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Volumn 41, Issue 4, 2016, Pages 338-355

The Chemical Biology of Human Metallo-β-Lactamase Fold Proteins

Author keywords

DNA repair; hydrogen sulphide metabolism; metallo lactamase fold protein; nuclease; RNA processing; lactam antibiotic and cancer drug resistance

Indexed keywords

ANTINEOPLASTIC AGENT; BETA LACTAM ANTIBIOTIC; CISPLATIN; CMAH PROTEIN; CPSF73 PROTEIN; ETHE1 PROTEIN; HYDROXYACYLGLUTATHIONE HYDROLASE; METALLO BETA LACTAMASE; MITOMYCIN; NAPE PLD PROTEIN; NUCLEASE; OXYGENASE; PHOSPHOLIPASE D; UNCLASSIFIED DRUG; ZINC ION; BETA LACTAM; BETA LACTAMASE; DCLRE1B PROTEIN, HUMAN; DNA LIGASE; ETHE1 PROTEIN, HUMAN; MITOCHONDRIAL PROTEIN; MUSCLE PROTEIN; NUCLEAR PROTEIN; NUCLEOCYTOPLASMIC TRANSPORT PROTEIN; PNKD PROTEIN, HUMAN; PROTEIN BINDING; THIOL ESTER HYDROLASE; ZINC;

EID: 84955494576     PISSN: 09680004     EISSN: 13624326     Source Type: Journal    
DOI: 10.1016/j.tibs.2015.12.007     Document Type: Review
Times cited : (89)

References (118)
  • 1
    • 80053247739 scopus 로고    scopus 로고
    • Epidemiological expansion, structural studies, and clinical challenges of new β-lactamases from gram-negative bacteria
    • Bush, K., Fisher, J.F., Epidemiological expansion, structural studies, and clinical challenges of new β-lactamases from gram-negative bacteria. Annu. Rev. Microbiol. 65 (2011), 455–478.
    • (2011) Annu. Rev. Microbiol. , vol.65 , pp. 455-478
    • Bush, K.1    Fisher, J.F.2
  • 2
    • 79955453026 scopus 로고    scopus 로고
    • Metallo-β-lacatamases: a last frontier for β-lactams?
    • Cornaglia, G., et al. Metallo-β-lacatamases: a last frontier for β-lactams?. Lancet Infect. Dis. 11 (2011), 381–393.
    • (2011) Lancet Infect. Dis. , vol.11 , pp. 381-393
    • Cornaglia, G.1
  • 3
    • 84872858103 scopus 로고    scopus 로고
    • Proliferation and significance of clinically relevant beta-lactamases
    • Bush, K., Proliferation and significance of clinically relevant beta-lactamases. Ann. N. Y. Acad. Sci. 1277 (2013), 84–90.
    • (2013) Ann. N. Y. Acad. Sci. , vol.1277 , pp. 84-90
    • Bush, K.1
  • 4
    • 84896968084 scopus 로고    scopus 로고
    • New β-lactamase inhibitors: a therapeutic renaissance in an MDR world
    • Drawz, S.M., et al. New β-lactamase inhibitors: a therapeutic renaissance in an MDR world. Antimicrob. Agents Chemother. 58 (2014), 1835–1846.
    • (2014) Antimicrob. Agents Chemother. , vol.58 , pp. 1835-1846
    • Drawz, S.M.1
  • 5
    • 0028810769 scopus 로고
    • The 3-D structure of a zinc metallo-β-lactamase from Bacillus cereus reveals a new type of protein fold
    • Carfi, A., et al. The 3-D structure of a zinc metallo-β-lactamase from Bacillus cereus reveals a new type of protein fold. EMBO J. 14 (1995), 4914–4921.
    • (1995) EMBO J. , vol.14 , pp. 4914-4921
    • Carfi, A.1
  • 6
    • 33750624074 scopus 로고    scopus 로고
    • Metallo-beta-lactamases: novel weaponry for antibiotic resistance in bacteria
    • Crowder, M.W., et al. Metallo-beta-lactamases: novel weaponry for antibiotic resistance in bacteria. Acc. Chem. Res. 39 (2006), 721–728.
    • (2006) Acc. Chem. Res. , vol.39 , pp. 721-728
    • Crowder, M.W.1
  • 7
    • 34948859355 scopus 로고    scopus 로고
    • Metallo-β-lactamases (classification, activity, genetic organization, structure, zinc coordination) and their superfamily
    • Bebrone, C., Metallo-β-lactamases (classification, activity, genetic organization, structure, zinc coordination) and their superfamily. Biochem. Pharmacol. 74 (2007), 1686–1701.
    • (2007) Biochem. Pharmacol. , vol.74 , pp. 1686-1701
    • Bebrone, C.1
  • 8
    • 0035839131 scopus 로고    scopus 로고
    • Expansion of the zinc metallo-hydrolase family of the beta-lactamase fold
    • Daiyasu, H., et al. Expansion of the zinc metallo-hydrolase family of the beta-lactamase fold. FEBS Lett. 503 (2001), 1–6.
    • (2001) FEBS Lett. , vol.503 , pp. 1-6
    • Daiyasu, H.1
  • 9
    • 84901807720 scopus 로고    scopus 로고
    • Connectivity between catalytic landscapes of the metallo-β-lactamase superfamily
    • Baier, F., Tokuriki, N., Connectivity between catalytic landscapes of the metallo-β-lactamase superfamily. J. Mol. Biol. 426 (2014), 2442–2456.
    • (2014) J. Mol. Biol. , vol.426 , pp. 2442-2456
    • Baier, F.1    Tokuriki, N.2
  • 10
    • 84871786683 scopus 로고    scopus 로고
    • Characterization of patient mutations in human persulfide dioxygenase (ETHE1) involved in H2S catabolism
    • Kabil, O., Banerjee, R., Characterization of patient mutations in human persulfide dioxygenase (ETHE1) involved in H2S catabolism. J. Biol. Chem. 287 (2012), 44561–44567.
    • (2012) J. Biol. Chem. , vol.287 , pp. 44561-44567
    • Kabil, O.1    Banerjee, R.2
  • 11
    • 10044250110 scopus 로고    scopus 로고
    • DNA cross-link repair protein SNM1A interacts with PIAS1 in nuclear focus formation
    • Ishiai, M., et al. DNA cross-link repair protein SNM1A interacts with PIAS1 in nuclear focus formation. Mol. Cell. Biol. 24 (2004), 10733–10741.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 10733-10741
    • Ishiai, M.1
  • 12
    • 3042753332 scopus 로고    scopus 로고
    • The binding of iron and zinc to glyoxalase II occurs exclusively as di-metal centers and is unique within the metallo-beta-lactamase family
    • Wenzel, N.F., et al. The binding of iron and zinc to glyoxalase II occurs exclusively as di-metal centers and is unique within the metallo-beta-lactamase family. J. Biol. Inorg. Chem. 9 (2004), 429–438.
