DOI: 10.1038/nrm1500. Targeting Rab GTPases to distinct membrane compartments

Targeting Rab GTPases to distinct membrane compartments

10.1038/nrm1500

Crossref journal-article

Springer Science and Business Media LLC

Nature Reviews Molecular Cell Biology (297)

Bibliography

Pfeffer, S., & Aivazian, D. (2004). Targeting Rab GTPases to distinct membrane compartments. Nature Reviews Molecular Cell Biology, 5(11), 886â896.

Authors 2

Suzanne Pfeffer (first)
Dikran Aivazian (additional)

References 56 Referenced 382

Zerial, M. & McBride, H. Rab proteins as membrane organizers. Nature Rev. Mol. Cell Biol. 2, 107–117 (2001). (10.1038/35052055) / Nature Rev. Mol. Cell Biol. by M Zerial (2001)
Pfeffer, S. R. Rab GTPases: specifying and deciphering organelle identity and function. Trends Cell Biol. 11, 487–491 (2001). (10.1016/S0962-8924(01)02147-X) / Trends Cell Biol. by SR Pfeffer (2001)
Pereira-Leal, J. B. & Seabra, M. C. Evolution of the Rab family of small GTP-binding proteins. J. Mol. Biol. 313, 889–901 (2001). (10.1006/jmbi.2001.5072) / J. Mol. Biol. by JB Pereira-Leal (2001)
Segev, N. Ypt and Rab GTPases: insight into functions through novel interactions. Curr. Opin. Cell Biol. 13, 500–511 (2001). (10.1016/S0955-0674(00)00242-8) / Curr. Opin. Cell Biol. by N Segev (2001)
Alory, C. & Balch, W. E. Organization of the Rab-GDI/Chm superfamily: the functional basis for choroideremia disease. Traffic 2, 532–543 (2001). (10.1034/j.1600-0854.2001.20803.x) / Traffic by C Alory (2001)
Ullrich, O., Horiuchi, H., Bucci, C. & Zerial, M. Membrane association of Rab5 mediated by GDP-dissociation inhibitor and accompanied by GDP/GTP exchange. Nature 368, 157–160 (1994). Reports the in vitro reconstitution of specific, prenylated Rab delivery onto membranes using streptolysin-O-permeabilized cells. (10.1038/368157a0) / Nature by O Ullrich (1994)
Soldati, T., Shapiro, A. D., Svejstrup, A. B. & Pfeffer, S. R. Membrane targeting of the small GTPase Rab9 is accompanied by nucleotide exchange. Nature 369, 76–78 (1994). Describes the in vitro reconstitution of specific, prenylated Rab delivery onto membranes using purified components. (10.1038/369076a0) / Nature by T Soldati (1994)
Soldati, T., Rancano, C., Geissler, H. & Pfeffer, S. R. Rab7 and Rab9 are recruited onto late endosomes by biochemically distinguishable processes. J. Biol. Chem. 270, 25541–25548 (1995). (10.1074/jbc.270.43.25541) / J. Biol. Chem. by T Soldati (1995)
Schalk, I. et al. Structure and mutational analysis of Rab GDP-dissociation inhibitor. Nature 381, 42–48 (1996). Describes the first three-dimensional structure of bovine GDI and a mutational analysis that identifies the residues that contribute to the Rab-binding site. (10.1038/381042a0) / Nature by I Schalk (1996)
Luan, P. et al. A new functional domain of guanine nucleotide dissociation inhibitor (αGDI) involved in Rab recycling. Traffic 1, 270–281 (2000). (10.1034/j.1600-0854.2000.010309.x) / Traffic by P Luan (2000)
An, Y. et al. Geranylgeranyl switching regulates GDI–Rab GTPase recycling. Structure 11, 347–357 (2003). Presents the structure of bovine GDIα crystallized with a prenyl (geranylgeranyl) group bound. The authors detected the ordering of a so-called 'mobile effector loop' that is probably important for GDI function. (10.1016/S0969-2126(03)00034-0) / Structure by Y An (2003)
Rak, A. et al. Structure of Rab GDP-dissociation inhibitor in complex with prenylated YPT1 GTPase. Science 302, 646–650 (2003). This beautiful paper identifies a prenyl-binding site at the base of GDI that becomes exposed when prenylated Ypt1 binds to the yeast GDI. (10.1126/science.1087761) / Science by A Rak (2003)
