Ahammed KS, et al. (2025) Humanized Saccharomyces cerevisiae provides a facile and effective tool to identify damaging human variants that cause exosomopathies. G3 (Bethesda) PMID:39982806
Sad K, et al. (2025) Histone H3E50K remodels chromatin to confer oncogenic activity and support an EMT phenotype. NAR Cancer 7(1):zcaf002 PMID:39901931
Fasken MB, et al. (2024) A biallelic variant of the RNA exosome gene, EXOSC4, associated with neurodevelopmental defects impairs RNA exosome function and translation. J Biol Chem 300(8):107571 PMID:39009343
Corbett AH and Fasken MB (2023) Fellowship of two rings: Unprecedented insights into the structure of the yeast nuclear pore complex. Mol Cell 83(18):3232-3233 PMID:37738961
Sterrett MC, et al. (2023) In vivo characterization of the critical interaction between the RNA exosome and the essential RNA helicase Mtr4 in Saccharomyces cerevisiae. G3 (Bethesda) 13(8) PMID:36861343
Zhang X, et al. (2023) Exploring the Molecular Underpinnings of Cancer-Causing Oncohistone Mutants Using Yeast as a Model. J Fungi (Basel) 9(12) PMID:38132788
Ambrocio RE, et al. (2022) A Budding Yeast Model System to Define Biological Pathways Altered by Pathogenic Missense Mutations in Histone Genes Identifies a Link between Histone H3K36 and the TOS4 Gene. FASEB J 36 Suppl 1.
Lehner MH, et al. (2022) Yeast Smy2 and its human homologs GIGYF1 and -2 regulate Cdc48/VCP function during transcription stress. Cell Rep 41(4):111536 PMID:36288698
Lemon LD, et al. (2022) A Saccharomyces cerevisiae model and screen to define the functional consequences of oncogenic histone missense mutations. G3 (Bethesda) 12(7) PMID:35567477
Sterrett MC, et al. (2021) A budding yeast model for human disease mutations in the EXOSC2 cap subunit of the RNA exosome complex. RNA 27(9):1046-1067 PMID:34162742
Fasken MB, et al. (2019) Structure-function relationships in the Nab2 polyadenosine-RNA binding Zn finger protein family. Protein Sci 28(3):513-523 PMID:30578643
Fasken MB, et al. (2017) Insight into the RNA Exosome Complex Through Modeling Pontocerebellar Hypoplasia Type 1b Disease Mutations in Yeast. Genetics 205(1):221-237 PMID:27777260
Swartzlander DB, et al. (2016) Identification of SUMO modification sites in the base excision repair protein, Ntg1. DNA Repair (Amst) 48:51-62 PMID:27839712
Fasken MB, et al. (2015) Nab3 facilitates the function of the TRAMP complex in RNA processing via recruitment of Rrp6 independent of Nrd1. PLoS Genet 11(3):e1005044 PMID:25775092
Kelly SM, et al. (2014) A conserved role for the zinc finger polyadenosine RNA binding protein, ZC3H14, in control of poly(A) tail length. RNA 20(5):681-8 PMID:24671764
Bauer NC, et al. (2013) Automated quantification of the subcellular localization of multicompartment proteins via Q-SCAn. Traffic 14(12):1200-8 PMID:24034606
Brockmann C, et al. (2012) Structural basis for polyadenosine-RNA binding by Nab2 Zn fingers and its function in mRNA nuclear export. Structure 20(6):1007-18 PMID:22560733
Soucek S, et al. (2012) The long and the short of it: the role of the zinc finger polyadenosine RNA binding protein, Nab2, in control of poly(A) tail length. Biochim Biophys Acta 1819(6):546-54 PMID:22484098
Swartzlander DB, et al. (2012) Regulation of base excision repair in eukaryotes by dynamic localization strategies. Prog Mol Biol Transl Sci 110:93-121 PMID:22749144
Fasken MB, et al. (2011) Air1 zinc knuckles 4 and 5 and a conserved IWRXY motif are critical for the function and integrity of the Trf4/5-Air1/2-Mtr4 polyadenylation (TRAMP) RNA quality control complex. J Biol Chem 286(43):37429-45 PMID:21878619
Forwood JK, et al. (2010) Quantitative structural analysis of importin-β flexibility: paradigm for solenoid protein structures. Structure 18(9):1171-83 PMID:20826343
Kelly SM, et al. (2010) Recognition of polyadenosine RNA by the zinc finger domain of nuclear poly(A) RNA-binding protein 2 (Nab2) is required for correct mRNA 3'-end formation. J Biol Chem 285(34):26022-32 PMID:20554526