    • (2004) J. Biol. Inorg. Chem. , vol.9 , pp. 429-438
    • Wenzel, N.F.1
  • 13
    • 79955952814 scopus 로고    scopus 로고
    • Glyoxalase in ageing
    • Xue, M., et al. Glyoxalase in ageing. Semin. Cell. Dev. Biol. 22 (2011), 293–301.
    • (2011) Semin. Cell. Dev. Biol. , vol.22 , pp. 293-301
    • Xue, M.1
  • 14
    • 0030027452 scopus 로고    scopus 로고
    • Molecular cloning, heterologous expression, and characterization of human glyoxalase II
    • Ridderström, M., et al. Molecular cloning, heterologous expression, and characterization of human glyoxalase II. J. Biol. Chem. 271 (1996), 319–323.
    • (1996) J. Biol. Chem. , vol.271 , pp. 319-323
    • Ridderström, M.1
  • 15
    • 0030608678 scopus 로고    scopus 로고
    • Glyoxalase II from A. thaliana requires Zn (II) for catalytic activity
    • Crowder, M.W., et al. Glyoxalase II from A. thaliana requires Zn (II) for catalytic activity. FEBS Lett. 418 (1997), 351–354.
    • (1997) FEBS Lett. , vol.418 , pp. 351-354
    • Crowder, M.W.1
  • 16
    • 0033200323 scopus 로고    scopus 로고
    • Crystal structure of human glyoxalase II and its complex with a glutathione thiolester substrate analogue
    • Cameron, A.D., et al. Crystal structure of human glyoxalase II and its complex with a glutathione thiolester substrate analogue. Structure 7 (1999), 1067–1078.
    • (1999) Structure , vol.7 , pp. 1067-1078
    • Cameron, A.D.1
  • 17
    • 0141928715 scopus 로고    scopus 로고
    • Flexible metal binding of the metallo-beta-lactamase domain: glyoxalase II incorporates iron, manganese, and zinc in vivo
    • Schilling, O., et al. Flexible metal binding of the metallo-beta-lactamase domain: glyoxalase II incorporates iron, manganese, and zinc in vivo. Biochem. 42 (2003), 11777–11786.
    • (2003) Biochem. , vol.42 , pp. 11777-11786
    • Schilling, O.1
  • 18
    • 84879067434 scopus 로고    scopus 로고
    • Metallo-β-lactamase: inhibitors and reporter substrates
    • Fast, W., Sutton, L.D., Metallo-β-lactamase: inhibitors and reporter substrates. Biochim. Biophys. Acta 1834 (2013), 1648–1659.
    • (2013) Biochim. Biophys. Acta , vol.1834 , pp. 1648-1659
    • Fast, W.1    Sutton, L.D.2
  • 19
    • 45449088355 scopus 로고    scopus 로고
    • Structural basis for the broad-spectrum inhibition of metallo-β-lactamases by thiols
    • Liénard, B.M.R., et al. Structural basis for the broad-spectrum inhibition of metallo-β-lactamases by thiols. Org. Biomol. Chem. 6 (2008), 2282–2294.
    • (2008) Org. Biomol. Chem. , vol.6 , pp. 2282-2294
    • Liénard, B.M.R.1
  • 20
    • 10744232283 scopus 로고    scopus 로고
    • Ethylmalonic encephalopathy is caused by mutations in ETHE1, a gene encoding a mitochondrial matrix protein
    • Tiranti, V., et al. Ethylmalonic encephalopathy is caused by mutations in ETHE1, a gene encoding a mitochondrial matrix protein. Am. J. Hum. Genet. 74 (2004), 239–252.
    • (2004) Am. J. Hum. Genet. , vol.74 , pp. 239-252
    • Tiranti, V.1
  • 21
    • 33645758448 scopus 로고    scopus 로고
    • ETHE1 mutations are specific to ethylmalonic encephalopathy
    • Tiranti, V., et al. ETHE1 mutations are specific to ethylmalonic encephalopathy. J. Med. Genet. 43 (2006), 340–346.
    • (2006) J. Med. Genet. , vol.43 , pp. 340-346
    • Tiranti, V.1
  • 22
    • 59649121556 scopus 로고    scopus 로고
    • Loss of ETHE1, a mitochondrial dioxygenase, causes fatal sulfide toxicity in ethylmalonic encephalopathy
    • Tiranti, V., et al. Loss of ETHE1, a mitochondrial dioxygenase, causes fatal sulfide toxicity in ethylmalonic encephalopathy. Nat. Med. 15 (2009), 200–205.
    • (2009) Nat. Med. , vol.15 , pp. 200-205
    • Tiranti, V.1
  • 23
    • 84911915073 scopus 로고    scopus 로고
    • Ethylmalonic encephalopathy ETHE1 R163W/R163Q mutations alter protein stability and redox properties of the iron centre
    • Henriques, B.J., et al. Ethylmalonic encephalopathy ETHE1 R163W/R163Q mutations alter protein stability and redox properties of the iron centre. PLoS ONE, 9, 2014, e107157.
    • (2014) PLoS ONE , vol.9 , pp. e107157
    • Henriques, B.J.1
  • 24
    • 33645758448 scopus 로고    scopus 로고
    • ETHE1 mutations are specific to ethylmalonic encephalopathy
    • Tiranti, V., et al. ETHE1 mutations are specific to ethylmalonic encephalopathy. J. Med. Genet. 43 (2005), 340–346.
    • (2005) J. Med. Genet. , vol.43 , pp. 340-346
    • Tiranti, V.1
  • 25
    • 47149107953 scopus 로고    scopus 로고
    • Identification of new mutations in the ETHE1 gene in a cohort of 14 patients presenting with ethylmalonic encephalopathy
    • Mineri, R., et al. Identification of new mutations in the ETHE1 gene in a cohort of 14 patients presenting with ethylmalonic encephalopathy. J. Med. Genet. 45 (2008), 473–478.
    • (2008) J. Med. Genet. , vol.45 , pp. 473-478
    • Mineri, R.1
  • 26
    • 0036782443 scopus 로고    scopus 로고
    • A novel protein overexpressed in hepatoma accelerates export of NF-κB from the nucleus and inhibits p53-dependent apoptosis
    • Higashitsuji, H., et al. A novel protein overexpressed in hepatoma accelerates export of NF-κB from the nucleus and inhibits p53-dependent apoptosis. Cancer Cell 2 (2002), 335–346.
    • (2002) Cancer Cell , vol.2 , pp. 335-346
    • Higashitsuji, H.1
  • 27
    • 34250357227 scopus 로고    scopus 로고
    • Enhanced deacetylation of p53 by the anti-apoptotic protein HSCO in association with histone deacetylase 1
    • Higashitsuji, H., et al. Enhanced deacetylation of p53 by the anti-apoptotic protein HSCO in association with histone deacetylase 1. J. Biol. Chem. 282 (2007), 13716–13725.
