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2025”N“x Research.com Œ¤‹†ŽÒƒ‰ƒ“ƒLƒ“ƒOi¶•¨ŠwA¶‰»Šw•ª–ìjF#84 (Japan ranking) #1497 (world ranking)

 

mŒ´’˜˜_•¶n

 

No.1) Fukuda, M., Kuroda, T. S. and Mikoshiba, K. (2002) Slac2-a/melanophilin, the missing link between Rab27 and myosin Va: Implications of a tripartite protein complex for melanosome transport. J. Biol. Chem. 277, 12432-12436 [PubMed]i”íˆø—p”299jm•\ކn“–ŠYŒ¤‹†•ª–ì‚É‚¨‚¢‚Ä”íˆø—p—¦‚ÅãˆÊ1%‚É‚àƒ‰ƒ“ƒN‚³‚ê‚Ü‚µ‚½mƒŠƒ“ƒNnB

 

No.2) Fukuda, M., Aruga, J., Niinobe, M., Aimoto, S. and Mikoshiba, K. (1994) Inositol-1,3,4,5-tetrakisphosphate binding to C2B domain of IP4BP/synaptotagmin II. J. Biol. Chem. 269, 29206-29211 [PubMed]i”íˆø—p”237j

 

No.3) Itoh, T., Fujita, N., Kanno, E., Yamamoto, A., Yoshimori, T. and Fukuda, M. (2008) Golgi-resident small GTPase Rab33B interacts with Atg16L and modulates autophagosome formation. Mol. Biol. Cell 19, 2916-2925 [PubMed] i”íˆø—p”224j

 

No.4) Fukuda, M., Kanno, E., Ishibashi, K. and Itoh, T. (2008) Large scale screening for novel Rab effectors reveals unexpected broad Rab binding specificity. Mol. Cell. Proteomics 7, 1031-1042 [PubMed] i”íˆø—p”203j

 

No.5) Fukuda, M., Kojima, T., Kabayama, H. and Mikoshiba, K. (1996) Mutation of the pleckstrin homology domain of Bruton's tyrosine kinase in immunodeficiency impaired inositol 1,3,4,5-tetrakisphosphate binding capacity. J. Biol. Chem. 271, 30303-30306 [PubMed]i”íˆø—p”194j

 

No.6) Kuroda, T. S., Fukuda, M., Ariga, H. and Mikoshiba, K. (2002) The Slp homology domain of synaptotagmin-like proteins 1-4 and Slac2 functions as a novel Rab27A binding domain. J. Biol. Chem. 277, 9212-9218 [PubMed]i”íˆø—p”181j

 

No.7) Fukuda, M., Kojima, T., Aruga, J., Niinobe, M. and Mikoshiba, K. (1995) Functional diversity of C2 domains of synaptotagmin family: Mutational analysis of inositol high polyphosphate binding domain. J. Biol. Chem. 270, 26523-26527 [PubMed]i”íˆø—p”168j

 

No.8) Fukuda, M. (2003) Distinct Rab binding specificity of Rim1, Rim2, rabphilin, and Noc2: Identification of a critical determinant of Rab3A/Rab27A recognition by Rim2. J. Biol. Chem. 278, 15373-15380 [PubMed]i”íˆø—p”161j

 

No.9) Tsuboi, T. and Fukuda, M. (2006) Rab3A and Rab27A cooperatively regulate the docking step of dense-core vesicle exocytosis in PC12 cells. J. Cell Sci. 119, 2196-2203 [PubMed] i”íˆø—p”158j

 

No.10) Fukuda, M., Kanno, E. and Mikoshiba, K. (1999) Conserved N-terminal cysteine motif is essential for homo- and heterodimer formation of synaptotagmins III, V, VI, and X. J. Biol. Chem. 274, 31421-31427 [PubMed]i”íˆø—p”150j

 

No.11) Fukuda, M., Moreira, J. E., Lewis, F. M. T., Sugimori, M., Niinobe, M., Mikoshiba, K. and Llinás, R. (1995) Role of the C2B domain of synaptotagmin in vesicular release and recycling as determined by specific antibody injection into the squid giant synapse preterminal. Proc. Natl. Acad. Sci. USA 92, 10708-10712 [PubMed]i”íˆø—p”145j

 

