메뉴 건너뛰기




Volumn 7, Issue 2, 2015, Pages

DNA-pairing and annealing processes in homologous recombination and homology-directed repair

Author keywords

[No Author keywords available]

Indexed keywords

CRUCIFORM DNA; DNA; DNA BINDING PROTEIN; HETERODUPLEX;

EID: 84922575928     PISSN: None     EISSN: 19430264     Source Type: Journal    
DOI: 10.1101/cshperspect.a016444     Document Type: Article
Times cited : (102)

References (170)
  • 1
  • 3
    • 78649501394 scopus 로고    scopus 로고
    • Meiotic versus mitotic recombination: Two different routes for double-strand break repair: The different functions of meiotic versus mitotic DSB repair are reflected in different pathway usage and different outcomes
    • Andersen SL, Sekelsky J. 2010. Meiotic versus mitotic recombination: Two different routes for double-strand break repair: The different functions of meiotic versus mitotic DSB repair are reflected in different pathway usage and different outcomes. Bioessays 32: 1058-1066.
    • (2010) Bioessays , vol.32 , pp. 1058-1066
    • Andersen, S.L.1    Sekelsky, J.2
  • 4
    • 0036913982 scopus 로고    scopus 로고
    • OB-fold domains: A snapshot of the evolution of sequence, structure and function
    • Arcus V 2002. OB-fold domains: A snapshot of the evolution of sequence, structure and function. Curr Opin Struct Biol 12: 794-801.
    • (2002) Curr Opin Struct Biol , vol.12 , pp. 794-801
    • Arcus, V.1
  • 5
    • 0030632241 scopus 로고    scopus 로고
    • Chiasmata, crossovers, and meiotic chromosome segregation
    • Bascom-Slack CA, Ross LO, Dawson DS. 1997. Chiasmata, crossovers, and meiotic chromosome segregation. Adv Genet 35: 253 -284.
    • (1997) Adv Genet , vol.35
    • Bascom-Slack, C.A.1    Ross, L.O.2    Dawson, D.S.3
  • 6
    • 0030584084 scopus 로고    scopus 로고
    • Human Rad51 protein promotes ATP-dependent homologous pairing and strand transfer reactions in vitro
    • Baumann P, Benson FE, West SC. 1996. Human Rad51 protein promotes ATP-dependent homologous pairing and strand transfer reactions in vitro. Cell 87: 757-766.
    • (1996) Cell , vol.87 , pp. 757-766
    • Baumann, P.1    Benson, F.2    West, S.C.3
  • 8
    • 0032554654 scopus 로고    scopus 로고
    • The uvsY recombination protein of bacteriophage T4 forms hexamers in the presence and absence of single-stranded DNA
    • Beernink HT, Morrical SW. 1998. The uvsY recombination protein of bacteriophage T4 forms hexamers in the presence and absence of single-stranded DNA. Biochemistry 37: 5673-5681.
    • (1998) Biochemistry , vol.37 , pp. 5673-5681
    • Beernink, H.T.1    Morrical, S.W.2
  • 9
    • 0033214860 scopus 로고    scopus 로고
    • RMPs: Recombination/ replication mediator proteins
    • Beernink HT, Morrical SW. 1999. RMPs: Recombination/ replication mediator proteins. Trends Biochem Sci 24: 385-389.
    • (1999) Trends Biochem Sci , vol.24 , pp. 385-389
    • Beernink, H.T.1    Morrical, S.W.2
  • 11
    • 0001865832 scopus 로고    scopus 로고
    • DNA strand exchange proteins: A biochemical and physical comparison
    • Bianco PR, Tracy RB, Kowalczykowski SC. 1998. DNA strand exchange proteins: A biochemical and physical comparison. Front Biosci 3: D570-D603.
    • (1998) Front Biosci , vol.3 , pp. D570-D603
    • Bianco, P.R.1    Tracy, R.B.2    Kowalczykowski, S.C.3
  • 12
    • 3442896884 scopus 로고    scopus 로고
    • Replication protein A phosphorylation and the cellular response to DNA damage
    • Binz SK, Sheehan AM, Wold MS. 2004. Replication protein A phosphorylation and the cellular response to DNA damage. DNA Repair (Amst) 3: 1015-1024.
    • (2004) DNA Repair (Amst) , vol.3 , pp. 1015-1024
    • Binz, S.K.1    Sheehan, A.M.2    Wold, M.S.3
  • 13
    • 1342302794 scopus 로고    scopus 로고
    • From RPA to BRCA2: Lessons from single-stranded DNA binding by the OB-fold
    • Bochkarev A, Bochkareva E. 2004. From RPA to BRCA2: Lessons from single-stranded DNA binding by the OB-fold. Curr Opin Struct Biol 14: 36-42.
    • (2004) Curr Opin Struct Biol , vol.14 , pp. 36-42
    • Bochkarev, A.1    Bochkareva, E.2
  • 14
    • 0021910631 scopus 로고
    • On the mechanism of renaturation of complementary DNA strands by the recA protein of Escherichia Coli
    • Bryant FR, Lehman IR. 1985. On the mechanism of renaturation of complementary DNA strands by the recA protein of Escherichia coli. Proc Natl Acad Sci 82: 297-301.
    • (1985) Proc Natl Acad Sci , vol.82 , pp. 297-301
    • Bryant, F.R.1    Lehman, I.R.2
  • 15
    • 80052675332 scopus 로고    scopus 로고
    • Functions of the Snf2/Swi2 family Rad54 motor protein in homologous recombination
    • Ceballos SJ, Heyer WD. 2011. Functions of the Snf2/Swi2 family Rad54 motor protein in homologous recombination. Biochim Biophys Acta 1809: 509-523.
    • (2011) Biochim Biophys Acta , vol.1809 , pp. 509-523
    • Ceballos, S.J.1    Heyer, W.D.2
  • 17
    • 44349162159 scopus 로고    scopus 로고
    • Mechanism of homologous recombination from the RecA-ssDNA/dsDNA structures
    • Chen Z, Yang H, Pavletich NR 2008. Mechanism of homologous recombination from the RecA-ssDNA/dsDNA structures. Nature 453: 489-494.
    • (2008) Nature , vol.453 , pp. 489-494
    • Chen, Z.1    Yang, H.2    Pavletich, N.R.3
  • 18
    • 77955777906 scopus 로고    scopus 로고
    • Insights into the mechanism of Rad51 recombinase from the structure and properties of a filament interface mutant
    • Chen J, Villanueva N, Rould MA, Morrical SW. 2010. Insights into the mechanism of Rad51 recombinase from the structure and properties of a filament interface mutant. Nucleic Acids Res 38: 4889-4906.
    • (2010) Nucleic Acids Res , vol.38 , pp. 4889-4906
    • Chen, J.1    Villanueva, N.2    Rould, M.A.3    Morrical, S.W.4
  • 19
    • 0027376678 scopus 로고
    • Genetic and molecular analyses of the C-terminal region of the recE gene from the Rac prophage of Escherichia coli K-12 reveal the recT gene
    • Clark AJ, Sharma V, Brenowitz S, Chu CC, Sandler S, Satin L, Templin A, Berger I, Cohen A. 1993. Genetic and molecular analyses of the C-terminal region of the recE gene from the Rac prophage of Escherichia coli K-12 reveal the recT gene. J. Bacteriol 175: 7673-7682.
    • (1993) J. Bacteriol , vol.175 , pp. 7673-7682
    • Clark, A.J.1    Sharma, V.2    Brenowitz, S.3    Chu, C.C.4    Sandler, S.5    Satin, L.6    Templin, A.7    Berger, I.8    Cohen, A.9
  • 20
    • 77951593741 scopus 로고    scopus 로고
    • Ring-shaped Rad51 paralog protein complexes bind Holliday junctions and replication forks as visualized by electron microscopy
    • Compton SA, Ozgür S, Griffith JD. 2010. Ring-shaped Rad51 paralog protein complexes bind Holliday junctions and replication forks as visualized by electron microscopy. J Biol Chem 285: 13349-13356.
    • (2010) J Biol Chem , vol.285 , pp. 13349-13356
    • Compton, S.A.1    Ozgür, S.2    Griffith, J.D.3
  • 22
    • 0032605682 scopus 로고    scopus 로고
    • Recombinational DNA repair in bacteria and the RecA protein
    • Cox MM. 1999. Recombinational DNA repair in bacteria and the RecA protein. Prog Nucleic Acid Res Mol Biol 63:311-366.
    • (1999) Prog Nucleic Acid Res Mol Biol , vol.63 , pp. 311-366
    • Cox, M.M.1
  • 23
    • 0242692609 scopus 로고    scopus 로고
    • The bacterial RecA protein as a motor protein
    • Cox MM. 2003. The bacterial RecA protein as a motor protein. Annu Rev Microbiol 57: 551-577.
    • (2003) Annu Rev Microbiol , vol.57 , pp. 551-577
    • Cox, M.M.1
  • 24
    • 0343551289 scopus 로고
    • RecA protein of Escherichia coli promotes branch migration, a kinetically distinct phase of DNA strand exchange
    • Cox MM, Lehman IR. 1981. recA protein of Escherichia coli promotes branch migration, a kinetically distinct phase of DNA strand exchange. Proc Natl Acad Sci 78: 3433-3437.
    • (1981) Proc Natl Acad Sci , vol.78 , pp. 3433-3437
    • Cox, M.M.1    Lehman, I.R.2
  • 25
    • 84873677484 scopus 로고    scopus 로고
    • Roles of DNA helicases in the mediation and regulation of homologous recombination
    • Daley JM, Niu H, Sung P. 2013. Roles of DNA helicases in the mediation and regulation of homologous recombination. Adv Exp Med Biol 767: 185-202.