    • (2007) J. Biol. Chem. , vol.282 , pp. 13716-13725
    • Higashitsuji, H.1
  • 28
    • 27744496468 scopus 로고    scopus 로고
    • Non-hydroxamate histone deacetylase inhibitors
    • Suzuki, T., Miyata, N., Non-hydroxamate histone deacetylase inhibitors. Curr. Med. Chem. 12 (2005), 2867–2880.
    • (2005) Curr. Med. Chem. , vol.12 , pp. 2867-2880
    • Suzuki, T.1    Miyata, N.2
  • 29
    • 33748339794 scopus 로고    scopus 로고
    • Structure of an ETHE1-like protein from Arabidopsis thaliana
    • McCoy, J.G., et al. Structure of an ETHE1-like protein from Arabidopsis thaliana. Acta. Crystallogr. D Biol. Crystallogr. 62 (2006), 964–970.
    • (2006) Acta. Crystallogr. D Biol. Crystallogr. , vol.62 , pp. 964-970
    • McCoy, J.G.1
  • 30
    • 84937831776 scopus 로고    scopus 로고
    • Crystal structure of human persulfide dioxygenase: structural basis of ethylmalonic encephalopathy
    • Pettinati, I., et al. Crystal structure of human persulfide dioxygenase: structural basis of ethylmalonic encephalopathy. Hum. Mol. Genet. 24 (2015), 2458–2469.
    • (2015) Hum. Mol. Genet. , vol.24 , pp. 2458-2469
    • Pettinati, I.1
  • 31
    • 84870883696 scopus 로고    scopus 로고
    • The enzymes of β-lactam biosynthesis
    • Hamed, R.B., et al. The enzymes of β-lactam biosynthesis. Nat. Prod. Rep. 30 (2013), 21–107.
    • (2013) Nat. Prod. Rep. , vol.30 , pp. 21-107
    • Hamed, R.B.1
  • 32
    • 19944407549 scopus 로고    scopus 로고
    • The gene for paroxysmal non-kinesigenic dyskinesia encodes an enzyme in a stress response pathway
    • Lee, H.Y., The gene for paroxysmal non-kinesigenic dyskinesia encodes an enzyme in a stress response pathway. Hum. Mol. Genet. 13 (2004), 3161–3170.
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 3161-3170
    • Lee, H.Y.1
  • 33
    • 3142721995 scopus 로고    scopus 로고
    • Myofibrillogenesis regulator 1 gene mutations cause paroxysmal dystonic choreoathetosis
    • Rainier, S., et al. Myofibrillogenesis regulator 1 gene mutations cause paroxysmal dystonic choreoathetosis. Arch. Neurol. 61 (2004), 1025–1029.
    • (2004) Arch. Neurol. , vol.61 , pp. 1025-1029
    • Rainier, S.1
  • 34
    • 79957489941 scopus 로고    scopus 로고
    • Mutations in PNKD causing paroxysmal dyskinesia alters protein cleavage and stability
    • Shen, Y., et al. Mutations in PNKD causing paroxysmal dyskinesia alters protein cleavage and stability. Hum. Mol. Genet. 20 (2011), 2322–2332.
    • (2011) Hum. Mol. Genet. , vol.20 , pp. 2322-2332
    • Shen, Y.1
  • 35
    • 84655169098 scopus 로고    scopus 로고
    • Paroxysmal non-kinesigenic dyskinesia due to a PNKD recurrent mutation: report of two Southern European families
    • Pons, R., Paroxysmal non-kinesigenic dyskinesia due to a PNKD recurrent mutation: report of two Southern European families. Eur. J. Paediatr. Neurol. 16 (2012), 86–89.
    • (2012) Eur. J. Paediatr. Neurol. , vol.16 , pp. 86-89
    • Pons, R.1
  • 36
    • 84863011960 scopus 로고    scopus 로고
    • Dopamine dysregulation in a mouse model of paroxysmal nonkinesigenic dyskinesia
    • Lee, H.Y., et al. Dopamine dysregulation in a mouse model of paroxysmal nonkinesigenic dyskinesia. J. Clin. Invest. 122 (2012), 507–518.
    • (2012) J. Clin. Invest. , vol.122 , pp. 507-518
    • Lee, H.Y.1
  • 37
    • 34247480145 scopus 로고    scopus 로고
    • D1 and D2 dopamine-receptor modulation of striatal glutamatergic signaling in striatal medium spiny neurons
    • Surmeier, D.J., et al. D1 and D2 dopamine-receptor modulation of striatal glutamatergic signaling in striatal medium spiny neurons. Trends Neurosci. 30 (2007), 228–235.
    • (2007) Trends Neurosci. , vol.30 , pp. 228-235
    • Surmeier, D.J.1
  • 38
    • 0242583853 scopus 로고    scopus 로고
    • The endocannabinoid system in the basal ganglia and in the mesolimbic reward system: implications for neurological and psychiatric disorders
    • van der Stelt, M., Di Marzo, V., The endocannabinoid system in the basal ganglia and in the mesolimbic reward system: implications for neurological and psychiatric disorders. Eur. J. Pharmacol. 480 (2003), 133–150.
    • (2003) Eur. J. Pharmacol. , vol.480 , pp. 133-150
    • van der Stelt, M.1    Di Marzo, V.2
  • 39
    • 56349143278 scopus 로고    scopus 로고
    • Striatal plasticity and basal ganglia circuit function
    • Kreitzer, A.C., Malenka, R.C., Striatal plasticity and basal ganglia circuit function. Neuron 60 (2008), 543–554.
    • (2008) Neuron , vol.60 , pp. 543-554
    • Kreitzer, A.C.1    Malenka, R.C.2
  • 40
    • 4143150897 scopus 로고    scopus 로고
    • Characterization of MR-1, a novel myofibrillogenesis regulator in human muscle
    • Li, T.B., et al. Characterization of MR-1, a novel myofibrillogenesis regulator in human muscle. Acta Biochim. Biophys. Sin. (Shanghai) 36 (2004), 412–418.
    • (2004) Acta Biochim. Biophys. Sin. (Shanghai) , vol.36 , pp. 412-418
    • Li, T.B.1
  • 41
    • 58149090237 scopus 로고    scopus 로고
    • MR-1 modulates proliferation and migration of human hepatoma HepG2 cells through myosin light chains-2(MLC2)/focal adhesion kinase (FAK)/Akt signaling pathway
    • Ren, K., et al. MR-1 modulates proliferation and migration of human hepatoma HepG2 cells through myosin light chains-2(MLC2)/focal adhesion kinase (FAK)/Akt signaling pathway. J. Biol. Chem. 283 (2008), 35598–35605.
    • (2008) J. Biol. Chem. , vol.283 , pp. 35598-35605
    • Ren, K.1
  • 42
    • 79959391005 scopus 로고    scopus 로고
    • Myofibrillogenesis regulator 1 (MR-1) is a novel biomarker and potential therapeutic target for human ovarian cancer
    • Lu, R., et al. Myofibrillogenesis regulator 1 (MR-1) is a novel biomarker and potential therapeutic target for human ovarian cancer. BMC Cancer, 11, 2011, 270.