No.12) Fukuda, M. and Kuroda, T. S. (2002) Slac2-c (synaptotagmin-like protein homologue lacking C2 domains-c), a novel linker protein that interacts with Rab27, myosin Va/VIIa, and actin. J. Biol. Chem. 277, 43096-43103 [PubMed] i”íˆø—p”137j

 

No.13) Itoh, T., Kanno, E., Uemura, T., Waguri, S. and Fukuda, M. (2011) OATL1, a novel autophagosome-resident Rab33B-GAP, regulates autophagosomal maturation. J. Cell Biol. 192, 839-853 [PubMed]i”íˆø—p”130j

 

No.14) Itoh, T., Satoh, M., Kanno, E. and Fukuda, M. (2006) Screening for target Rabs of TBC (Tre-2/Bub2/Cdc16) domain-containing proteins based on their Rab-binding activity. Genes Cells 11, 1023-1037 [PubMed]i”íˆø—p”130j

 

No.15) Kuroda, T. S. and Fukuda, M. (2004) Rab27A-binding protein Slp2-a is required for peripheral melanosome distribution and elongated cell shape in melanocytes. Nature Cell Biol. 6, 1195-1203 [PubMed]i”íˆø—p”129j

 

No.16) Fukuda, M., Kowalchyk, J. A., Zhang, X., Martin, T. F. J. and Mikoshiba, K. (2002) Synaptotagmin IX regulates Ca2+-dependent secretion in PC12 cells. J. Biol. Chem. 277, 4601-4604 [PubMed]i”íˆø—p”120j

 

No.17) Mikoshiba, K., Fukuda, M., Moreira, J. E., Lewis, F. M. T., Sugimori, M., Niinobe, M. and Llinás, R. (1995) Role of the C2A domain of synaptotagmin in transmitter release as determined by specific antibody injection into the squid giant synapse preterminal. Proc. Natl. Acad. Sci. USA 92, 10703-10707 [PubMed]i”íˆø—p”115j

 

No.18) Kuroda, T. S., Ariga, H. and Fukuda, M. (2003) The actin-binding domain of Slac2-a/melanophilin is required for melanosome distribution in melanocytes. Mol. Cell. Biol. 23, 5245-5255 [PubMed]i”íˆø—p”108j

 

No.19) Fukuda, M. and Mikoshiba, K. (1999) A novel alternatively spliced variant of synaptotagmin VI lacking a transmembrane domain: Implications for distinct functions of the two isoforms. J. Biol. Chem. 274, 31428-31434 [PubMed]i”íˆø—p”103j

 

No.20) Imai, A., Yoshie, S., Nashida, T., Shimomura, H. and Fukuda, M. (2004) The small GTPase Rab27B regulates amylase release from rat parotid acinar cells. J. Cell Sci. 117, 1945-1953 [PubMed]i”íˆø—p”95j

 

m‘àn

 

No.1) Fukuda, M. (2008) Regulation of secretory vesicle traffic by Rab small GTPases. Cell. Mol. Life Sci. 65, 2801-2813 [PubMed] i”íˆø—p”321j

 

No.2) Homma, Y. Hiragi, S. and Fukuda, M. (2021) Rab family of small GTPases: an updated view on their regulation and functions. FEBS J. 288, 36-55 [PubMed]iF1000Prime‚ÌRecommended paper‚Æ‚µ‚Ä‘I’èj[Certificate]i”íˆø—p”318j

 

No.3) Fukuda, M. (2005) Versatile role of Rab27 in membrane trafficking: Focus on the Rab27 effector families. J. Biochem. 137, 9-16 [PubMed]i”íˆø—p”192j

 

No.4) Fukuda, M. (2013) Rab27 effectors, pleiotropic regulators in secretory pathways. Traffic 14, 949-963 [PubMed] i”íˆø—p”179j

 

No.5) Fukuda, M. (2011) TBC proteins: GAPs for mammalian small GTPase Rab? Biosci. Rep. 31, 159-168 [PubMed]i”íˆø—p”155j

 

No.6) Fukuda, M. and Mikoshiba, K. (1997) The function of inositol high polyphosphate binding proteins. BioEssays 19, 593-603 [PubMed]i”íˆø—p”90j

 

No.7) Kuchitsu, Y. and Fukuda, M. (2018) Revisiting Rab7 functions in mammalian autophagy: Rab7 knockout studies. Cells 7, 215 [PubMed] [PubMed]i”íˆø—p”78j

 

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