    • (2013) Adv Exp Med Biol , vol.767 , pp. 185-202
    • Daley, J.M.1    Niu, H.2    Sung, P.3
  • 27
    • 0019457908 scopus 로고
    • Concerted strand exchange and formation of Holliday structures by E. Coli RecA protein
    • DasGupta C, Wu AM, Kahn R, Cunningham RP, Radding CM. 1983. Concerted strand exchange and formation of Holliday structures by E. coli RecA protein. Cell 25: 507-516.
    • (1983) Cell , vol.25 , pp. 507-516
    • Dasgupta, C.1    Wu, A.M.2    Kahn, R.3    Cunningham, R.4    Radding, C.M.5
  • 28
    • 0034759324 scopus 로고    scopus 로고
    • The yeast recombinational repair protein Rad59 interacts with Rad52 and stimulates single-strand annealing
    • Davis AP, Symington LS. 2001. The yeast recombinational repair protein Rad59 interacts with Rad52 and stimulates single-strand annealing. Genetics 159: 515-525.
    • (2001) Genetics , vol.159 , pp. 515-525
    • Davis, A.P.1    Symington, L.S.2
  • 29
    • 2542422284 scopus 로고    scopus 로고
    • The Rad52-Rad59 complex interacts with Rad51 and replication protein A
    • Davis AP, Symington LS. 2003. The Rad52-Rad59 complex interacts with Rad51 and replication protein A. DNA Repair (Amst) 2: 1127-1134.
    • (2003) DNA Repair (Amst) , vol.2 , pp. 1127-1134
    • Davis, A.P.1    Symington, L.S.2
  • 30
    • 67650489517 scopus 로고    scopus 로고
    • Human replication protein A-Rad52-single-stranded DNA complex: Stoichiometry and evidence for strand transfer regulation by phosphorylation
    • Deng X, Prakash A, Dhar K, Baia GS, Kolar C, Oakley GG, Borgstahl GE. 2009. Human replication protein A-Rad52-single-stranded DNA complex: Stoichiometry and evidence for strand transfer regulation by phosphorylation. Biochemistry 48: 6633-6643.
    • (2009) Biochemistry , vol.48 , pp. 6633-6643
    • Deng, X.1    Prakash, A.2    Dhar, K.3    Baia, G.S.4    Kolar, C.5    Oakley, G.G.6    Borgstahl, G.E.7
  • 31
    • 38649130654 scopus 로고    scopus 로고
    • The Srs2 helicase activity is stimulated by Rad51 filaments on dsDNA: Implications for crossover incidence during mitotic recombination
    • Dupaigne P, Le Breton C, Fabre F, Gangloff S, Le Cam E, Veaute X. 2008. The Srs2 helicase activity is stimulated by Rad51 filaments on dsDNA: Implications for crossover incidence during mitotic recombination. Mol Cell 29: 243-254.
    • (2008) Mol Cell , vol.29 , pp. 243-254
    • Dupaigne, P.1    Breton, C.2    Fabre, F.3    Gangloff, S.4    Le Cam, E.5    Veaute, X.6
  • 33
    • 84857118715 scopus 로고    scopus 로고
    • Single-molecule imaging of DNA pairing by RecA reveals a three-dimensional homology search
    • Forget AL, Kowalczykowski SC. 2012. Single-molecule imaging of DNA pairing by RecA reveals a three-dimensional homology search. Nature 482: 423-427.
    • (2012) Nature , vol.482 , pp. 423-427
    • Forget, A.L.1    Kowalczykowski, S.C.2
  • 34
    • 0022902536 scopus 로고
    • DNA synthesis dependent on genetic recombination: Characterization of a reaction catalyzed by purified bacteriophage T4 proteins
    • Formosa T, Alberts BM. 1986. DNA synthesis dependent on genetic recombination: Characterization of a reaction catalyzed by purified bacteriophage T4 proteins. Cell 47: 793-806.
    • (1986) Cell , vol.47 , pp. 793-806
    • Formosa, T.1    Alberts, B.M.2
  • 35
    • 78650418624 scopus 로고    scopus 로고
    • Crystal structure of the phage T4 recombinase UvsX and its functional interaction with the T4 SF2 helicase UvsW
    • Gajewski S, Webb MR, Galkin V, Egelman EH, Kreuzer KN, White SW. 2011. Crystal structure of the phage T4 recombinase UvsX and its functional interaction with the T4 SF2 helicase UvsW J Mol Biol 405: 65-76.
    • (2011) J Mol Biol , vol.405 , pp. 65-76
    • Gajewski, S.1    Webb, M.R.2    Galkin, V.3    Egelman, E.H.4    Kreuzer, K.N.5    White, S.W.6
  • 36
    • 19544394263 scopus 로고    scopus 로고
    • Homologous chromosome interactions in meiosis: Diversity amidst conservation
    • Gerton JL, Hawley RS. 2005. Homologous chromosome interactions in meiosis: diversity amidst conservation. Nat Rev Genet 6: 477-487.
    • (2005) Nat Rev Genet , vol.6 , pp. 477-487
    • Gerton, J.L.1    Hawley, R.S.2
  • 37
    • 0022881276 scopus 로고
    • The mechanism of the search for homology promoted by recA protein. Facilitated diffusion within nucleoprotein networks
    • Gonda DK, Radding CM. 1986. The mechanism of the search for homology promoted by recA protein. Facilitated diffusion within nucleoprotein networks, J Biol Chem 261: 13087-13096.
    • (1986) J Biol Chem , vol.261 , pp. 13087-13096
    • Gonda, D.K.1    Radding, C.M.2
  • 38
    • 0021954057 scopus 로고
    • The uvsX protein of bacteriophage T4 arranges single-stranded and double-stranded DNA into similar helical nucleoprotein filaments
    • Griffith J, Formosa T. 1985. The uvsX protein of bacteriophage T4 arranges single-stranded and double-stranded DNA into similar helical nucleoprotein filaments, J Biol Chem 260: 4484-4491.
    • (1985) J Biol Chem , vol.260 , pp. 4484-4491
    • Griffith, J.1    Formosa, T.2
  • 41
    • 0026876934 scopus 로고
    • Exploring the pathways of homologous recombination
    • Haber JE. 1992. Exploring the pathways of homologous recombination. Curr Opin Cell Biol 4: 401-412.
    • (1992) Curr Opin Cell Biol , vol.4 , pp. 401-412
    • Haber, J.E.1
  • 42
    • 0028343501 scopus 로고
    • Homologous pairing and strand exchange promoted by the Escherichia coli RecT protein
    • Hall SD, Kolodner RD. 1994. Homologous pairing and strand exchange promoted by the Escherichia coli RecT protein. Proc Natl Acad Sci 91: 3205-3209.
    • (1994) Proc Natl Acad Sci , vol.91 , pp. 3205-3209
    • Hall, S.D.1    Kolodner, R.D.2
  • 43
    • 0024498701 scopus 로고
    • UvsY protein of bacteriophage T4 is an accessory protein for in vitro catalysis of strand exchange
    • Harris LD, Griffith JD. 1989. UvsY protein of bacteriophage T4 is an accessory protein for in vitro catalysis of strand exchange, J Mol Biol 206: 19-27.
    • (1989) J Mol Biol , vol.206 , pp. 19-27
    • Harris, L.D.1    Griffith, J.D.2
  • 44
    • 0025804534 scopus 로고
    • The characterization of a complex of three bacteriophage T4 recombination proteins, uvsX protein, uvsY protein, and gene 32 protein, on single-stranded DNA
    • Hashimoto K, Yonesaki T. 1991. The characterization of a complex of three bacteriophage T4 recombination proteins, uvsX protein, uvsY protein, and gene 32 protein, on single-stranded DNA. J Biol Chem 266: 4883-4888.
    • (1991) J Biol Chem , vol.266 , pp. 4883-4888
    • Hashimoto, K.1    Yonesaki, T.2
  • 45
    • 33748713412 scopus 로고    scopus 로고
    • Rad54: The Swiss Army knife of homologous recombination?
    • Heyer WD, Li X, Rolfsmeier M, Zhang XP. 2006. Rad54: The Swiss Army knife of homologous recombination? Nucleic Acids Res 34: 4115-4125.
    • (2006) Nucleic Acids Res , vol.34 , pp. 4115-4125
    • Heyer, W.D.1    Li, X.2    Rolfsmeier, M.3    Zhang, X.P.4
  • 46
    • 80052870830 scopus 로고    scopus 로고
    • Processing of homologous recombination repair intermediates by the Sgsl-Top3-Rmil and Mus81-Mms4 complexes
    • Hickson ID, Mankouri HW. 2011. Processing of homologous recombination repair intermediates by the Sgsl-Top3-Rmil and Mus81-Mms4 complexes. Cell Cycle 10: 3078-3085.
    • (2011) Cell Cycle , vol.10 , pp. 3078-3085
    • Hickson, I.D.1    Mankouri, H.W.2
  • 47
    • 0345447604 scopus 로고    scopus 로고
    • Srs2 and Sgsl-Top3 suppress crossovers during double-strand break repair in yeast
    • Ira G, Malkova A, Liberi G, Foiani M, Haber JE. 2003. Srs2 and Sgsl-Top3 suppress crossovers during double-strand break repair in yeast. Cell 115: 401-411.