    • (2011) BMC Cancer , vol.11 , pp. 270
    • Lu, R.1
  • 43
    • 34247157802 scopus 로고    scopus 로고
    • Nucleases of the metallo-beta-lactamase family and their role in DNA and RNA metabolism
    • Dominski, Z., Nucleases of the metallo-beta-lactamase family and their role in DNA and RNA metabolism. Crit. Rev. Biochem. Mol. Biol. 42 (2007), 67–93.
    • (2007) Crit. Rev. Biochem. Mol. Biol. , vol.42 , pp. 67-93
    • Dominski, Z.1
  • 44
    • 0033105094 scopus 로고    scopus 로고
    • Conserved domains in DNA repair proteins and evolution of repair systems
    • Aravind, L., et al. Conserved domains in DNA repair proteins and evolution of repair systems. Nuc. Acids Res. 27 (1999), 1223–1242.
    • (1999) Nuc. Acids Res. , vol.27 , pp. 1223-1242
    • Aravind, L.1
  • 45
    • 0037102538 scopus 로고    scopus 로고
    • Metallo-β-lactamase fold within nucleic acids processing enzymes: the beta-CASP family
    • Callebaut, I., et al. Metallo-β-lactamase fold within nucleic acids processing enzymes: the beta-CASP family. Nuc. Acid Res. 30 (2002), 3592–3601.
    • (2002) Nuc. Acid Res. , vol.30 , pp. 3592-3601
    • Callebaut, I.1
  • 46
    • 84887613990 scopus 로고    scopus 로고
    • New features on Pso2 protein family in DNA interstrand cross-link repair 4 and in the maintenance of genomic integrity in Saccharomyces cerevisiae
    • Munari, F.M., et al. New features on Pso2 protein family in DNA interstrand cross-link repair 4 and in the maintenance of genomic integrity in Saccharomyces cerevisiae. Fungal Genet. Biol. 60 (2013), 122–132.
    • (2013) Fungal Genet. Biol. , vol.60 , pp. 122-132
    • Munari, F.M.1
  • 47
    • 77957273635 scopus 로고    scopus 로고
    • The multifunctional SNM1 gene family: not just nucleases
    • Yan, Y., et al. The multifunctional SNM1 gene family: not just nucleases. Future Oncol. 6 (2011), 1015–1029.
    • (2011) Future Oncol. , vol.6 , pp. 1015-1029
    • Yan, Y.1
  • 48
    • 84864389189 scopus 로고    scopus 로고
    • Characterisation of the human SNM1A and SNM1B/Apollo DNA repair exonucleases
    • Sengerova, B., et al. Characterisation of the human SNM1A and SNM1B/Apollo DNA repair exonucleases. J. Biol. Chem. 287 (2012), 26254–26267.
    • (2012) J. Biol. Chem. , vol.287 , pp. 26254-26267
    • Sengerova, B.1
  • 49
    • 37549001012 scopus 로고    scopus 로고
    • Human SNM1A suppresses the DNA repair defects of yeast Pso2 mutants
    • Hazrati, A., et al. Human SNM1A suppresses the DNA repair defects of yeast Pso2 mutants. DNA Repair (Amst). 7 (2008), 230–238.
    • (2008) DNA Repair (Amst). , vol.7 , pp. 230-238
    • Hazrati, A.1
  • 50
    • 77954958609 scopus 로고    scopus 로고
    • TRF2 and apollo cooperate with topoisomerase 2alpha to protect human telomeres from replicative damage
    • Ye, J., et al. TRF2 and apollo cooperate with topoisomerase 2alpha to protect human telomeres from replicative damage. Cell 142 (2010), 230–242.
    • (2010) Cell , vol.142 , pp. 230-242
    • Ye, J.1
  • 51
    • 80052440005 scopus 로고    scopus 로고
    • Human SNM1A and XPF-ERCC1 collaborate to initiate DNA interstrand cross-link repair
    • Wang, A.T., et al. Human SNM1A and XPF-ERCC1 collaborate to initiate DNA interstrand cross-link repair. Genes Dev. 25 (2011), 1859–1870.
    • (2011) Genes Dev. , vol.25 , pp. 1859-1870
    • Wang, A.T.1
  • 52
    • 54449088816 scopus 로고    scopus 로고
    • SNM1A acts downstream of ATM to promote the G1 cell cycle checkpoint
    • Akhter, S., Legerski, R.J., SNM1A acts downstream of ATM to promote the G1 cell cycle checkpoint. Biochem. Biophys. Res. Commun. 377 (2008), 236–241.
    • (2008) Biochem. Biophys. Res. Commun. , vol.377 , pp. 236-241
    • Akhter, S.1    Legerski, R.J.2
  • 53
    • 77954958459 scopus 로고    scopus 로고
    • SNM1B/Apollo protects leading-strand telomeres against NHEJ-mediated repair
    • Lam, Y.C., et al. SNM1B/Apollo protects leading-strand telomeres against NHEJ-mediated repair. EMBO J. 29 (2010), 2230–2241.
    • (2010) EMBO J. , vol.29 , pp. 2230-2241
    • Lam, Y.C.1
  • 54
    • 50649091340 scopus 로고    scopus 로고
    • Snm1B/Apollo mediates replication fork collapse and S Phase checkpoint activation in response to DNA interstrand cross-links
    • Bae, J.B., et al. Snm1B/Apollo mediates replication fork collapse and S Phase checkpoint activation in response to DNA interstrand cross-links. Oncogene 27 (2008), 5045–5056.
    • (2008) Oncogene , vol.27 , pp. 5045-5056
    • Bae, J.B.1
  • 55
    • 9644301156 scopus 로고    scopus 로고
    • Human SNM1B is required for normal cellular response to both DNA interstrand crosslink-inducing agents and ionizing radiation
    • Demuth, I., et al. Human SNM1B is required for normal cellular response to both DNA interstrand crosslink-inducing agents and ionizing radiation. Oncogene 23 (2004), 8611–8618.
    • (2004) Oncogene , vol.23 , pp. 8611-8618
    • Demuth, I.1
  • 56
    • 79958702602 scopus 로고    scopus 로고
    • Snm1B/Apollo functions in the Fanconi anemia pathway in response to DNA interstrand crosslinks
    • Mason, J.M., Sekiguchi, M.J., Snm1B/Apollo functions in the Fanconi anemia pathway in response to DNA interstrand crosslinks. Hum. Mol. Genet. 20 (2011), 2549–2559.
    • (2011) Hum. Mol. Genet. , vol.20 , pp. 2549-2559
    • Mason, J.M.1    Sekiguchi, M.J.2
  • 57
    • 0034162828 scopus 로고    scopus 로고
    • A new gene involved in DNA double-strand break repair and V(D)J recombination is located on human chromosome 10p
    • Moshous, D., et al. A new gene involved in DNA double-strand break repair and V(D)J recombination is located on human chromosome 10p. Hum. Mol. Genet. 9 (2000), 583–588.