Sasaki, T. et al. Purification and characterization from bovine brain cytosol of a protein that inhibits the dissociation of GDP from and the subsequent binding of GTP to smg p25A, a ras p21-like GTP-binding protein. J. Biol. Chem. 265, 2333–2337 (1990). Reports the discovery of Rab GDI. (10.1016/S0021-9258(19)39980-6) / J. Biol. Chem. by T Sasaki (1990)
Sasaki, T., Kaibuchi, K., Kabcenell, A. K., Novick, P. J. & Takai, Y. A mammalian inhibitory GDP/GTP exchange protein (GDP dissociation inhibitor) for smg p25A is active on the yeast SEC4 protein. Mol. Cell. Biol. 11, 2909–2912 (1991). (10.1128/MCB.11.5.2909) / Mol. Cell. Biol. by T Sasaki (1991)
Regazzi, R., Kikuchi, A., Takai, Y. & Wollheim, C. B. The small GTP-binding proteins in the cytosol of insulin-secreting cells are complexed to GDP dissociation inhibitor proteins. J. Biol. Chem. 267, 17512–17519 (1992). (10.1016/S0021-9258(19)37072-3) / J. Biol. Chem. by R Regazzi (1992)
Ullrich, O. et al. Rab GDP dissociation inhibitor as a general regulator for the membrane association of rab proteins. J. Biol. Chem. 268, 18143–18150 (1993). (10.1016/S0021-9258(17)46822-0) / J. Biol. Chem. by O Ullrich (1993)
Nishimura, N., Nakamura, H., Takai, Y. & Sano, K. Molecular cloning and characterization of two rab GDI species from rat brain: brain-specific and ubiquitous types. J. Biol. Chem. 269, 14191–14198 (1994). (10.1016/S0021-9258(17)36773-X) / J. Biol. Chem. by N Nishimura (1994)
Shisheva, A., Chinni, S. R. & DeMarco, C. General role of GDP dissociation inhibitor 2 in membrane release of Rab proteins: modulations of its functional interactions by in vitro and in vivo structural modifications. Biochemistry 38, 11711–11721 (1999). (10.1021/bi990200r) / Biochemistry by A Shisheva (1999)
Garrett, M. D., Zahner, J. E., Cheney, C. M. & Novick, P. J. GDI1 encodes a GDP dissociation inhibitor that plays an essential role in the yeast secretory pathway. EMBO J. 13, 1718–1728 (1994). (10.1002/j.1460-2075.1994.tb06436.x) / EMBO J. by MD Garrett (1994)
Luan, P., Balch, W. E., Emr, S. D. & Burd, C. G. Molecular dissection of guanine nucleotide dissociation inhibitor function in vivo. Rab-independent binding to membranes and role of Rab recycling factors. J. Biol. Chem. 274, 14806–14817 (1999). (10.1074/jbc.274.21.14806) / J. Biol. Chem. by P Luan (1999)
Stroupe, C. & Brunger, A. T. Crystal structures of a Rab protein in its inactive and active conformations. J. Mol. Biol. 304, 585–598 (2000). (10.1006/jmbi.2000.4236) / J. Mol. Biol. by C Stroupe (2000)
Chavrier, P., Gorvel, J. P., Stelzer, E., Simons, K., Gruenberg, J. & Zerial, M. Hypervariable C-terminal domain of rab proteins acts as a targeting signal. Nature 353, 769–772 (1991). (10.1038/353769a0) / Nature by P Chavrier (1991)
Shapiro, A. D. & Pfeffer, S. R. Quantitative analysis of the interactions between prenyl Rab9, GDP dissociation inhibitor-α, and guanine nucleotides. J. Biol. Chem. 270, 11085–11090 (1995). (10.1074/jbc.270.19.11085) / J. Biol. Chem. by AD Shapiro (1995)
Calero, M. et al. Dual prenylation is required for Rab protein localization and function. Mol. Biol. Cell 14, 1852–1867 (2003). (10.1091/mbc.e02-11-0707) / Mol. Biol. Cell by M Calero (2003)
Calero, M., Whittaker, G. R. & Collins, R. N. Yop1p, the yeast homolog of the polyposis locus protein 1, interacts with Yip1p and negatively regulates cell growth. J. Biol. Chem. 276, 12100–12112 (2001). (10.1074/jbc.M008439200) / J. Biol. Chem. by M Calero (2001)
Andres, D. A. et al. cDNA cloning of component A of Rab geranylgeranyl transferase and demonstration of its role as a Rab escort protein. Cell 73, 1091–1099 (1993). (10.1016/0092-8674(93)90639-8) / Cell by DA Andres (1993)
Pylypenko, O. et al. Structure of Rab escort protein-1 in complex with Rab geranylgeranyltransferase. Mol. Cell 11, 483–494 (2003). (10.1016/S1097-2765(03)00044-3) / Mol. Cell by O Pylypenko (2003)
