메뉴 건너뛰기




Volumn 22, Issue 9, 2013, Pages 1266-1278

Development of a fluorescent monoclonal antibody-based assay to measure the allosteric effects of synthetic peptides on self-oligomerization of AGR2 protein

Author keywords

Allostery; Monoclonal antibody; Oligomerization; Protein interactions

Indexed keywords

MONOCLONAL ANTIBODY; PROTEIN AGR2; SYNTHETIC PEPTIDE; TUMOR PROTEIN; UNCLASSIFIED DRUG; AGR2 PROTEIN, HUMAN; CARRIER PROTEIN; DNA HELICASE; FLUORESCENT DYE; LIGAND; PROTEIN; PROTEIN BINDING; RUVBL2 PROTEIN, HUMAN;

EID: 84892934018     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.2299     Document Type: Article
Times cited : (21)

References (35)
  • 1
    • 84866978465 scopus 로고    scopus 로고
    • Searching for the holy grail protein-protein interaction analysis and modulation
    • Morelli X, Hupp T (2012) Searching for the Holy Grail; protein-protein interaction analysis and modulation. EMBO Rep 13:877-879.
    • (2012) EMBO Rep , vol.13 , pp. 877-879
    • Morelli, X.1    Hupp, T.2
  • 2
    • 84855812283 scopus 로고    scopus 로고
    • Modulating protein-protein interactions with small molecules: The importance of binding hotspots
    • Thangudu R, Bryant SH, Panchenko R, Madej T (2012) Modulating protein-protein interactions with small molecules: The importance of binding hotspots. J Mol Biol 415:443-453.
    • (2012) J Mol Biol , vol.415 , pp. 443-453
    • Thangudu, R.1    Bryant, S.H.2    Panchenko, R.3    Madej, T.4
  • 3
    • 0032749078 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins: Re-assessing the protein structure-function paradigm
    • Wright PE, Dyson HJ (1999) Intrinsically unstructured proteins: Re-assessing the protein structure-function paradigm. J Mol Biol 293:321-331.
    • (1999) J Mol Biol , vol.293 , pp. 321-331
    • Wright, P.E.1    Dyson, H.J.2
  • 4
  • 5
    • 84870810902 scopus 로고    scopus 로고
    • Biophysical and computational fragment-based approaches to targeting protein- protein interactions: Applications in structure-guided drug discovery
    • Winter A, Higueruelo AP, Marsh M, Sigurdardottir A, Pitt WR, Blundell TL (2012) Biophysical and computational fragment-based approaches to targeting protein- protein interactions: Applications in structure-guided drug discovery. Q Rev Biophys 45:383-426.
    • (2012) Q Rev Biophys , vol.45 , pp. 383-426
    • Winter, A.1    Higueruelo, A.P.2    Marsh, M.3    Sigurdardottir, A.4    Pitt, W.R.5    Blundell, T.L.6
  • 6
    • 84874517756 scopus 로고    scopus 로고
    • Features of protein- protein interactions that translate into potent inhibitors: Topology, surface area and affinity
    • Smith MC, Gestwicki JE (2012) Features of protein- protein interactions that translate into potent inhibitors: Topology, surface area and affinity. Expert Rev Mol Med 14:e16.
    • (2012) Expert Rev Mol Med , vol.14
    • Smith, M.C.1    Gestwicki, J.E.2
  • 10
    • 84857828499 scopus 로고    scopus 로고
    • Allostery and the dynamic oligomerization of porphobilinogen synthase
    • Jaffe EK, Lawrence SH (2012) Allostery and the dynamic oligomerization of porphobilinogen synthase. Arch Biochem Biophys 519:144-153.
    • (2012) Arch Biochem Biophys , vol.519 , pp. 144-153
    • Jaffe, E.K.1    Lawrence, S.H.2
  • 12
    • 48249097986 scopus 로고    scopus 로고
    • Intrinsically disordered proteins in human diseases: Introducing the D2 concept
    • Uversky VN, Oldfield CJ, Dunker AK (2008) Intrinsically disordered proteins in human diseases: Introducing the D2 concept. Annu Rev Biophys 37:215-246.
    • (2008) Annu Rev Biophys , vol.37 , pp. 215-246