Swartzlander DB, et al. (2010) Regulation of base excision repair: Ntg1 nuclear and mitochondrial dynamic localization in response to genotoxic stress. Nucleic Acids Res 38(12):3963-74 PMID:20194111
Zheng C, et al. (2010) Structural basis for the function of the Saccharomyces cerevisiae Gfd1 protein in mRNA nuclear export. J Biol Chem 285(27):20704-15 PMID:20463024
Griffiths LM, et al. (2009) Dynamic compartmentalization of base excision repair proteins in response to nuclear and mitochondrial oxidative stress. Mol Cell Biol 29(3):794-807 PMID:19029246
Kitchen CM, et al. (2009) The mating response cascade does not modulate changes in the steady-state level of target mRNAs through control of mRNA stability. Yeast 26(5):261-72 PMID:19319831
Pulliam KF, et al. (2009) The classical nuclear localization signal receptor, importin-alpha, is required for efficient transition through the G1/S stage of the cell cycle in Saccharomyces cerevisiae. Genetics 181(1):105-18 PMID:18984568
Fasken MB, et al. (2008) Functional significance of the interaction between the mRNA-binding protein, Nab2, and the nuclear pore-associated protein, Mlp1, in mRNA export. J Biol Chem 283(40):27130-43 PMID:18682389
Grant RP, et al. (2008) Structure of the N-terminal Mlp1-binding domain of the Saccharomyces cerevisiae mRNA-binding protein, Nab2. J Mol Biol 376(4):1048-59 PMID:18190927
Lange A, et al. (2008) A PY-NLS nuclear targeting signal is required for nuclear localization and function of the Saccharomyces cerevisiae mRNA-binding protein Hrp1. J Biol Chem 283(19):12926-34 PMID:18343812
McLane LM, et al. (2008) The Ty1 integrase protein can exploit the classical nuclear protein import machinery for entry into the nucleus. Nucleic Acids Res 36(13):4317-26 PMID:18586821
Qiu H, et al. (2008) Identification of genes that function in the biogenesis and localization of small nucleolar RNAs in Saccharomyces cerevisiae. Mol Cell Biol 28(11):3686-99 PMID:18378690
Apponi LH, et al. (2007) An interaction between two RNA binding proteins, Nab2 and Pub1, links mRNA processing/export and mRNA stability. Mol Cell Biol 27(18):6569-79 PMID:17636033
Berger AC, et al. (2007) The subcellular localization of the Niemann-Pick Type C proteins depends on the adaptor complex AP-3. J Cell Sci 120(Pt 20):3640-52 PMID:17895371
Brykailo MA, et al. (2007) Analysis of a predicted nuclear localization signal: implications for the intracellular localization and function of the Saccharomyces cerevisiae RNA-binding protein Scp160. Nucleic Acids Res 35(20):6862-9 PMID:17933776
Brykailo MA, et al. (2007) Functional overlap between conserved and diverged KH domains in Saccharomyces cerevisiae SCP160. Nucleic Acids Res 35(4):1108-18 PMID:17264125
Luthra R, et al. (2007) Actively transcribed GAL genes can be physically linked to the nuclear pore by the SAGA chromatin modifying complex. J Biol Chem 282(5):3042-9 PMID:17158105
Tran EJ, et al. (2007) The DEAD-box protein Dbp5 controls mRNA export by triggering specific RNA:protein remodeling events. Mol Cell 28(5):850-9 PMID:18082609
Hodel AE, et al. (2006) Nuclear localization signal receptor affinity correlates with in vivo localization in Saccharomyces cerevisiae. J Biol Chem 281(33):23545-56 PMID:16785238
Zhao Q, et al. (2006) Identification and characterization of the Arabidopsis orthologs of nuclear transport factor 2, the nuclear import factor of ran. Plant Physiol 140(3):869-78 PMID:16428596
Baldwin EL, et al. (2005) Mms22p protects Saccharomyces cerevisiae from DNA damage induced by topoisomerase II. Nucleic Acids Res 33(3):1021-30 PMID:15718301
Berger AC, et al. (2005) Saccharomyces cerevisiae Npc2p is a functionally conserved homologue of the human Niemann-Pick disease type C 2 protein, hNPC2. Eukaryot Cell 4(11):1851-62 PMID:16278452
Berger AC, et al. (2005) A yeast model system for functional analysis of the Niemann-Pick type C protein 1 homolog, Ncr1p. Traffic 6(10):907-17 PMID:16138904
Harreman MT, et al. (2004) Regulation of nuclear import by phosphorylation adjacent to nuclear localization signals. J Biol Chem 279(20):20613-21 PMID:14998990