    • (2003) Cell , vol.115 , pp. 401-411
    • Ira, G.1    Malkova, A.2    Liberi, G.3    Foiani, M.4    Haber, J.E.5
  • 48
    • 9144244444 scopus 로고    scopus 로고
    • Classification and evolutionary history of the single-strand annealing proteins, RecT, Redbeta, ERF and RAD52
    • Iyer LM, Koonin EV, Aravind L. 2002. Classification and evolutionary history of the single-strand annealing proteins, RecT, Redbeta, ERF and RAD52. BMC Genomics 3: 8.
    • (2002) BMC Genomics , vol.3 , pp. 8
    • Iyer, L.M.1    Koonin, E.V.2    Aravind, L.3
  • 49
    • 77957975815 scopus 로고    scopus 로고
    • Purified human BRCA2 stimulates RAD51-mediated recombination
    • Jensen RB, Carreira A, Kowalczykowski SC. 2010. Purified human BRCA2 stimulates RAD51-mediated recombination. Nature 467: 678-683.
    • (2010) Nature , vol.467 , pp. 678-683
    • Jensen, R.B.1    Carreira, A.2    Kowalczykowski, S.C.3
  • 50
    • 0037180443 scopus 로고    scopus 로고
    • Escherichia coli reco protein anneals ssdna complexed with its cognate ssdna-binding protein: A common step in genetic recombination
    • Kantake N, Madiraju MV, Sugiyama T, Kowalczykowski SC 2002. Escherichia coli RecO protein anneals ssDNA complexed with its cognate ssDNA-binding protein: A common step in genetic recombination. Proc Natl Acad Sci 99: 15327-15332.
    • (2002) Proc Natl Acad Sci , vol.99 , pp. 15327-15332
    • Kantake, N.1    Madiraju, M.V.2    Sugiyama, T.3    Kowalczykowski, S.C.4
  • 51
    • 0032489495 scopus 로고    scopus 로고
    • The βprotein of phage X binds preferentially to an intermediate in DNA renaturation
    • Karakousis G, Ye N, Li Z, Chiu SK, Reddy G, Radding CM. 1998. The β protein of phage X binds preferentially to an intermediate in DNA renaturation. J Mol Biol 276: 721-731.
    • (1998) J Mol Biol , vol.276 , pp. 721-731
    • Karakousis, G.1    Ye, N.2    Li, Z.3    Chiu, S.K.4    Reddy, G.5    Radding, C.M.6
  • 52
    • 0026662981 scopus 로고
    • On the role of ATP hydrolysis in RecA protein-mediated DNA strand exchange. II. Four-strand exchanges
    • Kim JI, Cox MM, Inman RB. 1992. On the role of ATP hydrolysis in RecA protein-mediated DNA strand exchange. II. Four-strand exchanges, J Biol Chem 267: 16444-16449.
    • (1992) J Biol Chem , vol.267 , pp. 16444-16449
    • Kim, J.I.1    Cox, M.M.2    Inman, R.B.3
  • 53
    • 0025610719 scopus 로고
    • The role of the bacteriophage T4 gene 32 protein in homologous pairing
    • Kodadek T 1990. The role of the bacteriophage T4 gene 32 protein in homologous pairing. J Biol Chem 265:20966-20969.
    • (1990) J Biol Chem , vol.265 , pp. 20966-20969
    • Kodadek, T.1
  • 54
    • 0023919927 scopus 로고
    • The mechanism of homologous DNA strand exchange catalyzed by the bacteriophage T4 uvsX and gene 32 proteins
    • Kodadek T, Wong ML, Alberts BM. 1988. The mechanism of homologous DNA strand exchange catalyzed by the bacteriophage T4 uvsX and gene 32 proteins, J Biol Chem 263: 9427-9436.
    • (1988) J Biol Chem , vol.263 , pp. 9427-9436
    • Kodadek, T.1    Wong, M.L.2    Alberts, B.M.3
  • 55
    • 0024474142 scopus 로고
    • The phage T4 uvs Y recombination protein stabilizes presynaptic filaments
    • Kodadek T, Gan DC, Stemke-Hale K. 1989. The phage T4 uvs Y recombination protein stabilizes presynaptic filaments. J Biol Chem 264: 16451-16457.
    • (1989) J Biol Chem , vol.264 , pp. 16451-16457
    • Kodadek, T.1    Gan, D.C.2    Stemke-Hale, K.3
  • 56
    • 0028233078 scopus 로고
    • Homologous pairing proteins encoded by the Escherichia coli recE and recT genes
    • Kolodner R, Hall SD, Luisi-DeLuca C. 1994. Homologous pairing proteins encoded by the Escherichia coli recE and recT genes. Mol Microbiol 11: 23-30.
    • (1994) Mol Microbiol , vol.11 , pp. 23-30
    • Kolodner, R.1    Hall, S.D.2    Luisi-Deluca, C.3
  • 57
    • 0025891414 scopus 로고
    • Biochemistry of genetic recombination: Energetics and mechanism of DNA strand exchange
    • Kowalczykowski SC. 1991. Biochemistry of genetic recombination: Energetics and mechanism of DNA strand exchange. Annu Rev Biophys Biophys Chem 20: 539-575.
    • (1991) Annu Rev Biophys Biophys Chem , vol.20 , pp. 539-575
    • Kowalczykowski, S.C.1
  • 58
    • 44349104598 scopus 로고    scopus 로고
    • Structural biology: Snapshots of DNA repair
    • Kowalczykowski SC. 2008. Structural biology: Snapshots of DNA repair. Nature 453: 463-466.
    • (2008) Nature , vol.453 , pp. 463-466
    • Kowalczykowski, S.C.1
  • 59
    • 0034176951 scopus 로고    scopus 로고
    • Recombination-dependentDNAreplication in phage T4
    • Kreuzer KN. 2000. Recombination-dependent DNA replication in phage T4. Trends Biochem Sci 25: 165-173.
    • (2000) Trends Biochem Sci , vol.25 , pp. 165-173
    • Kreuzer, K.N.1
  • 60
    • 78649531872 scopus 로고    scopus 로고
    • Initiation of bacteriophage T4 DNA replication and replication fork dynamics: A review in the Virology Journal Series on Bacteriophage T4 and Its Relatives
    • Kreuzer KN, Brister JR. 2010. Initiation of bacteriophage T4 DNA replication and replication fork dynamics: A review in the Virology Journal series on bacteriophage T4 and its relatives. Virol J 7: 358.
    • (2010) Virol J , vol.7 , pp. 358
    • Kreuzer, K.N.1    Brister, J.R.2
  • 61
    • 3042759750 scopus 로고    scopus 로고
    • Strand exchange activity of human recombination protein Rad52
    • Kumar JK, Gupta RC. 2004. Strand exchange activity of human recombination protein Rad52. Proc Natl Acad Sci 101: 9562-9567.
    • (2004) Proc Natl Acad Sci , vol.101 , pp. 9562-9567
    • Kumar, J.K.1    Gupta, R.C.2
  • 62
    • 84920527784 scopus 로고    scopus 로고
    • Mechanism and regulation of meiotic recombination initiation
    • Lam I, Keeney S. 2015. Mechanism and regulation of meiotic recombination initiation. Cold Spring Harb Perspect Biol 7: a016634.
    • Cold Spring Harb Perspect Biol , vol.7
    • Lam, I.1    Keeney, S.2
  • 63
    • 33745279076 scopus 로고    scopus 로고
    • Origins of sequence selectivity in homologous genetic recombination: Insights from rapid kinetic probing of RecA-mediated DNA strand exchange
    • Lee AM, Xiao J, Singleton SE 2006. Origins of sequence selectivity in homologous genetic recombination: Insights from rapid kinetic probing of RecA-mediated DNA strand exchange. J Mol Biol 360: 343-359.
    • (2006) J Mol Biol , vol.360 , pp. 343-359
    • Lee, A.M.1    Xiao, J.2    Singleton, S.E.3
  • 64
    • 59649102253 scopus 로고    scopus 로고
    • RAD54 controls access to the invading 3’-OH end after RAD51-mediated DNA strand invasion in homologous recombination in Saccharomyces Cerevisiae
    • Li X, Heyer WD. 2009. RAD54 controls access to the invading 3’-OH end after RAD51-mediated DNA strand invasion in homologous recombination in Saccharomyces cerevisiae. Nucleic Acids Res 37: 638-646.
    • (2009) Nucleic Acids Res , vol.37 , pp. 638-646
    • Li, X.1    Heyer, W.D.2
  • 66
    • 78649607001 scopus 로고    scopus 로고
    • Assembly and dynamics of the bacteriophage T4 homologous recombination machinery
    • Liu J, Morrical SW. 2010. Assembly and dynamics of the bacteriophage T4 homologous recombination machinery. Virol J 7: 357.
    • (2010) Virol J , vol.7 , pp. 357
    • Liu, J.1    Morrical, S.W.2
  • 67
    • 33748755117 scopus 로고    scopus 로고
    • Dynamics of bacteriophage T4 presynaptic filament assembly from extrinsic fluorescence measurements of Gp32-single-stranded DNA interactions
    • Liu J, Qian N, Morrical SW. 2006. Dynamics of bacteriophage T4 presynaptic filament assembly from extrinsic fluorescence measurements of Gp32-single-stranded DNA interactions. J Biol Chem 281: 26308-26319.