    • Uversky, V.N.1    Oldfield, C.J.2    Dunker, A.K.3
  • 13
    • 84862873871 scopus 로고    scopus 로고
    • On the supertertiary structure of proteins
    • Tompa P (2012) On the supertertiary structure of proteins. Nat Chem Biol 8:597-600.
    • (2012) Nat Chem Biol , vol.8 , pp. 597-600
    • Tompa, P.1
  • 14
    • 84875826727 scopus 로고    scopus 로고
    • Intrinsically disordered proteins undergo and assist folding transitions in the proteome
    • Kovacs D, Szabo B, Pancsa R, Tompa P (2012) Intrinsically disordered proteins undergo and assist folding transitions in the proteome. Arch Biochem Biophys 531:80-89.
    • (2012) Arch Biochem Biophys , vol.531 , pp. 80-89
    • Kovacs, D.1    Szabo, B.2    Pancsa, R.3    Tompa, P.4
  • 16
    • 33846239416 scopus 로고    scopus 로고
    • The Mdm2 RING domain Cterminus is required for supramolecular assembly and ubiquitin ligase activity
    • Poyurovsky MV, Priest C, Kentsis A, Borden KL, Pan ZQ, Pavletich N, Prives C (2007) The Mdm2 RING domain Cterminus is required for supramolecular assembly and ubiquitin ligase activity. EMBO J 26:90-101.
    • (2007) EMBO J , vol.26 , pp. 90-101
    • Poyurovsky, M.V.1    Priest, C.2    Kentsis, A.3    Borden, K.L.4    Pan, Z.Q.5    Pavletich, N.6    Prives, C.7
  • 17
    • 33748920505 scopus 로고    scopus 로고
    • Solution structure of the Hdm2 C2H2C4 RING, a domain critical for ubiquitination of p53
    • Kostic M, Matt T, Martinez-Yamout MA, Dyson HJ, Wright PE (2006) Solution structure of the Hdm2 C2H2C4 RING, a domain critical for ubiquitination of p53. J Mol Biol 363:433-450.
    • (2006) J Mol Biol , vol.363 , pp. 433-450
    • Kostic, M.1    Matt, T.2    Martinez-Yamout, M.A.3    Dyson, H.J.4    Wright, P.E.5
  • 18
    • 77956186383 scopus 로고    scopus 로고
    • Drug discovery and mutant p53
    • Maslon MM, Hupp TR (2010) Drug discovery and mutant p53. Trends Cell Biol 20:542-555.
    • (2010) Trends Cell Biol , vol.20 , pp. 542-555
    • Maslon, M.M.1    Hupp, T.R.2
  • 22
    • 68449083815 scopus 로고    scopus 로고
    • The anterior gradient-2 pathway as a model for developing peptideaptamer anti-cancer drug leads that stimulate p53 function
    • Fourtouna A, Murray E, Nicholson J, Maslon MM, Pang L, Dryden DTF, Hupp TR (2009) The anterior gradient-2 pathway as a model for developing peptideaptamer anti-cancer drug leads that stimulate p53 function. Curr Chem Biol 3:124-137.
    • (2009) Curr Chem Biol , vol.3 , pp. 124-137
    • Fourtouna, A.1    Murray, E.2    Nicholson, J.3    Maslon, M.M.4    Pang, L.5    Dryden, D.T.F.6    Hupp, T.R.7
  • 23
    • 84874111354 scopus 로고    scopus 로고
    • Metastasis- promoting anterior gradient 2 protein has a dimeric thioredoxin fold structure and a role in cell adhesion
    • Patel P, Clarke, C, Barraclough DL, Jowitt TA, Rudland PS, Barraclough R, Lian, LY (2012) Metastasis- promoting anterior gradient 2 protein has a dimeric thioredoxin fold structure and a role in cell adhesion. J Mol Biol 425:929-943.
    • (2012) J Mol Biol , vol.425 , pp. 929-943
    • Patel, P.1    Clarke, C.2    Barraclough, D.L.3    Jowitt, T.A.4    Rudland, P.S.5    Barraclough, R.6    Lian, L.Y.7
  • 26
    • 78349311416 scopus 로고    scopus 로고
    • A divergent substrate-binding loop within the prooncogenic protein anterior gradient-2 forms a docking site for Reptin
    • Maslon MM, Hrstka R, Vojtesek B, Hupp TR (2010) A divergent substrate-binding loop within the prooncogenic protein anterior gradient-2 forms a docking site for Reptin. J Mol Biol 404:418-438.
    • (2010) J Mol Biol , vol.404 , pp. 418-438