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 583-588
    • Moshous, D.1
  • 58
    • 84896289647 scopus 로고    scopus 로고
    • Evidence that the DNA endonuclease ARTEMIS also has intrinsic 5′-exonuclease activity
    • Li, S., et al. Evidence that the DNA endonuclease ARTEMIS also has intrinsic 5′-exonuclease activity. J. Biol. Chem. 289 (2014), 7825–7834.
    • (2014) J. Biol. Chem. , vol.289 , pp. 7825-7834
    • Li, S.1
  • 59
    • 0037155703 scopus 로고    scopus 로고
    • Hairpin opening and overhang processing by an Artemis/DNA-dependent protein kinase complex in nonhomologous end joining and V(D)J recombination
    • Ma, Y., et al. Hairpin opening and overhang processing by an Artemis/DNA-dependent protein kinase complex in nonhomologous end joining and V(D)J recombination. Cell 108 (2002), 781–794.
    • (2002) Cell , vol.108 , pp. 781-794
    • Ma, Y.1
  • 60
    • 84871686867 scopus 로고    scopus 로고
    • Structural basis of DNA ligase IV-Artemis interaction in nonhomologous end-joining
    • De Ioannes, P., et al. Structural basis of DNA ligase IV-Artemis interaction in nonhomologous end-joining. Cell Rep. 2 (2012), 1505–1512.
    • (2012) Cell Rep. , vol.2 , pp. 1505-1512
    • De Ioannes, P.1
  • 61
    • 82855181506 scopus 로고    scopus 로고
    • Artemis interacts with the Cul4A-DDB1DDB2 ubiquitin E3 ligase and regulates degradation of the CDK inhibitor p27
    • Yan, Y., et al. Artemis interacts with the Cul4A-DDB1DDB2 ubiquitin E3 ligase and regulates degradation of the CDK inhibitor p27. Cell Cycle 10 (2011), 4098–4109.
    • (2011) Cell Cycle , vol.10 , pp. 4098-4109
    • Yan, Y.1
  • 62
    • 29044449835 scopus 로고    scopus 로고
    • The tRNase Z family of proteins: physiological functions, substrate specificity and structural properties
    • Vogel, A., et al. The tRNase Z family of proteins: physiological functions, substrate specificity and structural properties. Biol. Chem. 386 (2005), 1253–1264.
    • (2005) Biol. Chem. , vol.386 , pp. 1253-1264
    • Vogel, A.1
  • 63
    • 46749129676 scopus 로고    scopus 로고
    • Regulation of the human tRNA Zs gene expression
    • Takahashi, M., et al. Regulation of the human tRNA Zs gene expression. FEBS Lett. 582 (2008), 2532–2536.
    • (2008) FEBS Lett. , vol.582 , pp. 2532-2536
    • Takahashi, M.1
  • 64
    • 84897527933 scopus 로고    scopus 로고
    • Initial steps in RNA processing and ribosome assembly occur at mitochondrial DNA nucleoids
    • Bogenhagen, D.F., et al. Initial steps in RNA processing and ribosome assembly occur at mitochondrial DNA nucleoids. Cell Metab. 19 (2014), 618–629.
    • (2014) Cell Metab. , vol.19 , pp. 618-629
    • Bogenhagen, D.F.1
  • 65
    • 85046980054 scopus 로고    scopus 로고
    • Involvement of human ELAC2 gene product in 3′ end processing of mitochondrial tRNAs
    • Brzezniak, L.K., et al. Involvement of human ELAC2 gene product in 3′ end processing of mitochondrial tRNAs. RNA Biol. 8 (2011), 616–626.
    • (2011) RNA Biol. , vol.8 , pp. 616-626
    • Brzezniak, L.K.1
  • 66
    • 84881663733 scopus 로고    scopus 로고
    • ELAC2 mutations cause a mitochondrial RNA processing defect associated with hypertrophic cardiomyopathy
    • Haack, T.B., et al. ELAC2 mutations cause a mitochondrial RNA processing defect associated with hypertrophic cardiomyopathy. Am. J. Hum. Genet. 93 (2013), 211–223.
    • (2013) Am. J. Hum. Genet. , vol.93 , pp. 211-223
    • Haack, T.B.1
  • 67
    • 0037013852 scopus 로고    scopus 로고
    • Assigning a function to a conserved group of proteins: the tRNA 3′- processing enzymes
    • Schiffer, S., et al. Assigning a function to a conserved group of proteins: the tRNA 3′- processing enzymes. EMBO J. 21 (2002), 2769–2777.
    • (2002) EMBO J. , vol.21 , pp. 2769-2777
    • Schiffer, S.1
  • 68
    • 79955716664 scopus 로고    scopus 로고
    • Localization of human RNase Z isoforms: dual nuclear/mitochondrial targeting of the ELAC2 gene product by alternative translation initiation
    • Rossmanith, W., Localization of human RNase Z isoforms: dual nuclear/mitochondrial targeting of the ELAC2 gene product by alternative translation initiation. PLoS ONE, 6, 2011, 19152.
    • (2011) PLoS ONE , vol.6 , pp. 19152
    • Rossmanith, W.1
  • 69
    • 0035135523 scopus 로고    scopus 로고
    • A candidate prostate cancer susceptibility gene at chromosome 17p
    • Tavtigian, S.V., et al. A candidate prostate cancer susceptibility gene at chromosome 17p. Nat. Genet. 27 (2001), 172–180.
    • (2001) Nat. Genet. , vol.27 , pp. 172-180
    • Tavtigian, S.V.1
  • 70
    • 0038750928 scopus 로고    scopus 로고
    • A candidate prostate cancer susceptibility gene encodes tRNA 3′ processing endoribonuclease
    • Takaku, H., et al. A candidate prostate cancer susceptibility gene encodes tRNA 3′ processing endoribonuclease. Nuc. Acids Res. 31 (2003), 2272–2278.
    • (2003) Nuc. Acids Res. , vol.31 , pp. 2272-2278
    • Takaku, H.1
  • 71
    • 84945127819 scopus 로고    scopus 로고
    • Prognostic role of genetic biomarkers in clinical progression of prostate cancer
    • Alvarez-Cubero, M.J., et al. Prognostic role of genetic biomarkers in clinical progression of prostate cancer. Exp. Mol. Med., 47, 2015, e176.
    • (2015) Exp. Mol. Med. , vol.47 , pp. e176
    • Alvarez-Cubero, M.J.1
  • 72
    • 0037431434 scopus 로고    scopus 로고
    • The product of the candidate prostate cancer susceptibility gene ELAC2 interacts with the gamma-tubulin complex
    • Korver, W., et al. The product of the candidate prostate cancer susceptibility gene ELAC2 interacts with the gamma-tubulin complex. Int. J. Cancer 104 (2003), 283–288.
    • (2003) Int. J. Cancer , vol.104 , pp. 283-288
    • Korver, W.1
  • 73
    • 84929453434 scopus 로고    scopus 로고
    • The end of the message: multiple protein-RNA interactions define the mRNA polyadenylation site
    • Shi, Y., Manley, J.L., The end of the message: multiple protein-RNA interactions define the mRNA polyadenylation site. Genes Dev. 29 (2015), 889–897.