    • (2006) J Biol Chem , vol.281 , pp. 26308-26319
    • Liu, J.1    Qian, N.2    Morrical, S.W.3
  • 68
    • 77957804215 scopus 로고    scopus 로고
    • Human BRCA2 protein promotes RAD51 filament formation on RPA-covered single-stranded DNA
    • Liu J, Doty T, Gibson B, Heyer WD. 2010. Human BRCA2 protein promotes RAD51 filament formation on RPA-covered single-stranded DNA. Nat Struct Mol Biol 17: 1260-1262.
    • (2010) Nat Struct Mol Biol , vol.17 , pp. 1260-1262
    • Liu, J.1    Doty, T.2    Gibson, B.3    Heyer, W.D.4
  • 69
    • 79956365920 scopus 로고    scopus 로고
    • Presynaptic filament dynamics in homologous recombination and DNA repair
    • Liu J, Ehmsen KT, Heyer WD, Morrical SW. 2011a. Presynaptic filament dynamics in homologous recombination and DNA repair. Crit Rev Biochem Mol Biol 46:240-270.
    • (2011) Crit Rev Biochem Mol Biol , vol.46 , pp. 240-270
    • Liu, J.1    Ehmsen, K.T.2    Heyer, W.D.3    Morrical, S.W.4
  • 70
    • 80855132890 scopus 로고    scopus 로고
    • Rad51 paralogues Rad55-Rad57 balance the anti-recombinase Srs2 in Rad51 filament formation
    • Liu J, Renault L, Veaute X, Fabre F, Stahlberg H, Heyer WD. 2011b. Rad51 paralogues Rad55-Rad57 balance the anti-recombinase Srs2 in Rad51 filament formation. Nature 479: 245-248.
    • (2011) Nature , vol.479 , pp. 245-248
    • Liu, J.1    Renault, L.2    Veaute, X.3    Fabre, F.4    Stahlberg, H.5    Heyer, W.D.6
  • 71
    • 84887603325 scopus 로고    scopus 로고
    • Kinetics of presynaptic filament assembly in the presence of single-stranded DNA binding protein and recombination mediator protein
    • Liu J, Berger CL, Morrical SW. 2013. Kinetics of presynaptic filament assembly in the presence of single-stranded DNA binding protein and recombination mediator protein. Biochemistry 52: 7878-7889.
    • (2013) Biochemistry , vol.52 , pp. 7878-7889
    • Liu, J.1    Berger, C.L.2    Morrical, S.W.3
  • 72
    • 42449130956 scopus 로고    scopus 로고
    • Break-induced replication: What is it and what is it for?
    • Llorente B, Smith CE, Symington LS. 2008. Break-induced replication: What is it and what is it for? Cell Cycle 7:859-864.
    • (2008) Cell Cycle , vol.7 , pp. 859-864
    • Llorente, B.1    Smith, C.E.2    Symington, L.S.3
  • 73
    • 0028246888 scopus 로고
    • Escherichia Coli Single-Stranded Dna-Binding Protein: Multiple Dna-Binding Modes and Cooperativities
    • Lohman TM, Ferrari ME. 1994. Escherichia coli single-stranded DNA-binding protein: Multiple DNA-binding modes and cooperativities. Annu Rev Biochem 63: 527-570.
    • (1994) Annu Rev Biochem , vol.63 , pp. 527-570
    • Lohman, T.M.1    Ferrari, M.E.2
  • 75
    • 77953076932 scopus 로고    scopus 로고
    • Break-induced replication requires all essential DNA replication factors except those specific for pre-RC assembly
    • Lydeard JR, Lipkin-Moore Z, Sheu YJ, Stillman B, Burgers PM, Haber JE. 2010. Break-induced replication requires all essential DNA replication factors except those specific for pre-RC assembly. Genes Dev 24: 1133-1144.
    • (2010) Genes Dev , vol.24 , pp. 1133-1144
    • Lydeard, J.R.1    Lipkin-Moore, Z.2    Sheu, Y.J.3    Stillman, B.4    Burgers, P.M.5    Haber, J.E.6
  • 76
    • 84879158902 scopus 로고    scopus 로고
    • Coordinated binding of single-stranded and double-stranded DNA by uvsX recombinase
    • Maher RL, Morrical SW. 2013. Coordinated binding of single-stranded and double-stranded DNA by uvsX recombinase. PLoS ONR 8: e66654.
    • (2013) Plos ONR , vol.8
    • Maher, R.L.1    Morrical, S.W.2
  • 77
    • 80053186097 scopus 로고    scopus 로고
    • Coordination of DNA replication and recombination activities in the maintenance of genome stability
    • Maher RL, Branagan AM, Morrical SW. 2011. Coordination of DNA replication and recombination activities in the maintenance of genome stability, J Cell Biochem 112: 2672-2682.
    • (2011) J Cell Biochem , vol.112 , pp. 2672-2682
    • Maher, R.L.1    Branagan, A.M.2    Morrical, S.W.3
  • 78
    • 29444455190 scopus 로고    scopus 로고
    • Visualization of the annealing of complementary single-stranded DNA catalyzed by the herpes simplex virus type 1ICP8 SSB/recombinase
    • Makhov AM, Griffith JD. 2006. Visualization of the annealing of complementary single-stranded DNA catalyzed by the herpes simplex virus type 1ICP8 SSB/recombinase. J Mol Biol 355: 911-922.
    • (2006) J Mol Biol , vol.355 , pp. 911-922
    • Makhov, A.M.1    Griffith, J.D.2
  • 79
    • 59149090528 scopus 로고    scopus 로고
    • The bipolar filaments formed by herpes simplex virus type 1SSB/recombination protein (ICP8) suggest a mechanism for DNA annealing
    • Makhov AM, Sen A, Yu X, Simon MN, Griffith JD, Egelman EH. 2009. The bipolar filaments formed by herpes simplex virus type 1SSB/recombination protein (ICP8) suggest a mechanism for DNA annealing, J Mol Biol 386: 273-279.
    • (2009) J Mol Biol , vol.386 , pp. 273-279
    • Makhov, A.M.1    Sen, A.2    Yu, X.3    Simon, M.N.4    Griffith, J.D.5    Egelman, E.H.6
  • 80
    • 79953196154 scopus 로고    scopus 로고
    • Holliday junction-containing DNA structures persist in cells lacking Sgsl or Top3 following exposure to DNA damage
    • Mankouri HW, Ashton TM, Hickson ID. 2011. Holliday junction-containing DNA structures persist in cells lacking Sgsl or Top3 following exposure to DNA damage. Proc Natl Acad Sci 108: 4944-4949.
    • (2011) Proc Natl Acad Sci , vol.108 , pp. 4944-4949
    • Mankouri, H.W.1    Ashton, T.M.2    Hickson, I.D.3
  • 83
    • 0029762349 scopus 로고    scopus 로고
    • The specificity of the secondary DNA binding site of RecA protein defines its role in DNA strand exchange
    • Mazin AV, Kowalczykowski SC. 1996. The specificity of the secondary DNA binding site of RecA protein defines its role in DNA strand exchange. Proc Natl Acad Sci 93: 10673-10678.
    • (1996) Proc Natl Acad Sci , vol.93 , pp. 10673-10678
    • Mazin, A.V.1    Kowalczykowski, S.C.2
  • 84
    • 0032481374 scopus 로고    scopus 로고
    • The function of the secondary DNA-binding site of RecA protein during DNA strand exchange
    • Mazin AV, Kowalczykowski SC. 1998. The function of the secondary DNA-binding site of RecA protein during DNA strand exchange. EMBO J 17: 1161-1168.
    • (1998) EMBO J , vol.17 , pp. 1161-1168
    • Mazin, A.V.1    Kowalczykowski, S.C.2
  • 85
    • 0037900075 scopus 로고    scopus 로고
    • A novel function of Rad54 protein. Stabilization of the Rad51 nucleoprotein filament
    • Mazin AV, Alexeev AA, Kowalczykowski SC. 2003. A novel function of Rad54 protein. Stabilization of the Rad51 nucleoprotein filament, J Biol Chem 278: 14029-14036.
    • (2003) J Biol Chem , vol.278 , pp. 14029-14036
    • Mazin, A.V.1    Alexeev, A.A.2    Kowalczykowski, S.C.3
  • 86
    • 0021929926 scopus 로고
    • Kinetics of DNArenaturation catalyzed by the RecA protein of Escherichia Coli
    • McEntee K. 1985. Kinetics of DNArenaturation catalyzed by the RecA protein of Escherichia coli. Biochemistry 24: 4345-4351.
    • (1985) Biochemistry , vol.24 , pp. 4345-4351
    • McEntee, K.1
  • 87
    • 0019835729 scopus 로고
    • Binding of the recA protein of Escherichia coli to single- and double-stranded DNA
    • McEntee K, Weinstock GM, Lehman IR. 1981. Binding of the recA protein of Escherichia coli to single- and double-stranded DNA. J Biol Chem 256: 8835-8844.
    • (1981) J Biol Chem , vol.256 , pp. 8835-8844
    • McEntee, K.1    Weinstock, G.M.2    Lehman, I.R.3
  • 88
    • 0034711381 scopus 로고    scopus 로고
    • Reconstitutionof the strand invasion step of double-strand break repair using human Rad51 Rad52 and RPA proteins
    • Mcllwraith MJ, Van Dyck E, Masson JY, Stasiak AZ, Stasiak A, West SC. 2000. Reconstitution of the strand invasion step of double-strand break repair using human Rad51 Rad52 and RPA proteins. J Mol Biol 304: 151-164.