    • Maslon, M.M.1    Hrstka, R.2    Vojtesek, B.3    Hupp, T.R.4
  • 27
    • 84455192726 scopus 로고    scopus 로고
    • Role of pro-oncogenic protein disulfide isomerase (PDI) family member anterior gradient 2 (AGR2) in the control of endoplasmic reticulum homeostasis
    • Higa A, Mulot A, Delom F, Bouchecareilh M, Nguyen DT, Boismenu D, Wise MJ, Chevet E (2011) Role of pro-oncogenic protein disulfide isomerase (PDI) family member anterior gradient 2 (AGR2) in the control of endoplasmic reticulum homeostasis. J Biol Chem 286: 44855-44868.
    • (2011) J Biol Chem , vol.286 , pp. 44855-44868
    • Higa, A.1    Mulot, A.2    Delom, F.3    Bouchecareilh, M.4    Nguyen, D.T.5    Boismenu, D.6    Wise, M.J.7    Chevet, E.8
  • 28
    • 84863394519 scopus 로고    scopus 로고
    • AGR2 gene function requires a unique endoplasmic reticulum localization motif
    • Gupta A, Dong A, Lowe AW (2012) AGR2 gene function requires a unique endoplasmic reticulum localization motif. J Biol Chem 287:4773-4782.
    • (2012) J Biol Chem , vol.287 , pp. 4773-4782
    • Gupta, A.1    Dong, A.2    Lowe, A.W.3
  • 30
    • 80052668828 scopus 로고    scopus 로고
    • Peptides derived from the bifunctional kinase/RNase enzyme IRE1alpha modulate IRE1alpha activity and protect cells from endoplasmic reticulum stress
    • Bouchecareilh M, Higa A, Fribourg S, Moenner M, Chevet E (2011) Peptides derived from the bifunctional kinase/RNase enzyme IRE1alpha modulate IRE1alpha activity and protect cells from endoplasmic reticulum stress. FASEB J 25:3115-3129.
    • (2011) FASEB J , vol.25 , pp. 3115-3129
    • Bouchecareilh, M.1    Higa, A.2    Fribourg, S.3    Moenner, M.4    Chevet, E.5
  • 31
    • 84868306591 scopus 로고    scopus 로고
    • An iTRAQ proteomics screen reveals the effects of the MDM2 binding ligand Nutlin-3 on cellular proteostasis
    • Nicholson J, Neelagandan K, Huart AS, Ball K, Molloy MP, Hupp TR (2012) An iTRAQ proteomics screen reveals the effects of the MDM2 binding ligand Nutlin-3 on cellular proteostasis. J Proteome Res 11: 5464-5478.
    • (2012) J Proteome Res , vol.11 , pp. 5464-5478
    • Nicholson, J.1    Neelagandan, K.2    Huart, A.S.3    Ball, K.4    Molloy, M.P.5    Hupp, T.R.6
  • 32
    • 56349140518 scopus 로고    scopus 로고
    • A simple and efficient expression and purification system using two newly constructed vectors
    • Liu H, Naismith JH (2009) A simple and efficient expression and purification system using two newly constructed vectors. Protein Expr Purif 63:102-111.
    • (2009) Protein Expr Purif , vol.63 , pp. 102-111
    • Liu, H.1    Naismith, J.H.2
  • 34
    • 35448956141 scopus 로고    scopus 로고
    • Hydrogen/deuterium exchange-mass spectrometry: A powerful tool for probing protein structure, dynamics and interactions
    • Tsutsui Y, Wintrode PL (2007) Hydrogen/deuterium exchange-mass spectrometry: A powerful tool for probing protein structure, dynamics and interactions. Curr Med Chem 14:2344-2358.
    • (2007) Curr Med Chem , vol.14 , pp. 2344-2358
    • Tsutsui, Y.1    Wintrode, P.L.2
  • 35
    • 84873954938 scopus 로고    scopus 로고
    • The intrinsically disordered N-terminal region of AtREM1.3 remorin protein mediates protein-protein interactions
    • Marin M, Thallmair V, Ott T (2012) The intrinsically disordered N-terminal region of AtREM1.3 remorin protein mediates protein-protein interactions. J Biol Chem 287:39982-39991.
    • (2012) J Biol Chem , vol.287 , pp. 39982-39991
    • Marin, M.1    Thallmair, V.2    Ott, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.