    • (2015) Genes Dev. , vol.29 , pp. 889-897
    • Shi, Y.1    Manley, J.L.2
  • 74
    • 33845902048 scopus 로고    scopus 로고
    • Polyadenylation factor CPSF-73 is the pre-mRNA 3′-end-processing endonuclease
    • Mandel, C.R., et al. Polyadenylation factor CPSF-73 is the pre-mRNA 3′-end-processing endonuclease. Nature 444 (2006), 953–956.
    • (2006) Nature , vol.444 , pp. 953-956
    • Mandel, C.R.1
  • 75
    • 58149460414 scopus 로고    scopus 로고
    • Studies of the 5′ exonuclease and endonuclease activities of CPSF-73 in histone pre-mRNA processing
    • Yang, X., et al. Studies of the 5′ exonuclease and endonuclease activities of CPSF-73 in histone pre-mRNA processing. Mol. Cell. Biol. 29 (2009), 31–42.
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 31-42
    • Yang, X.1
  • 76
    • 53249132654 scopus 로고    scopus 로고
    • Conserved motifs in both CPSF73 and CPSF100 are required to assemble the active endonuclease for histone mRNA 3′-end maturation
    • Kolev, N.G., et al. Conserved motifs in both CPSF73 and CPSF100 are required to assemble the active endonuclease for histone mRNA 3′-end maturation. EMBO Rep. 9 (2008), 1013–1018.
    • (2008) EMBO Rep. , vol.9 , pp. 1013-1018
    • Kolev, N.G.1
  • 77
    • 65549149976 scopus 로고    scopus 로고
    • A core complex of CPSF73 CPSF100, and Symplekin may form two different cleavage factors for processing of poly (A) and histone mRNAs
    • Sullivan, K.D., et al. A core complex of CPSF73 CPSF100, and Symplekin may form two different cleavage factors for processing of poly (A) and histone mRNAs. Mol. Cell 34 (2009), 322–332.
    • (2009) Mol. Cell , vol.34 , pp. 322-332
    • Sullivan, K.D.1
  • 78
    • 84927911840 scopus 로고    scopus 로고
    • Integrator: surprisingly diverse functions in gene expression
    • Baillat, D., Wagner, E.J., Integrator: surprisingly diverse functions in gene expression. Trends Biochem. Sci. 40 (2015), 257–264.
    • (2015) Trends Biochem. Sci. , vol.40 , pp. 257-264
    • Baillat, D.1    Wagner, E.J.2
  • 79
    • 84924431008 scopus 로고    scopus 로고
    • The Integrator complex controls the termination of transcription at diverse classes of gene targets
    • Skaar, J.R., et al. The Integrator complex controls the termination of transcription at diverse classes of gene targets. Cell Res. 25 (2015), 288–305.
    • (2015) Cell Res. , vol.25 , pp. 288-305
    • Skaar, J.R.1
  • 80
    • 13444249745 scopus 로고    scopus 로고
    • A CPSF-73 homologue is required for cell cycle progression but not cell growth and interacts with a protein having features of CPSF-100
    • Dominski, Z., et al. A CPSF-73 homologue is required for cell cycle progression but not cell growth and interacts with a protein having features of CPSF-100. Mol. Cell. Biol. 25 (2005), 1489–1500.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 1489-1500
    • Dominski, Z.1
  • 81
    • 84857883120 scopus 로고    scopus 로고
    • snRNA 3′ end formation requires heterodimeric association of integrator subunits
    • Albrecht, T.R., Wagner, E.J., snRNA 3′ end formation requires heterodimeric association of integrator subunits. Mol. Cell. Biol. 32 (2012), 1112–1123.
    • (2012) Mol. Cell. Biol. , vol.32 , pp. 1112-1123
    • Albrecht, T.R.1    Wagner, E.J.2
  • 82
    • 23044479751 scopus 로고    scopus 로고
    • N-acylphosphatidylethanolamine-hydrolyzing phospholipase D: a novel enzyme of the beta-lactamase fold family releasing anandamide and other N-acylethanolamines
    • Ueda, N., et al. N-acylphosphatidylethanolamine-hydrolyzing phospholipase D: a novel enzyme of the beta-lactamase fold family releasing anandamide and other N-acylethanolamines. Life Sci. 77 (2005), 1750–1758.
    • (2005) Life Sci. , vol.77 , pp. 1750-1758
    • Ueda, N.1
  • 83
    • 33744962965 scopus 로고    scopus 로고
    • Functional analysis of the purified anandamide-generating phospholipase D as a member of the metallo-beta-lactamase family
    • Wang, J., et al. Functional analysis of the purified anandamide-generating phospholipase D as a member of the metallo-beta-lactamase family. J. Biol. Chem. 281 (2006), 12325–12335.
    • (2006) J. Biol. Chem. , vol.281 , pp. 12325-12335
    • Wang, J.1
  • 84
    • 34548512479 scopus 로고    scopus 로고
    • Biosynthetic pathways of the endocannabinoid anandamide
    • Okamoto, Y., et al. Biosynthetic pathways of the endocannabinoid anandamide. Chem. Biodiv. 4 (2007), 1842–1857.
    • (2007) Chem. Biodiv. , vol.4 , pp. 1842-1857
    • Okamoto, Y.1
  • 85
    • 21244465211 scopus 로고    scopus 로고
    • N-acylphosphatidylethanolamine-hydrolyzing phospholipase D Is an Important determinant of uterine anandamide levels during implantation
    • Guo, Y., et al. N-acylphosphatidylethanolamine-hydrolyzing phospholipase D Is an Important determinant of uterine anandamide levels during implantation. J. Biol. Chem. 280 (2005), 23429–23432.
    • (2005) J. Biol. Chem. , vol.280 , pp. 23429-23432
    • Guo, Y.1
  • 86
    • 84924667080 scopus 로고    scopus 로고
    • Adipose tissue NAPE–PLD controls fat mass development by altering the browning process and gut microbiota
    • Geurts, L., et al. Adipose tissue NAPE–PLD controls fat mass development by altering the browning process and gut microbiota. Nat. Commun., 6, 2015, 6495.
    • (2015) Nat. Commun. , vol.6 , pp. 6495
    • Geurts, L.1
  • 87
    • 84924039134 scopus 로고    scopus 로고
    • Structure of human N-acylphosphatidylethanolamine-hydrolyzing phospholipase D: regulation of fatty acid ethanolamide biosynthesis by bile acids
    • Magotti, P., et al. Structure of human N-acylphosphatidylethanolamine-hydrolyzing phospholipase D: regulation of fatty acid ethanolamide biosynthesis by bile acids. Structure 23 (2015), 598–604.
