    • COI: 1:CAS:528:DC%2BC2cXhslOhtA%3D%3D, PID: 23920110
    • Kavishwar A, Moore A (2013) Sphingomyelin patches on pancreatic beta-cells are indicative of insulin secretory capacity. J Histochem Cytochem 61:910–919
    • (2013) J Histochem Cytochem , vol.61 , pp. 910-919
    • Kavishwar, A.1    Moore, A.2


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