    • (2000) J Mol Biol , vol.304 , pp. 151-164
    • McLlwraith, M.J.1    Van Dyck, E.2    Masson, J.Y.3    Stasiak, A.Z.4    Stasiak, A.5    West, S.C.6
  • 89
    • 37249083430 scopus 로고    scopus 로고
    • Synthesis-dependent strand annealing in meiosis
    • McMahill MS, Sham CW, Bishop DK 2007. Synthesis-dependent strand annealing in meiosis. PLoS Biol 5: e299.
    • (2007) Plos Biol , vol.5
    • McMahill, M.S.1    Sham, C.W.2    Bishop, D.K.3
  • 90
    • 84903757525 scopus 로고    scopus 로고
    • Sources of DNA double-strand breaks and models for recombinational DNA repair
    • Mehta A, Haber JE. 2014. Sources of DNA double-strand breaks and models for recombinational DNA repair. Cold Spring Harb Perspect Biol 6: a016428.
    • (2014) Cold Spring Harb Perspect Biol , vol.6
    • Mehta, A.1    Haber, J.E.2
  • 91
    • 0025166577 scopus 로고
    • Stable DNA heteroduplex formation catalyzed by the Escherichia coli RecA protein in the absence of ATP hydrolysis
    • Menetski JP, Bear DG, Kowalczykowski SC. 1990. Stable DNA heteroduplex formation catalyzed by the Escherichia coli RecA protein in the absence of ATP hydrolysis. Proc Natl Acad Sci 87: 21-25.
    • (1990) Proc Natl Acad Sci , vol.87 , pp. 21-25
    • Menetski, J.P.1    Bear, D.G.2    Kowalczykowski, S.C.3
  • 92
    • 68249116573 scopus 로고    scopus 로고
    • DNA end resection: Many nucleases make light work
    • Mimitou EP, Symington LS. 2009. DNA end resection: Many nucleases make light work. DNA Repair (Amst) 8: 983-995.
    • (2009) Dnarepair (Amst) , vol.8 , pp. 983-995
    • Mimitou, E.P.1    Symington, L.S.2
  • 93
    • 84875974599 scopus 로고    scopus 로고
    • Heteroduplex DNA position defines the roles of the Sgsl, Srs2, and Mphl helicases in promoting distinct recombination outcomes
    • Mitchel K, Lehner K Jinks-Robertson S. 2013. Heteroduplex DNA position defines the roles of the Sgsl, Srs2, and Mphl helicases in promoting distinct recombination outcomes. PLoS Genet 9: el003340.
    • (2013) Plos Genet , vol.9
    • Mitchel, K.1
  • 94
    • 84860551748 scopus 로고    scopus 로고
    • Homologous recombination via synthesis-dependent strand annealing in yeast requires the Irc20 and Srs2 DNA helicases
    • Miura T, Yamana Y, Usui T, Ogawa HI, Yamamoto MT, Kusano K. 2012. Homologous recombination via synthesis-dependent strand annealing in yeast requires the Irc20 and Srs2 DNA helicases. Genetics 191: 65-78.
    • (2012) Genetics , vol.191 , pp. 65-78
    • Miura, T.1    Yamana, Y.2    Usui, T.3    Ogawa, H.I.4    Yamamoto, M.T.5    Kusano, K.6
  • 95
    • 0027985084 scopus 로고
    • Effect of length and location of heterologous sequences on RecA-mediated strand exchange
    • Morel P, Stasiak A, Ehrlich SD, Cassuto E. 1994. Effect of length and location of heterologous sequences on RecA-mediated strand exchange, J Biol Chem 269: 19830-19835.
    • (1994) J Biol Chem , vol.269 , pp. 19830-19835
    • Morel, P.1    Stasiak, A.2    Ehrlich, S.D.3    Cassuto, E.4
  • 96
    • 0038392868 scopus 로고    scopus 로고
    • RecFOR proteins load RecA protein onto gapped DNA to accelerate DNA strand exchange: A universal step of recombinational repair
    • Morimatsu K, Kowalczykowski SC. 2003. RecFOR proteins load RecA protein onto gapped DNA to accelerate DNA strand exchange: A universal step of recombinational repair. Mol Cell 11: 1337-1347.
    • (2003) Mol Cell , vol.11 , pp. 1337-1347
    • Morimatsu, K.1    Kowalczykowski, S.C.2
  • 97
    • 0025111215 scopus 로고
    • The UvsY protein of bacteriophage T4 modulates recombination-dependent DNA synthesis in vitro
    • Morrical SW, Alberts BM. 1990. The UvsY protein of bacteriophage T4 modulates recombination-dependent DNA synthesis in vitro. J Biol Chem 265: 15096-15103.
    • (1990) J Biol Chem , vol.265 , pp. 15096-15103
    • Morrical, S.W.1    Alberts, B.M.2
  • 99
    • 0030044828 scopus 로고    scopus 로고
    • Intron mobility in phage T4 occurs in the context of recombination-dependent DNA replication by way of multiple pathways
    • Mueller JE, Clyman J, Huang YJ, Parker MM, Belfort M. 1996. Intron mobility in phage T4 occurs in the context of recombination-dependent DNA replication by way of multiple pathways. Genes Dev 10: 351-364.
    • (1996) Genes Dev , vol.10 , pp. 351-364
    • Mueller, J.E.1    Clyman, J.2    Huang, Y.J.3    Parker, M.M.4    Belfort, M.5
  • 100
    • 84862906340 scopus 로고    scopus 로고
    • Phage recombinases and their applications
    • Murphy KC. 2012. Phage recombinases and their applications. Adv Virus Res 83: 367-414.
    • (2012) Adv Virus Res , vol.83 , pp. 367-414
    • Murphy, K.C.1
  • 101
    • 0033624563 scopus 로고    scopus 로고
    • RecE/ RecTand Redα/Redβinitiate double-stranded break repair by specifically interacting with their respective partners
    • Muyrers JP, Zhang Y, Buchholz F, Stewart AF. 2000. RecE/ RecTand Redα/Redβ initiate double-stranded break repair by specifically interacting with their respective partners. Genes Dev 14: 1971-1982.
    • (2000) Genes Dev , vol.14 , pp. 1971-1982
    • Muyrers, J.P.1    Zhang, Y.2    Buchholz, F.3    Stewart, A.F.4
  • 102
    • 0346333311 scopus 로고    scopus 로고
    • Human Rad52 facilitates a three-stranded pairing that follows no strand exchange: A novel pairing function of the protein
    • Navadgi VM, Dutta A, Rao BJ. 2003. Human Rad52 facilitates a three-stranded pairing that follows no strand exchange: A novel pairing function of the protein. Biochemistry 42: 15237-15251.
    • (2003) Biochemistry , vol.42 , pp. 15237-15251
    • Navadgi, V.M.1    Dutta, A.2    Rao, B.J.3
  • 103
    • 0032556870 scopus 로고    scopus 로고
    • Rad52 protein stimulates DNA strand exchange by Rad51 and replication protein A
    • New JH, Sugiyama T, Zaitseva E, Kowalczykowski SC. 1998. Rad52 protein stimulates DNA strand exchange by Rad51 and replication protein A. Nature 391: 407-410.
    • (1998) Nature , vol.391 , pp. 407-410
    • New, J.H.1    Sugiyama, T.2    Zaitseva, E.3    Kowalczykowski, S.C.4
  • 104
    • 67649327128 scopus 로고    scopus 로고
    • Second-end DNA capture in double-strand break repair: How to catch a DNA by its tail
    • Nimonkar AV, Kowalczykowski SC. 2009. Second-end DNA capture in double-strand break repair: How to catch a DNA by its tail. Cell Cycle 8: 1816-1817.
    • (2009) Cell Cycle , vol.8 , pp. 1816-1817
    • Nimonkar, A.V.1    Kowalczykowski, S.C.2
  • 105
    • 62549160340 scopus 로고    scopus 로고
    • Rad52 promotes second-end DNA capture in double-stranded break repair to form complement-stabilized joint molecules
    • Nimonkar AV, Sica RA, Kowalczykowski SC. 2009. Rad52 promotes second-end DNA capture in double-stranded break repair to form complement-stabilized joint molecules. Proc Natl Acad Sci 106: 3077-3082.
    • (2009) Proc Natl Acad Sci , vol.106 , pp. 3077-3082
    • Nimonkar, A.V.1    Sica, R.A.2    Kowalczykowski, S.C.3
  • 106
    • 0037439088 scopus 로고    scopus 로고
    • Hallmarks of homology recognition by RecA-like recombinases are exhibited by the unrelated EscherichiacoliRecT protein
    • Noirot P, Gupta RC, Radding CM, Kolodner RD. 2003. Hallmarks of homology recognition by RecA-like recombinases are exhibited by the unrelated Escherichia coli RecT protein. EMBO J 22: 324-334.
    • (2003) EMBO J , vol.22 , pp. 324-334
    • Noirot, P.1    Gupta, R.C.2    Radding, C.M.3    Kolodner, R.D.4
  • 107
    • 0027167689 scopus 로고
    • Similarity of the yeast RAD 51 filament to the bacterial RecA filament
    • Ogawa T, Yu X, Shinohara A, Egelman EH. 1993. Similarity of the yeast RAD 51 filament to the bacterial RecA filament. Science 259: 1896-1899.
    • (1993) Science , vol.259 , pp. 1896-1899
    • Ogawa, T.1    Yu, X.2    Shinohara, A.3    Egelman, E.H.4
  • 108
    • 42249089039 scopus 로고    scopus 로고
    • RAD59 is required for efficient repair of simultaneous double-strand breaks resulting in translocations in Saccharomyces Cerevisiae
    • Pannunzio NR, Manthey GM, Bailis AM. 2008. RAD59 is required for efficient repair of simultaneous double-strand breaks resulting in translocations in Saccharomyces cerevisiae. DNA Repair (Amst) 7: 788-800.