    • (2015) Structure , vol.23 , pp. 598-604
    • Magotti, P.1
  • 88
    • 84923377448 scopus 로고    scopus 로고
    • Discovery of Desketoraloxifene analogues as inhibitors of mammalian, Pseudomonas aeruginosa, and NAPE phospholipase D enzymes
    • Scott, S.A., et al. Discovery of Desketoraloxifene analogues as inhibitors of mammalian, Pseudomonas aeruginosa, and NAPE phospholipase D enzymes. ACS Chem. Biol. 10 (2014), 421–432.
    • (2014) ACS Chem. Biol. , vol.10 , pp. 421-432
    • Scott, S.A.1
  • 89
    • 62449189961 scopus 로고    scopus 로고
    • Multiple changes in sialic acid biology during human evolution
    • Varki, A., Multiple changes in sialic acid biology during human evolution. Glycoconj. J. 26 (2009), 231–245.
    • (2009) Glycoconj. J. , vol.26 , pp. 231-245
    • Varki, A.1
  • 90
    • 0037015010 scopus 로고    scopus 로고
    • Inactivation of CMP-N-acetylneuraminic acid hydroxylase occurred prior to brain expansion during human evolution
    • Chou, H.H., et al. Inactivation of CMP-N-acetylneuraminic acid hydroxylase occurred prior to brain expansion during human evolution. Proc. Natl. Acad. Sci. U.S.A. 99 (2002), 11736–11741.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 11736-11741
    • Chou, H.H.1
  • 91
    • 33644780854 scopus 로고    scopus 로고
    • Fixation of the human-specific CMP-N-acetylneuraminic acid hydroxylase pseudogene and implications of haplotype diversity for human evolution
    • Hayakawa, T., et al. Fixation of the human-specific CMP-N-acetylneuraminic acid hydroxylase pseudogene and implications of haplotype diversity for human evolution. Genetics 172 (2006), 1139–1146.
    • (2006) Genetics , vol.172 , pp. 1139-1146
    • Hayakawa, T.1
  • 92
    • 24644481321 scopus 로고    scopus 로고
    • Evolution of human-chimpanzee differences in malaria susceptibility: relationship to human genetic loss of N-glycolylneuraminic acid
    • Martin, M.J., et al. Evolution of human-chimpanzee differences in malaria susceptibility: relationship to human genetic loss of N-glycolylneuraminic acid. Proc. Natl. Acad. Sci. U.S.A. 102 (2005), 12819–12824.
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 12819-12824
    • Martin, M.J.1
  • 93
    • 84925433305 scopus 로고    scopus 로고
    • Host adaptation of a bacterial toxin from the human pathogen Salmonella Typhi
    • Deng, L., et al. Host adaptation of a bacterial toxin from the human pathogen Salmonella Typhi. Cell 159 (2014), 1290–1299.
    • (2014) Cell , vol.159 , pp. 1290-1299
    • Deng, L.1
  • 94
    • 77149167804 scopus 로고    scopus 로고
    • Human CMP-N-acetylneuraminic acid hydroxylase is a novel stem cell marker linked to stem cell-specific mechanisms
    • Nystedt, J., et al. Human CMP-N-acetylneuraminic acid hydroxylase is a novel stem cell marker linked to stem cell-specific mechanisms. Stem Cells 28 (2010), 258–267.
    • (2010) Stem Cells , vol.28 , pp. 258-267
    • Nystedt, J.1
  • 95
    • 79957893186 scopus 로고    scopus 로고
    • Pancreatic beta-cell failure in obese mice with human-like CMP-Neu5Ac hydroxylase deficiency
    • Kavaler, S., et al. Pancreatic beta-cell failure in obese mice with human-like CMP-Neu5Ac hydroxylase deficiency. FASEB J. 25 (2011), 1887–1893.
    • (2011) FASEB J. , vol.25 , pp. 1887-1893
    • Kavaler, S.1
  • 96
    • 33646693852 scopus 로고    scopus 로고
    • Genetic basis for the lack of N-glycolylneuraminic acid expression in human tissues and its implication to human evolution
    • Suzuki, A., Genetic basis for the lack of N-glycolylneuraminic acid expression in human tissues and its implication to human evolution. Proc. Jpn. Acad. Ser. B Phys. Biol. Sci. 82 (2006), 93–103.
    • (2006) Proc. Jpn. Acad. Ser. B Phys. Biol. Sci. , vol.82 , pp. 93-103
    • Suzuki, A.1
  • 97
    • 0029000263 scopus 로고
    • Molecular cloning of cytidine monophospho-N-acetylneuraminic acid hydroxylase. Regulation of species- and tissue-specific expression of N-glycolylneuraminic acid
    • Kawano, T., et al. Molecular cloning of cytidine monophospho-N-acetylneuraminic acid hydroxylase. Regulation of species- and tissue-specific expression of N-glycolylneuraminic acid. J. Biol. Chem. 270 (1995), 16458–16463.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16458-16463
    • Kawano, T.1
  • 98
    • 0033082703 scopus 로고    scopus 로고
    • The beta-lactamase cycle: a tale of selective pressure and bacterial ingenuity
    • Matagne, A., et al. The beta-lactamase cycle: a tale of selective pressure and bacterial ingenuity. Nat. Prod. Rep. 16 (1999), 1–19.
    • (1999) Nat. Prod. Rep. , vol.16 , pp. 1-19
    • Matagne, A.1
  • 99
    • 17444363393 scopus 로고    scopus 로고
    • Metallo-beta-lactamases: the quiet before the storm?
    • Walsh, T.R., et al. Metallo-beta-lactamases: the quiet before the storm?. Clin. Micr. Rev. 18 (2005), 306–325.
    • (2005) Clin. Micr. Rev. , vol.18 , pp. 306-325
    • Walsh, T.R.1
  • 100
    • 84875923394 scopus 로고    scopus 로고
    • Stormy waters ahead”: global emergence of carbapenemases
    • Patel, G., Bonomo, R.A., Stormy waters ahead”: global emergence of carbapenemases. Front. Microbiol. 14 (2013), 4–48.
    • (2013) Front. Microbiol. , vol.14 , pp. 4-48
    • Patel, G.1    Bonomo, R.A.2
  • 101
    • 67651180741 scopus 로고    scopus 로고
    • Beta-lactams and beta-lactamase-inhibitors in current- or potential-clinical practice: a comprehensive update
    • Shahid, M., et al. Beta-lactams and beta-lactamase-inhibitors in current- or potential-clinical practice: a comprehensive update. Crit. Rev. Microbiol. 35 (2009), 81–108.
    • (2009) Crit. Rev. Microbiol. , vol.35 , pp. 81-108
    • Shahid, M.1
  • 102
    • 84884764949 scopus 로고    scopus 로고
    • Kinetics of avibactam inhibition against class A, C and D β-lactamases
    • Ehmann, D.E., et al. Kinetics of avibactam inhibition against class A, C and D β-lactamases. J. Biol. Chem. 288 (2013), 27960–27971.
    • (2013) J. Biol. Chem. , vol.288 , pp. 27960-27971
    • Ehmann, D.E.1
  • 103
    • 84872871981 scopus 로고    scopus 로고
    • Metallo-β-lactamase structure and function
    • Palzkill, T., Metallo-β-lactamase structure and function. Ann. N. Y. Acad. Sci. 1277 (2013), 91–104.
