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Cited by in CrossRef
For: Yamaoka M, Ishizaki T, Kimura T. Interplay between Rab27a effectors in pancreatic β-cells. World J Diabetes 2015; 6(3): 508-516 [PMID: 25897360 DOI: 10.4239/wjd.v6.i3.508]
URL: https://www.wjgnet.com/1948-9358/full/v6/i3/508.htm
Number Citing Articles
1
Mostafa Jamshidiha, Inmaculada Pérez-Dorado, James W. Murray, Edward W. Tate, Ernesto Cota, Randy J. Read. Coping with strong translational noncrystallographic symmetry and extreme anisotropy in molecular replacement withPhaser: human Rab27aActa Crystallographica Section D Structural Biology 2019; 75(3): 342 doi: 10.1107/S2059798318017825
2
Xia Li, Haiying Wang, Qinggan Ni, Zhiyuan Tang, Jun Ni, Liqin Xu, Hua Huang, Songshi Ni, Jian Feng. Effects of silencing Rab27a gene on biological characteristics and chemosensitivity of non-small cell lung cancerOncotarget 2017; 8(55): 94481 doi: 10.18632/oncotarget.21782
3
Rajakrishnan Veluthakal, Debbie C. Thurmond. Emerging Roles of Small GTPases in Islet β-Cell FunctionCells 2021; 10(6): 1503 doi: 10.3390/cells10061503
4
Yanxing Shang, Xueqin Wang, Sixuan Su, Feng Ji, Donghai Shao, Chengwei Duan, Tianpeng Chen, Caixia Liang, Dongmei Zhang, Hongjian Lu. Identifying of immune‐associated genes for assessing the obesity‐associated risk to the offspring in maternal obesity: A bioinformatics and machine learningCNS Neuroscience & Therapeutics 2024; 30(3) doi: 10.1111/cns.14700
5
Matías A. Bustos, Ornella Lucchesi, María C. Ruete, Claudia N. Tomes. Membrane-permeable Rab27A is a regulator of the acrosome reaction: Role of geranylgeranylation and guanine nucleotidesCellular Signalling 2018; 44: 72 doi: 10.1016/j.cellsig.2018.01.010
6
Anjaneyulu Kowluru. Comprehensive Physiology2020; : 453 doi: 10.1002/cphy.c190028
7
Wen-feng Su, Yun Gu, Zhong-ya Wei, Yun-tian Shen, Zi-han Jin, Ying Yuan, Xiao-song Gu, Gang Chen. Rab27a/Slp2-a complex is involved in Schwann cell myelinationNeural Regeneration Research 2016; 11(11): 1830 doi: 10.4103/1673-5374.194755
8
Aml A. Alnaas, Abena Watson-Siriboe, Sherleen Tran, Mikias Negussie, Jack A. Henderson, J. Ryan Osterberg, Nara L. Chon, Beckston M. Harrott, Julianna Oviedo, Tatyana Lyakhova, Cole Michel, Nichole Reisdorph, Richard Reisdorph, Colin T. Shearn, Hai Lin, Jefferson D. Knight. Multivalent lipid targeting by the calcium-independent C2A domain of synaptotagmin-like protein 4/granuphilinJournal of Biological Chemistry 2021; 296: 100159 doi: 10.1074/jbc.RA120.014618
9
Mai E. Oguchi, Mitsunori Fukuda. Encyclopedia of Signaling Molecules2018; : 4378 doi: 10.1007/978-3-319-67199-4_101791
10
Mami Yamaoka, Tomomi Ando, Takeshi Terabayashi, Mitsuhiro Okamoto, Masahiro Takei, Tomoki Nishioka, Kozo Kaibuchi, Kohichi Matsunaga, Ray Ishizaki, Tetsuro Izumi, Ichiro Niki, Toshimasa Ishizaki, Toshihide Kimura. PI3K regulates endocytosis after insulin secretion by mediating signaling crosstalk between Arf6 and Rab27aJournal of Cell Science 2016; 129(3): 637 doi: 10.1242/jcs.180141
11
Toshihide Kimura, Mami Yamaoka, Takeshi Terabayashi, Kozo Kaibuchi, Tomohisa Ishikawa, Toshimasa Ishizaki. GDP-Bound Rab27a Dissociates from the Endocytic Machinery in a Phosphorylation-Dependent Manner after Insulin SecretionBiological and Pharmaceutical Bulletin 2019; 42(9): 1532 doi: 10.1248/bpb.b19-00242
12
Nara L. Chon, Sherleen Tran, Christopher S. Miller, Hai Lin, Jefferson D. Knight. A conserved electrostatic membrane‐binding surface in synaptotagmin‐like proteins revealed using molecular phylogenetic analysis and homology modelingProtein Science 2024; 33(1) doi: 10.1002/pro.4850
13
Mai E. Oguchi, Mitsunori Fukuda. Encyclopedia of Signaling Molecules2016; : 1 doi: 10.1007/978-1-4614-6438-9_101791-1