    • (2008) DNA Repair (Amst) , vol.7 , pp. 788-800
    • Pannunzio, N.R.1    Manthey, G.M.2    Bailis, A.M.3
  • 110
    • 0033551177 scopus 로고    scopus 로고
    • Rings and Filaments of βprotein from Bacteriophage λ Suggest a Superfamily of Recombination Proteins
    • Passy SI, Yu X, Li Z, Radding CM, Egelman EH. 1999. Rings and filaments of β protein from bacteriophage λ suggest a superfamily of recombination proteins. Proc Natl Acad Sci 96: 4279-4284.
    • (1999) Proc Natl Acad Sci , vol.96 , pp. 4279-4284
    • Passy, S.I.1    Yu, X.2    Li, Z.3    Radding, C.M.4    Egelman, E.H.5
  • 112
    • 0033607640 scopus 로고    scopus 로고
    • Single strand DNA binding and annealing activities in the yeast recombination factor Rad59
    • Petukhova G, Stratton SA, Sung P. 1999. Single strand DNA binding and annealing activities in the yeast recombination factor Rad59. J Biol Chem 274: 33839-33842.
    • (1999) J Biol Chem , vol.274 , pp. 33839-33842
    • Petukhova, G.1    Stratton, S.A.2    Sung, P.3
  • 113
    • 0023139868 scopus 로고
    • Stable binding of recA protein to duplex DNA. Unraveling a paradox
    • Pugh BF, Cox MM. 1987a. Stable binding of recA protein to duplex DNA. Unraveling a paradox, J Biol Chem 262: 1326-1336.
    • (1987) J Biol Chem , vol.262 , pp. 1326-1336
    • Pugh, B.F.1    Cox, M.M.2
  • 114
    • 0023118206 scopus 로고
    • RecA protein binding to the
    • Pugh BF, Cox MM. 1987b. recA protein binding to the heteroduplex product of DNA strand exchange. J Biol Chem 262: 1337-1343.
    • (1987) J Biol Chem , vol.262 , pp. 1337-1343
    • Pugh, B.F.1    Cox, M.M.2
  • 115
    • 0023726413 scopus 로고
    • General mechanism for RecA protein binding to duplex DNA
    • Pugh BF, Cox MM. 1988. General mechanism for RecA protein binding to duplex DNA. J Mol Biol 203:479-493.
    • (1988) J Mol Biol , vol.203 , pp. 479-493
    • Pugh, B.F.1    Cox, M.M.2
  • 116
    • 80051527439 scopus 로고    scopus 로고
    • Real-time observation of strand exchange reaction with high spatiotemporal resolution
    • Ragunathan K, Joo C, Ha T. 2011. Real-time observation of strand exchange reaction with high spatiotemporal resolution. Structure 19: 1064-1073.
    • (2011) Structure , vol.19 , pp. 1064-1073
    • Ragunathan, K.1    Joo, C.2    Ha, T.3
  • 117
    • 78149422766 scopus 로고    scopus 로고
    • Achieving fidelity in homologous recombination despite extreme complexity: Informed decisions by molecular profiling
    • Rambo RP, Williams GJ, Tainer JA. 2010. Achieving fidelity in homologous recombination despite extreme complexity: Informed decisions by molecular profiling. Mol Cell 40: 347-348.
    • (2010) Mol Cell , vol.40 , pp. 347-348
    • Rambo, R.P.1    Williams, G.J.2    Tainer, J.A.3
  • 118
    • 10644237810 scopus 로고    scopus 로고
    • Multiple interactions with the Rad51 recombinase govern the homologous recombination function of Rad54
    • Raschle M, Van Komen S, Chi P, Ellenberger T, Sung P. 2004. Multiple interactions with the Rad51 recombinase govern the homologous recombination function of Rad54. J Biol Chem 279: 51973-51980.
    • (2004) J Biol Chem , vol.279 , pp. 51973-51980
    • Raschle, M.1    Van Komen, S.2    Chi, P.3    Ellenberger, T.4    Sung, P.5
  • 119
    • 0030966978 scopus 로고    scopus 로고
    • Human Rad52 protein promotes single-strand DNA annealing followed by branch migration
    • Reddy G, Golub EI, Radding CM. 1997. Human Rad52 protein promotes single-strand DNA annealing followed by branch migration. Mutat Res 377: 53-59.
    • (1997) Mutat Res , vol.377 , pp. 53-59
    • Reddy, G.1    Golub, E.I.2    Radding, C.M.3
  • 120
    • 21644463281 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 single-strand DNA binding protein ICP8 enhances the nuclease activity of the UL12 alkaline nuclease by increasing its processivity
    • Reuven NB, Weller SK. 2005. Herpes simplex virus type 1 single-strand DNA binding protein ICP8 enhances the nuclease activity of the UL12 alkaline nuclease by increasing its processivity. J Virol 79: 9356-9358.
    • (2005) J Virol , vol.79 , pp. 9356-9358
    • Reuven, N.B.1    Weller, S.K.2
  • 121
    • 0038468334 scopus 로고    scopus 로고
    • The herpes simplex virus type 1 alkaline nuclease and single-stranded DNA binding protein mediate strand exchange in vitro
    • Reuven NB, Staire AE, Myers RS, Weller SK. 2003. The herpes simplex virus type 1 alkaline nuclease and single-stranded DNA binding protein mediate strand exchange in vitro, J Virol 77: 7425-7433.
    • (2003) J Virol , vol.77 , pp. 7425-7433
    • Reuven, N.B.1    Staire, A.E.2    Myers, R.S.3    Weller, S.K.4
  • 122
    • 4143140939 scopus 로고    scopus 로고
    • Catalysis of strand exchange by the HSV-1 UL12 and ICP8 proteins: Potent ICP8 recombinase activity is revealed upon resection of dsDNA substrate by nuclease
    • Reuven NB, Willcox S, Griffith JD, Weller SK. 2004. Catalysis of strand exchange by the HSV-1 UL12 and ICP8 proteins: Potent ICP8 recombinase activity is revealed upon resection of dsDNA substrate by nuclease, J Mol Biol 342: 57-71.
    • (2004) J Mol Biol , vol.342 , pp. 57-71
    • Reuven, N.B.1    Willcox, S.2    Griffith, J.D.3    Weller, S.K.4
  • 123
    • 70350491426 scopus 로고    scopus 로고
    • Multiple human single-stranded DNA binding proteins function in genome maintenance: Structural, biochemical and functional analysis
    • Richard DJ, Bolderson E, Khanna KK. 2009. Multiple human single-stranded DNA binding proteins function in genome maintenance: Structural, biochemical and functional analysis. Crit Rev Biochem Mol Biol 44: 98-116.
    • (2009) Crit Rev Biochem Mol Biol , vol.44 , pp. 98-116
    • Richard, D.J.1    Bolderson, E.2    Khanna, K.K.3
  • 124
    • 0025222848 scopus 로고
    • Differential recognition of ultraviolet lesions by RecA protein. Possible mechanism for preferential targeting of SOS mutagenesis to (6-4) dipyrimidine sites
    • Rosenberg M, Echols H. 1990. Differential recognition of ultraviolet lesions by RecA protein. Possible mechanism for preferential targeting of SOS mutagenesis to (6-4) dipyrimidine sites. J Biol Chem 265: 20641-20645.
    • (1990) J Biol Chem , vol.265 , pp. 20641-20645
    • Rosenberg, M.1    Echols, H.2
  • 125
    • 84934441831 scopus 로고    scopus 로고
    • Structural studies of SSB interaction with RecO
    • Ryzhikov M, Korolev S. 2012. Structural studies of SSB interaction with RecO. Methods Mol Biol 922: 123-131.
    • (2012) Methods Mol Biol , vol.922 , pp. 123-131
    • Ryzhikov, M.1    Korolev, S.2
  • 126
    • 79960790784 scopus 로고    scopus 로고
    • Mechanism of RecO recruitment to DNA by single-stranded DNA binding protein
    • Ryzhikov M, Koroleva O, Postnov D, Tran A, Korolev S. 2011. Mechanism of RecO recruitment to DNA by single-stranded DNA binding protein. Nucleic Acids Res 39: 6305-6314.
    • (2011) Nucleic Acids Res , vol.39 , pp. 6305-6314
    • Ryzhikov, M.1    Koroleva, O.2    Postnov, D.3    Tran, A.4    Korolev, S.5
  • 127
    • 85016350482 scopus 로고    scopus 로고
    • Break-induced replication and genome stability
    • Sakofsky CJ, Ayyar S, Malkova A. 2012. Break-induced replication and genome stability. Biomolecules 2: 483-504.
    • (2012) Biomolecules , vol.2 , pp. 483-504
    • Sakofsky, C.J.1    Ayyar, S.2    Malkova, A.3
  • 128
    • 50649100744 scopus 로고    scopus 로고
    • Mechanism of eukaryotic homologous recombination
    • San Filippo J, Sung P, Klein H. 2008. Mechanism of eukaryotic homologous recombination. Annu Rev Biochem 77: 229-257.
    • (2008) Annu Rev Biochem , vol.77 , pp. 229-257
    • San Filippo, J.1    Sung, P.2    Klein, H.3
  • 129
    • 77956062712 scopus 로고    scopus 로고
    • RecA-mediated homology search as a nearly optimal signal detection system
    • Savir Y, Tlusty T. 2010. RecA-mediated homology search as a nearly optimal signal detection system. Mol Cell 40: 388-396.