Rak, A. et al. Structure of the Rab7:REP-1 complex: insights into the mechanism of Rab prenylation and choroideremia disease. Cell 117, 749–760 (2004). (10.1016/j.cell.2004.05.017) / Cell by A Rak (2004)
Steele-Mortimer, O., Gruenberg, J. & Clague, M. J. Phosphorylation of GDI and membrane cycling of Rab proteins. FEBS Lett. 329, 313–318 (1993). (10.1016/0014-5793(93)80244-O) / FEBS Lett. by O Steele-Mortimer (1993)
Cavalli, V. et al. The stress-induced MAP kinase p38 regulates endocytic trafficking via the GDI:Rab5 complex. Mol. Cell 7, 421–432 (2001). Indicates that phosphorylation of a key serine residue has a role in GDI function. (10.1016/S1097-2765(01)00189-7) / Mol. Cell by V Cavalli (2001)
Dirac-Svejstrup, A. B., Sumizawa, T. & Pfeffer, S. R. Identification of a GDI displacement factor that releases endosomal Rab GTPases from Rab–GDI. EMBO J. 16, 465–472 (1997). Describes a novel assay that was designed to detect GDF activity, for the first time, on endosome membranes. The activity studied was specific for endosomal Rabs. (10.1093/emboj/16.3.465) / EMBO J. by AB Dirac-Svejstrup (1997)
Sivars, U., Aivazian, D. & Pfeffer, S. R. Yip3 catalyses the dissociation of endosomal Rab–GDI complexes. Nature 425, 856–859 (2003). The first description of GDF identification using biochemical analysis. (10.1038/nature02057) / Nature by U Sivars (2003)
Yang, X., Matern, H. T. & Gallwitz, D. Specific binding to a novel and essential Golgi membrane protein (Yip1p) functionally links the transport GTPases Ypt1p and Ypt31p. EMBO J. 17, 4954–4963 (1998). The first report of Yip proteins as interactors with yeast Rab/Ypt GTPases. (10.1093/emboj/17.17.4954) / EMBO J. by X Yang (1998)
Calero, M. & Collins, R. N. S. cerevisiae Pra1p/Yip3 interacts with Yip1p and Rab proteins. Biochem. Biophys. Res. Comm. 290, 676–681 (2002). (10.1006/bbrc.2001.6242) / Biochem. Biophys. Res. Comm. by M Calero (2002)
Calero, M., Winand, N. J. & Collins, R. N. Identification of the novel proteins Yip4p and Yip5p as Rab GTPase interacting factors. FEBS Lett. 515, 89–98 (2002). (10.1016/S0014-5793(02)02442-0) / FEBS Lett. by M Calero (2002)
Matern, H. et al. A novel Golgi membrane protein is part of a GTPase-binding protein complex involved in vesicle targeting. EMBO J. 19, 4485–4492 (2000). The first characterization of Yif1. (10.1093/emboj/19.17.4485) / EMBO J. by H Matern (2000)
Lin, J., Liang, Z., Zhang, Z. & Li, G. Membrane topography and topogenesis of prenylated Rab acceptor (PRA1). J. Biol. Chem. 276, 41733–41741 (2001). (10.1074/jbc.M103475200) / J. Biol. Chem. by J Lin (2001)
Martincic, I., Peralta, M. E. & Ngsee, J. K. Isolation and characterization of a dual prenylated Rab and VAMP2 receptor. J. Biol. Chem. 272, 26991–26998 (1997). Shows that PRA1 (human Yip3) can bind to certain v-SNAREs and to numerous prenylated Rab GTPases. (10.1074/jbc.272.43.26991) / J. Biol. Chem. by I Martincic (1997)
Bucci, C., Chiariello, M., Lattero, D., Maiorano, M. & Bruni, C. B. Interaction cloning and characterization of the cDNA encoding the human prenylated Rab acceptor (PRA1). Biochem. Biophys. Res. Comm. 258, 657–662 (1999). (10.1006/bbrc.1999.0651) / Biochem. Biophys. Res. Comm. by C Bucci (1999)
Hutt, D. M., Da-Silva, L. F., Chang, L. H., Prosser, D. C. & Ngsee, J. K. PRA1 inhibits the extraction of membrane-bound Rab GTPase by GDI1. J. Biol. Chem. 275, 18511–18519 (2000). (10.1074/jbc.M909309199) / J. Biol. Chem. by DM Hutt (2000)
Abdul-Ghani, M., Gougeon, P. Y., Prosser, D. C., Da-Silva, L. F. & Ngsee, J. K. PRA isoforms are targeted to distinct membrane compartments. J. Biol. Chem. 276, 6225–6233 (2001). (10.1074/jbc.M009073200) / J. Biol. Chem. by M Abdul-Ghani (2001)