Li AM, et al. (2004) Both KH and non-KH domain sequences are required for polyribosome association of Scp160p in yeast. Nucleic Acids Res 32(16):4768-75 PMID:15356294
Green DM, et al. (2003) The C-terminal domain of myosin-like protein 1 (Mlp1p) is a docking site for heterogeneous nuclear ribonucleoproteins that are required for mRNA export. Proc Natl Acad Sci U S A 100(3):1010-5 PMID:12531921
Harreman MT, et al. (2003) Characterization of the auto-inhibitory sequence within the N-terminal domain of importin alpha. J Biol Chem 278(24):21361-9 PMID:12672802
Leung SW, et al. (2003) Dissection of the karyopherin alpha nuclear localization signal (NLS)-binding groove: functional requirements for NLS binding. J Biol Chem 278(43):41947-53 PMID:12917403
Marfatia KA, et al. (2003) Domain analysis of the Saccharomyces cerevisiae heterogeneous nuclear ribonucleoprotein, Nab2p. Dissecting the requirements for Nab2p-facilitated poly(A) RNA export. J Biol Chem 278(9):6731-40 PMID:12496292
Matsuura Y, et al. (2003) Structural basis for Nup2p function in cargo release and karyopherin recycling in nuclear import. EMBO J 22(20):5358-69 PMID:14532109
Narayanan A, et al. (2003) Nuclear RanGTP is not required for targeting small nucleolar RNAs to the nucleolus. J Cell Sci 116(Pt 1):177-86 PMID:12456727
Green DM, et al. (2002) Nab2p is required for poly(A) RNA export in Saccharomyces cerevisiae and is regulated by arginine methylation via Hmt1p. J Biol Chem 277(10):7752-60 PMID:11779864
Miyamoto Y, et al. (2002) Importin alpha can migrate into the nucleus in an importin beta- and Ran-independent manner. EMBO J 21(21):5833-42 PMID:12411501
Akhtar N, et al. (2001) Functional analysis of the yeast Ran exchange factor Prp20p: in vivo evidence for the RanGTP gradient model. Mol Genet Genomics 265(5):851-64 PMID:11523802
Quimby BB, et al. (2001) Functional analysis of the hydrophobic patch on nuclear transport factor 2 involved in interactions with the nuclear pore in vivo. J Biol Chem 276(42):38820-9 PMID:11489893
Wei H, et al. (2001) Carboxymethylation of the PP2A catalytic subunit in Saccharomyces cerevisiae is required for efficient interaction with the B-type subunits Cdc55p and Rts1p. J Biol Chem 276(2):1570-7 PMID:11038366
Akhtar N, et al. (2000) SGD1 encodes an essential nuclear protein of Saccharomyces cerevisiae that affects expression of the GPD1 gene for glycerol 3-phosphate dehydrogenase. FEBS Lett 483(2-3):87-92 PMID:11042259
Bayliss R, et al. (2000) Crystallization and initial X-ray diffraction characterization of complexes of FxFG nucleoporin repeats with nuclear transport factors. J Struct Biol 131(3):240-7 PMID:11052897
Fanara P, et al. (2000) Quantitative analysis of nuclear localization signal (NLS)-importin alpha interaction through fluorescence depolarization. Evidence for auto-inhibitory regulation of NLS binding. J Biol Chem 275(28):21218-23 PMID:10806202
Kent HM, et al. (1999) Engineered mutants in the switch II loop of Ran define the contribution made by key residues to the interaction with nuclear transport factor 2 (NTF2) and the role of this interaction in nuclear protein import. J Mol Biol 289(3):565-77 PMID:10356329
You HJ, et al. (1999) Saccharomyces cerevisiae Ntg1p and Ntg2p: broad specificity N-glycosylases for the repair of oxidative DNA damage in the nucleus and mitochondria. Biochemistry 38(35):11298-306 PMID:10471279
Clarkson WD, et al. (1997) Nuclear protein import is decreased by engineered mutants of nuclear transport factor 2 (NTF2) that do not bind GDP-Ran. J Mol Biol 272(5):716-30 PMID:9368653
Wong DH, et al. (1997) Interaction between the small GTPase Ran/Gsp1p and Ntf2p is required for nuclear transport. Mol Cell Biol 17(7):3755-67 PMID:9199309
Corbett AH and Silver PA (1996) The NTF2 gene encodes an essential, highly conserved protein that functions in nuclear transport in vivo. J Biol Chem 271(31):18477-84 PMID:8702493
Koepp DM, et al. (1996) Dynamic localization of the nuclear import receptor and its interactions with transport factors. J Cell Biol 133(6):1163-76 PMID:8682856