    • (2010) Mol Cell , vol.40 , pp. 388-396
    • Savir, Y.1    Tlusty, T.2
  • 131
    • 0031556955 scopus 로고    scopus 로고
    • RecA protein filaments: End-dependent dissociation from ssDNA and stabilization by RecO and RecR proteins
    • Shan Q, Bork JM, Webb BL, Inman RB, Cox MM. 1997. RecA protein filaments: End-dependent dissociation from ssDNA and stabilization by RecO and RecR proteins. J Mol Biol 265: 519-540.
    • (1997) J Mol Biol , vol.265 , pp. 519-540
    • Shan, Q.1    Bork, J.M.2    Webb, B.L.3    Inman, R.B.4    Cox, M.M.5
  • 132
    • 3242880580 scopus 로고    scopus 로고
    • Structure and function of the double-strand break repair machinery
    • Shin DS, Chahwan C, Huffman JL, Tainer JA 2004. Structure and function of the double-strand break repair machinery. DNA Repair (Amst) 3: 863-873.
    • (2004) DNA Repair (Amst) , vol.3 , pp. 863-873
    • Shin, D.S.1    Chahwan, C.2    Huffman, J.L.3    Tainer, J.A.4
  • 133
    • 0031902872 scopus 로고    scopus 로고
    • Rad52 forms ring structures and co-operates with RPA in single-strand DNA annealing
    • Shinohara A, Shinohara M, Ohta T, Matsuda S, Ogawa T 1998. Rad52 forms ring structures and co-operates with RPA in single-strand DNA annealing. Genes Cells 3:145-156.
    • (1998) Genes Cells , vol.3 , pp. 145-156
    • Shinohara, A.1    Shinohara, M.2    Ohta, T.3    Matsuda, S.4    Ogawa, T.5
  • 134
    • 0036864703 scopus 로고    scopus 로고
    • Rad54, a Swi2/ Snf2-like recombinational repair protein, disassembles Rad51:DsDNA filaments
    • Solinger JA, Kiianitsa K, Heyer WD. 2002. Rad54, a Swi2/ Snf2-like recombinational repair protein, disassembles Rad51:dsDNA filaments. Mol Cell 10: 1175-1188.
    • (2002) Mol Cell , vol.10 , pp. 1175-1188
    • Solinger, J.A.1    Kiianitsa, K.2    Heyer, W.D.3
  • 135
    • 0034717199 scopus 로고    scopus 로고
    • Functional interactions among yeast Rad51 recombinase, Rad52 mediator, and replication protein A in DNA strand exchange
    • Song B, Sung P. 2000. Functional interactions among yeast Rad51 recombinase, Rad52 mediator, and replication protein A in DNA strand exchange, J Biol Chem 275: 15895-15904.
    • (2000) J Biol Chem , vol.275 , pp. 15895-15904
    • Song, B.1    Sung, P.2
  • 136
    • 0026500416 scopus 로고
    • The structure of the E. Coli recA protein monomer and polymer
    • Story RM, Weber IT, Steitz TA 1992. The structure of the E. coli recA protein monomer and polymer. Nature 355: 318-325.
    • (1992) Nature , vol.355 , pp. 318-325
    • Story, R.M.1    Weber, I.T.2    Steitz, T.A.3
  • 137
    • 0033946617 scopus 로고    scopus 로고
    • DNA length dependence of the single-strand annealing pathway and the role of Saccharomyces cerevisiae RAD59 in double-strand break repair
    • Sugawara N, Ira G, Haber JE. 2000. DNA length dependence of the single-strand annealing pathway and the role of Saccharomyces cerevisiae RAD59 in double-strand break repair. Mol Cell Biol 20: 5300-5309.
    • (2000) Mol Cell Biol , vol.20 , pp. 5300-5309
    • Sugawara, N.1    Ira, G.2    Haber, J.E.3
  • 138
    • 0037199924 scopus 로고    scopus 로고
    • Rad52 protein associates with replication protein A (RPA)-single-stranded DNA to accelerate Rad51-mediated displacement of RPA and presynaptic complex formation
    • Sugiyama T, Kowalczykowski SC. 2002. Rad52 protein associates with replication protein A (RPA)-single-stranded DNA to accelerate Rad51-mediated displacement of RPA and presynaptic complex formation, J Biol Chem 277: 31663-31672.
    • (2002) J Biol Chem , vol.277 , pp. 31663-31672
    • Sugiyama, T.1    Kowalczykowski, S.C.2
  • 139
    • 0032568595 scopus 로고    scopus 로고
    • DNA annealing by RAD52 protein is stimulated by specific interaction with the complex of replication protein A and single-stranded DNA
    • Sugiyama T, New JH, Kowalczykowski SC. 1998. DNA annealing by RAD52 protein is stimulated by specific interaction with the complex of replication protein A and single-stranded DNA. Proc Natl Acad Sci 95:6049-6054.
    • (1998) Proc Natl Acad Sci , vol.95 , pp. 6049-6054
    • Sugiyama, T.1    New, J.H.2    Kowalczykowski, S.C.3
  • 140
    • 0027978039 scopus 로고
    • Catalysis of ATP-dependent homologous DNA pairing and strand exchange by yeast RAD51 protein
    • Sung P. 1994. Catalysis of ATP-dependent homologous DNA pairing and strand exchange by yeast RAD51 protein. Science 265: 1241-1243.
    • (1994) Science , vol.265 , pp. 1241-1243
    • Sung, P.1
  • 141
    • 0030995362 scopus 로고    scopus 로고
    • Yeast Rad55 and Rad57 proteins form a heterodimer that functions with replication protein A to promoteDNAstrand exchange by Rad51 recombinase
    • Sung P. 1997a. Yeast Rad55 and Rad57 proteins form a heterodimer that functions with replication protein A to promote DNA strand exchange by Rad51 recombinase. Genes Dev 11: 1111-1121.
    • (1997) Genes Dev , vol.11 , pp. 1111-1121
    • Sung, P.1
  • 142
    • 0030666945 scopus 로고    scopus 로고
    • Function of yeast Rad52 protein as a mediator between replication protein A and the Rad51 recombinase
    • Sung P. 1997b. Function of yeast Rad52 protein as a mediator between replication protein A and the Rad51 recombinase. J Biol Chem 272: 28194-28197.
    • (1997) J Biol Chem , vol.272 , pp. 28194-28197
    • Sung, P.1
  • 143
    • 0029112483 scopus 로고
    • DNA strand exchange mediated by a RAD51-ssDNA nucleoprotein filament with polarity opposite to that of RecA
    • Sung P, Robberson DL. 1995. DNA strand exchange mediated by a RAD51-ssDNA nucleoprotein filament with polarity opposite to that of RecA. Cell 82: 453-461.
    • (1995) Cell , vol.82 , pp. 453-461
    • Sung, P.1    Robberson, D.L.2
  • 144
    • 0033579935 scopus 로고    scopus 로고
    • Biochemical interactions within a ternary complex of the bacteriophage T4 recombination proteins uvsYand gp32 bound to single-stranded DNA
    • Sweezy MA, Morrical SW. 1999. Biochemical interactions within a ternary complex of the bacteriophage T4 recombination proteins uvsYand gp32 bound to single-stranded DNA Biochemistry 38: 936-944.
    • (1999) Biochemistry , vol.38 , pp. 936-944
    • Sweezy, M.A.1    Morrical, S.W.2
  • 145
    • 0036900120 scopus 로고    scopus 로고
    • Role of RAD52 epistasis group genes in homologous recombination and double-strand break repair
    • Symington LS. 2002. Role of RAD52 epistasis group genes in homologous recombination and double-strand break repair. Microbiol Mol Biol Rev 66: 630-670.
    • (2002) Microbiol , vol.66 , pp. 630-670
    • Symington, L.S.1
  • 146
    • 84905493192 scopus 로고    scopus 로고
    • End section at double-strand breaks: Mechanism and regulation
    • Symington LS. 2014. End section at double-strand breaks: Mechanism and regulation. Cold Spring Harb Perspect Biol 6: a016436.
    • (2014) Cold Spring Harb Perspect Biol , vol.6
    • Symington, L.S.1
  • 148
    • 33845599600 scopus 로고    scopus 로고
    • Calorimetric analysis of binding of two consecutiveDNAstrands to RecA protein illuminates mechanism for recognition of homology
    • Takahashi M, Maraboeuf F, Morimatsu K, Selmane T, Fleury F, Norden B. 2007. Calorimetric analysis of binding of two consecutive DNA strands to RecA protein illuminates mechanism for recognition of homology. J Mol Biol 365: 603-611.
    • (2007) J Mol Biol , vol.365 , pp. 603-611
    • Takahashi, M.1    Maraboeuf, F.2    Morimatsu, K.3    Selmane, T.4    Fleury, F.5    Norden, B.6
  • 149
    • 0029563182 scopus 로고
    • Electron microscopic visualization of RecT protein and its complexes with DNA
    • Thresher RJ, Makhov AM, Hall SD, Kolodner R, Griffith JD. 1995. Electron microscopic visualization of RecT protein and its complexes with DNA. J Mol Biol 254: 364-371.
    • (1995) J Mol Biol , vol.254 , pp. 364-371
    • Thresher, R.J.1    Makhov, A.M.2    Hall, S.D.3    Kolodner, R.4    Griffith, J.D.5
  • 150
    • 23944475626 scopus 로고    scopus 로고
    • Mechanisms of, and barriers to, horizontal gene transfer between bacteria
    • Thomas CM, Nielsen KM. 2005. Mechanisms of, and barriers to, horizontal gene transfer between bacteria. Nat Rev Microbiol 3: 711-721.