Figueroa, C., Taylor, J. & Vojtek, A. B. Prenylated Rab acceptor protein is a receptor for prenylated small GTPases. J. Biol. Chem. 276, 28219–28225 (2001). (10.1074/jbc.M101763200) / J. Biol. Chem. by C Figueroa (2001)
Du, L. L. & Novick, P. Yeast rab GTPase-activating protein Gyp1p localizes to the Golgi apparatus and is a negative regulator of Ypt1p. Mol. Biol. Cell 12, 1215–1226 (2001). Shows that a Rab-GTPase-activating protein, which can function on numerous Rabs in vitro , is highly specific in living cells. (10.1091/mbc.12.5.1215) / Mol. Biol. Cell by LL Du (2001)
Heidtman, M., Chen, C. Z., Collins, R. N. & Barlowe, C. A role for Yip1p in COPII vesicle biogenesis. J. Cell Biol. 163, 57–69 (2003). (10.1083/jcb.200306118) / J. Cell Biol. by M Heidtman (2003)
Barrowman, J., Wang, W., Zhang, Y. & Ferro-Novick, S. The Yip1p–Yif1p complex is required for the fusion competence of endoplasmic reticulum-derived vesicles. J. Biol. Chem. 278, 19878–19884 (2003). (10.1074/jbc.M302406200) / J. Biol. Chem. by J Barrowman (2003)
Tang, B. L. et al. Membrane protein enriched in ER exit sites interacts with COPII. J. Biol. Chem. 276, 40008–40017 (2001). (10.1074/jbc.M106189200) / J. Biol. Chem. by BL Tang (2001)
Otte, S., Belden, W. J., Heidtman, M., Liu, J., Jensen, O. N. & Barlowe, C. Erv41p and Erv46p: new components of COPII vesicles involved in transport between the ER and Golgi complex. J. Cell Biol. 152, 503–518 (2001). (10.1083/jcb.152.3.503) / J. Cell Biol. by S Otte (2001)
Yamashita, T. & Tohyama, M. The p75 receptor acts as a displacement factor that releases Rho from Rho-GDI. Nature Neurosci. 6, 461–467 (2003). (10.1038/nn1045) / Nature Neurosci. by T Yamashita (2003)
Robbe, K., Otto-Bruc, A., Chardin, P. & Antonny, B. Dissociation of GDP dissociation inhibitor and membrane translocation are required for efficient activation of Rac by the Dbl homology-pleckstrin homology region of Tiam. J. Biol. Chem. 278, 4756–4762 (2003). (10.1074/jbc.M210412200) / J. Biol. Chem. by K Robbe (2003)
Del Pozo, M. A. et al. Integrins regulate GTP-Rac localized effector interactions through dissociation of Rho-GDI. Nature Cell Biol. 4, 232–239 (2002). (10.1038/ncb759) / Nature Cell Biol. by MA Del Pozo (2002)
Sakisaka, T., Meerlo, T., Matteson, J., Plutner, H. & Balch, W. E. Rabα-GDI activity is regulated by a Hsp90 chaperone complex. EMBO J. 21, 6125–6135 (2002). (10.1093/emboj/cdf603) / EMBO J. by T Sakisaka (2002)
Shakoori, A. et al. Identification of a five-pass transmembrane protein family localizing in the Golgi apparatus and the ER. Biochem. Biophys. Res. Comm. 312, 850–857 (2003). (10.1016/j.bbrc.2003.10.197) / Biochem. Biophys. Res. Comm. by A Shakoori (2003)
Liang, Z., Veeraprame, H., Bayan, N. & Li, G. The C-terminus of prenylin is important in forming a dimer conformation necessary for endoplasmic-reticulum-to-Golgi transport. Biochem. J. 380, 43–49 (2004). (10.1042/bj20031788) / Biochem. J. by Z Liang (2004)
Janoueix-Lerosey, I., Jollivet, F., Camonis, J., Marche, P. N. & Goud, B. Two-hybrid system screen with the small GTP-binding protein Rab6. Identification of a novel mouse GDP dissociation inhibitor isoform and two other potential partners of Rab6. J. Biol. Chem. 270, 14801–14808 (1995). (10.1074/jbc.270.24.14801) / J. Biol. Chem. by I Janoueix-Lerosey (1995)
Evans, D. T., Tillman, K. C. & Desrosiers, R. C. Envelope glycoprotein cytoplasmic domains from diverse lentiviruses interact with the prenylated Rab acceptor. J. Virol. 76, 327–337 (2002). (10.1128/JVI.76.1.327-337.2002) / J. Virol. by DT Evans (2002)
Fenster, S. D. et al. Piccolo, a presynaptic zinc finger protein structurally related to Bassoon. Neuron 25, 203–214 (2000). (10.1016/S0896-6273(00)80883-1) / Neuron by SD Fenster (2000)