    • (2013) Ann. N. Y. Acad. Sci. , vol.1277 , pp. 91-104
    • Palzkill, T.1
  • 104
    • 0035119114 scopus 로고    scopus 로고
    • Standard numbering scheme for class B β-lactamases
    • Galleni, M., et al. Standard numbering scheme for class B β-lactamases. Antimicrob. Agents Chemother. 45 (2001), 660–663.
    • (2001) Antimicrob. Agents Chemother. , vol.45 , pp. 660-663
    • Galleni, M.1
  • 105
    • 84877931035 scopus 로고    scopus 로고
    • Beta-lactamase-mediated resistance: a biochemical, epidemiological and genetic overview
    • Gutkind, G.O., et al. Beta-lactamase-mediated resistance: a biochemical, epidemiological and genetic overview. Curr. Pharm. Des. 19 (2013), 164–208.
    • (2013) Curr. Pharm. Des. , vol.19 , pp. 164-208
    • Gutkind, G.O.1
  • 106
    • 84875181975 scopus 로고    scopus 로고
    • Global spread of antibiotic resistance: the example of New Delhi metallo-β-lactamase (NDM)-mediated carbapenem resistance
    • Johnson, A.P., Woodford, N., Global spread of antibiotic resistance: the example of New Delhi metallo-β-lactamase (NDM)-mediated carbapenem resistance. J. Med. Microbiol. 62 (2013), 499–513.
    • (2013) J. Med. Microbiol. , vol.62 , pp. 499-513
    • Johnson, A.P.1    Woodford, N.2
  • 107
    • 84866417151 scopus 로고    scopus 로고
    • Binuclear metallohydrolases: complex mechanistic strategies for a simple chemical reaction
    • Schenk, G., et al. Binuclear metallohydrolases: complex mechanistic strategies for a simple chemical reaction. Acc. Chem. Res. 45 (2012), 1593–1603.
    • (2012) Acc. Chem. Res. , vol.45 , pp. 1593-1603
    • Schenk, G.1
  • 108
    • 34547889078 scopus 로고    scopus 로고
    • A minimalistic approach to identify substrate binding features in B1 Metallo-beta-lactamases
    • Poeylaut-Palena, A.A., A minimalistic approach to identify substrate binding features in B1 Metallo-beta-lactamases. Bioorg. Med. Chem. Lett. 17 (2007), 5171–5174.
    • (2007) Bioorg. Med. Chem. Lett. , vol.17 , pp. 5171-5174
    • Poeylaut-Palena, A.A.1
  • 109
    • 84879302319 scopus 로고    scopus 로고
    • An update on the status of potent inhibitors of metallo-β–lactamases
    • Faridoon, UI Islam, N., An update on the status of potent inhibitors of metallo-β–lactamases. Sci. Pharm. 81 (2013), 309–327.
    • (2013) Sci. Pharm. , vol.81 , pp. 309-327
    • Faridoon1    UI Islam, N.2
  • 110
    • 84886877549 scopus 로고    scopus 로고
    • β-Lactamase inhibitors: a review of the patent literature (2010-2013)
    • Buynak, J.D., β-Lactamase inhibitors: a review of the patent literature (2010-2013). Expert. Opin. Ther. Pat. 23 (2013), 1469–1481.
    • (2013) Expert. Opin. Ther. Pat. , vol.23 , pp. 1469-1481
    • Buynak, J.D.1
  • 111
    • 80054078476 scopus 로고    scopus 로고
    • Fast, scalable generation of high-quality protein multiple sequence alignments using Clustal Omega
    • Sievers, F., et al. Fast, scalable generation of high-quality protein multiple sequence alignments using Clustal Omega. Mol. Syst. Biol., 7, 2011, 539.
    • (2011) Mol. Syst. Biol. , vol.7 , pp. 539
    • Sievers, F.1
  • 112
    • 84891782659 scopus 로고    scopus 로고
    • Pfam protein families database
    • Finn, R.D., et al. Pfam protein families database. Nucl. Acids Res. 42 (2014), 222–230.
    • (2014) Nucl. Acids Res. , vol.42 , pp. 222-230
    • Finn, R.D.1
  • 113
    • 84937130981 scopus 로고    scopus 로고
    • Distinct metal isoforms underlie promiscuous activity profiles of metalloenzymes
    • Baier, F., et al. Distinct metal isoforms underlie promiscuous activity profiles of metalloenzymes. ACS Chem. Biol. 10 (2015), 1684–1693.
    • (2015) ACS Chem. Biol. , vol.10 , pp. 1684-1693
    • Baier, F.1
  • 114
    • 84908461884 scopus 로고    scopus 로고
    • Structural and mechanistic insights into NDM-1 catalyzed hydrolysis of cephalosporins
    • Feng, H., et al. Structural and mechanistic insights into NDM-1 catalyzed hydrolysis of cephalosporins. J. Am. Chem. Soc. 136 (2014), 14694–14697.
    • (2014) J. Am. Chem. Soc. , vol.136 , pp. 14694-14697
    • Feng, H.1
  • 115
    • 3142543755 scopus 로고    scopus 로고
    • The human hydroxyacylglutathione hydrolase (HAGH) gene encodes both cytosolic and mitochondrial forms of glyoxalase II
    • Cordell, P.A., et al. The human hydroxyacylglutathione hydrolase (HAGH) gene encodes both cytosolic and mitochondrial forms of glyoxalase II. J. Biol. Chem. 279 (2004), 28653–28661.
    • (2004) J. Biol. Chem. , vol.279 , pp. 28653-28661
    • Cordell, P.A.1
  • 116
    • 77953395030 scopus 로고    scopus 로고
    • Function of Apollo (SNM1B) at telomere highlighted by a splice variant identified in a patient with Hoyeraal-Hreidarsson syndrome
    • Touzot, F., et al. Function of Apollo (SNM1B) at telomere highlighted by a splice variant identified in a patient with Hoyeraal-Hreidarsson syndrome. Proc. Natl. Acad. Sci. U.S.A. 107 (2010), 10097–10102.
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 10097-10102
    • Touzot, F.1
  • 117
    • 3142555854 scopus 로고    scopus 로고
    • Functional and biochemical dissection of the structure-specific nuclease ARTEMIS
    • Pannicke, U., et al. Functional and biochemical dissection of the structure-specific nuclease ARTEMIS. EMBO J. 23 (2004), 1987–1997.
    • (2004) EMBO J. , vol.23 , pp. 1987-1997
    • Pannicke, U.1
  • 118
    • 19344374008 scopus 로고    scopus 로고
    • Omenn syndrome due to ARTEMIS mutations
    • Ege, M., et al. Omenn syndrome due to ARTEMIS mutations. Blood 105 (2005), 4179–4186.
    • (2005) Blood , vol.105 , pp. 4179-4186
    • Ege, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.