    • (2005) Nat Rev Microbiol , vol.3 , pp. 711-721
    • Thomas, C.M.1    Nielsen, K.M.2
  • 152
    • 0026633047 scopus 로고
    • ATP-dependent branch migration of Holliday junctions promoted by the RuvA and RuvB proteins of E. Coli
    • Tsaneva IR, Müller B, West SC. 1992. ATP-dependent branch migration of Holliday junctions promoted by the RuvA and RuvB proteins of E. coli. Cell 69: 1171-1180.
    • (1992) Cell , vol.69 , pp. 1171-1180
    • Tsaneva, I.R.1    Müller, B.2    West, S.C.3
  • 153
    • 0028034452 scopus 로고
    • Protein interactions in genetic recombination in Escherichia coli. Interactions involving RecO and RecR overcome the inhibition of RecA by single-stranded DNA-binding protein
    • Umezu K, Kolodner RD. 1994. Protein interactions in genetic recombination in Escherichia coli. Interactions involving RecO and RecR overcome the inhibition of RecA by single-stranded DNA-binding protein. J Biol Chem 269: 30005-30013.
    • (1994) J Biol Chem , vol.269 , pp. 30005-30013
    • Umezu, K.1    Kolodner, R.D.2
  • 154
    • 0027238208 scopus 로고
    • Biochemical interaction of the Escherichia coli RecF, RecO, and RecR proteins with RecA protein and single-stranded DNA binding protein
    • Umezu K, Chi NW, Kolodner RD. 1993. Biochemical interaction of the Escherichia coli RecF, RecO, and RecR proteins with RecA protein and single-stranded DNA binding protein. Proc Natl Acad Sci 90: 3875-3879.
    • (1993) Proc Natl Acad Sci , vol.90 , pp. 3875-3879
    • Umezu, K.1    Chi, N.W.2    Kolodner, R.D.3
  • 155
    • 0037113947 scopus 로고    scopus 로고
    • Functional cross-talk among Rad51, Rad54, and replication protein A in heteroduplex DNA joint formation
    • Van Komen S, Petukhova G, Sigurdsson S, Sung P. 2002. Functional cross-talk among Rad51, Rad54, and replication protein A in heteroduplex DNA joint formation. J Biol Chem 277: 43578-43587.
    • (2002) J Biol Chem , vol.277 , pp. 43578-43587
    • Van Komen, S.1    Petukhova, G.2    Sigurdsson, S.3    Sung, P.4
  • 156
    • 0030908093 scopus 로고    scopus 로고
    • Replication protein A: A heterotrimeric, single-stranded DNA-binding protein required for eukaryotic DNA metabolism
    • Wold MS. 1997. Replication protein A: A heterotrimeric, single-stranded DNA-binding protein required for eukaryotic DNA metabolism. Annu Rev Biochem 66:61-92.
    • (1997) Annu Rev Biochem , vol.66 , pp. 61-92
    • Wold, M.S.1
  • 157
    • 84893749175 scopus 로고    scopus 로고
    • Rad54 functions as a heteroduplex DNA pump modulated by its DNA substrates and Rad51 during D-loop formation
    • Wright WD, Heyer WD. 2014. Rad54 functions as a heteroduplex DNA pump modulated by its DNA substrates and Rad51 during D-loop formation. Mol Cell 53: 420-432.
    • (2014) Mol Cell , vol.53 , pp. 420-432
    • Wright, W.D.1    Heyer, W.D.2
  • 158
    • 4143068081 scopus 로고    scopus 로고
    • Crystal structure of archaeal recombinase RADA: A snapshot of its extended conformation
    • Wu Y, He Y, Moya IA, Qian X, Luo Y. 2004. Crystal structure of archaeal recombinase RADA: A snapshot of its extended conformation. Mol Cell 15: 423-435.
    • (2004) Mol Cell , vol.15 , pp. 423-435
    • Wu, Y.1    He, Y.2    Moya, I.A.3    Qian, X.4    Luo, Y.5
  • 159
    • 33744962417 scopus 로고    scopus 로고
    • DNA annealing mediated by Rad52 and Rad59 proteins
    • Wu Y, Sugiyama T, Kowalczykowski SC. 2006. DNA annealing mediated by Rad52 and Rad59 proteins, J Biol Chem 281: 15441-15449.
    • (2006) J Biol Chem , vol.281 , pp. 15441-15449
    • Wu, Y.1    Sugiyama, T.2    Kowalczykowski, S.C.3
  • 160
  • 161
    • 77955802913 scopus 로고    scopus 로고
    • DNA-binding properties of T4 UvsY recombination mediator protein: Polynucleotide wrapping promotes high-affinity binding to single-stranded DNA
    • Xu H, Beernink HT, Morrical SW. 2010. DNA-binding properties of T4 UvsY recombination mediator protein: Polynucleotide wrapping promotes high-affinity binding to single-stranded DNA Nucleic Acids Res 38: 4821-4833.
    • (2010) Nucleic Acids Res , vol.38 , pp. 4821-4833
    • Xu, H.1    Beernink, H.T.2    Morrical, S.W.3
  • 162
    • 0035812601 scopus 로고    scopus 로고
    • Comparison of bacteriophage T4 UvsX and human Rad51 filaments suggests that RecA-like polymers may have evolved independently
    • Yang S, VanLoock MS, Yu X, Egelman EH. 2001. Comparison of bacteriophage T4 UvsX and human Rad51 filaments suggests that RecA-like polymers may have evolved independently, J Mol Biol 312: 999-1009.
    • (2001) J Mol Biol , vol.312 , pp. 999-1009
    • Yang, S.1    Vanloock, M.S.2    Yu, X.3    Egelman, E.H.4
  • 163
    • 3042676518 scopus 로고    scopus 로고
    • Preferential binding to branched DNA strands and strand-annealing activity of the human Rad51B, Rad51C, Rad51D and Xrcc2 protein complex
    • Yokoyama H, Sarai N, Kagawa W, Enomoto R, Shibata T, Kurumizaka H, Yokoyama S. 2004. Preferential binding to branched DNA strands and strand-annealing activity of the human Rad51B, Rad51C, Rad51D and Xrcc2 protein complex. Nucleic Acids Res 32: 2556-2565.
    • (2004) Nucleic Acids Res , vol.32 , pp. 2556-2565
    • Yokoyama, H.1    Sarai, N.2    Kagawa, W.3    Enomoto, R.4    Shibata, T.5    Kurumizaka, H.6    Yokoyama, S.7
  • 164
    • 0024394537 scopus 로고
    • Synergistic action of three recombination gene products of bacteriophage T4, uvsX, uvsY, and gene 32 proteins
    • Yonesaki T, Minagawa T. 1989. Synergistic action of three recombination gene products of bacteriophage T4, uvsX, uvsY, and gene 32 proteins. J Biol Chem 264: 7814-7820.
    • (1989) J Biol Chem , vol.264 , pp. 7814-7820
    • Yonesaki, T.1    Minagawa, T.2
  • 165
    • 0026666652 scopus 로고
    • Structural data suggest that the active and inactive forms of the RecA filament are not simply interconvertible
    • Yu X, Egelman EH. 1992. Structural data suggest that the active and inactive forms of the RecA filament are not simply interconvertible, J Mol Biol 227: 334-346.
    • (1992) J Mol Biol , vol.227 , pp. 334-346
    • Yu, X.1    Egelman, E.H.2
  • 166
    • 0027199391 scopus 로고
    • DNA conformation induced by the bacteriophage T4 UvsX protein appears identical to the conformation induced by the Escherichia coli RecA protein, J
    • Yu X, Egelman EH. 1993. DNA conformation induced by the bacteriophage T4 UvsX protein appears identical to the conformation induced by the Escherichia coli RecA protein, J Mol Biol 232: 1-4.
    • (1993) Mol Biol , vol.232 , pp. 1-4
    • Yu, X.1    Egelman, E.H.2
  • 167
    • 0035902614 scopus 로고    scopus 로고
    • Domain structure and dynamics in the helical filaments formed by RecA and Rad51 on DNA
    • Yu X, Jacobs SA, West SC, Ogawa T, Egelman EH. 2001. Domain structure and dynamics in the helical filaments formed by RecA and Rad51 on DNA Proc Natl Acad Sci 98: 8419-8424.
    • (2001) Proc Natl Acad Sci , vol.98 , pp. 8419-8424
    • Yu, X.1    Jacobs, S.A.2    West, S.C.3    Ogawa, T.4    Egelman, E.H.5
  • 168
    • 0033614034 scopus 로고    scopus 로고
    • The DNA binding properties of Saccharomyces cerevisiae Rad51 protein
    • Zaitseva EM, Zaitsev EN, Kowalczykowski SC. 1999. The DNA binding properties of Saccharomyces cerevisiae Rad51 protein, J Biol Chem 274: 2907-2915.
    • (1999) J Biol Chem , vol.274 , pp. 2907-2915
    • Zaitseva, E.M.1    Zaitsev, E.N.2    Kowalczykowski, S.C.3
  • 170
    • 84922517270 scopus 로고    scopus 로고
    • Recombination, pairing, and synapsis of homologs during meiosis
    • Zickler D, Kleckner N. 2015. Recombination, pairing, and synapsis of homologs during meiosis. Cold Spring Harb Perspect Biol doi: 10.1101/cshperspect.a016626.
    • (2015) Cold Spring Harb Perspect Biol
    • Zickler, D.1    Kleckner, N.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.