Dates

Type	When
Created	20 years, 10 months ago (Nov. 2, 2004, 12:27 p.m.)
Deposited	2 years, 3 months ago (May 18, 2023, 11:48 p.m.)
Indexed	2 weeks, 2 days ago (Aug. 19, 2025, 6:56 a.m.)
Issued	20 years, 10 months ago (Nov. 1, 2004)
Published	20 years, 10 months ago (Nov. 1, 2004)
Published Print	20 years, 10 months ago (Nov. 1, 2004)

Funders 0

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BibTeX

@article{Pfeffer_2004, title={Targeting Rab GTPases to distinct membrane compartments}, volume={5}, ISSN={1471-0080}, url={http://dx.doi.org/10.1038/nrm1500}, DOI={10.1038/nrm1500}, number={11}, journal={Nature Reviews Molecular Cell Biology}, publisher={Springer Science and Business Media LLC}, author={Pfeffer, Suzanne and Aivazian, Dikran}, year={2004}, month=nov, pages={886–896} }

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    },
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      "journal-title": "J. Biol. Chem."
    },
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      "journal-title": "J. Biol. Chem."
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      "journal-title": "J. Biol. Chem."
    },
    {
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      "journal-title": "J. Biol. Chem."
    },
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      "year": "2000",
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      "journal-title": "J. Mol. Biol."
    },
    {
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      "journal-title": "J. Biol. Chem."
    },
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      "year": "2003",
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      "year": "2004",
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      "year": "1993",
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      "journal-title": "FEBS Lett."
    },
    {
      "key": "BFnrm1500_CR30",
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      "year": "2001",
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    },
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      "year": "2003",
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    },
    {
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      "year": "2002",
      "unstructured": "Calero, M. & Collins, R. N. S. cerevisiae Pra1p/Yip3 interacts with Yip1p and Rab proteins. Biochem. Biophys. Res. Comm. 290, 676\u2013681 (2002).",
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    },
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      "author": "M Calero",
      "year": "2002",
      "unstructured": "Calero, M., Winand, N. J. & Collins, R. N. Identification of the novel proteins Yip4p and Yip5p as Rab GTPase interacting factors. FEBS Lett. 515, 89\u201398 (2002).",
      "journal-title": "FEBS Lett."
    },
    {
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      "year": "2000",
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      "journal-title": "EMBO J."
    },
    {
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      "author": "J Lin",
      "year": "2001",
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      "journal-title": "J. Biol. Chem."
    },
    {
      "key": "BFnrm1500_CR38",
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      "journal-title": "J. Biol. Chem."
    },
    {
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      "year": "1999",
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    },
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      "journal-title": "J. Biol. Chem."
    },
    {
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    },
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      "author": "C Figueroa",
      "year": "2001",
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      "year": "2001",
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      "journal-title": "J. Biol. Chem."
    },
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    },
    {
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      "year": "2003",
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      "journal-title": "J. Biol. Chem."
    },
    {
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      "doi-asserted-by": "publisher",
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      "DOI": "10.1038/ncb759",
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      "year": "2002",
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    {
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      "year": "2002",
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      "journal-title": "EMBO J."
    },
    {
      "key": "BFnrm1500_CR52",
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      "year": "2003",
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      "journal-title": "Biochem. Biophys. Res. Comm."
    },
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      "doi-asserted-by": "publisher",
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      "DOI": "10.1042/bj20031788",
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      "author": "Z Liang",
      "year": "2004",
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      "journal-title": "Biochem. J."
    },
    {
      "key": "BFnrm1500_CR54",
      "doi-asserted-by": "publisher",
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      "year": "1995",
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      "journal-title": "J. Biol. Chem."
    },
    {
      "key": "BFnrm1500_CR55",
      "doi-asserted-by": "publisher",
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      "year": "2002",
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