메뉴 건너뛰기




Volumn 17, Issue 5, 2005, Pages 733-743

The disposition of nascent strands at stalled replication forks dictates the pathway of replisome loading during restart

Author keywords

[No Author keywords available]

Indexed keywords

DEOXYRIBONUCLEOPROTEIN; HELICASE; REPLISOME;

EID: 14644415982     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcel.2005.01.019     Document Type: Article
Times cited : (125)

References (52)
  • 1
    • 0016813835 scopus 로고
    • DnaG gene product, a rifampicin-resistant RNA polymerase, initiates the conversion of a single-stranded coliphage DNA to its duplex replicative form
    • J.P. Bouche, K. Zechel, and A. Kornberg dnaG gene product, a rifampicin-resistant RNA polymerase, initiates the conversion of a single-stranded coliphage DNA to its duplex replicative form J. Biol. Chem. 250 1975 5995 6001
    • (1975) J. Biol. Chem. , vol.250 , pp. 5995-6001
    • Bouche, J.P.1    Zechel, K.2    Kornberg, A.3
  • 3
    • 2442489945 scopus 로고    scopus 로고
    • RuvAB and RecG are not essential for the recovery of DNA synthesis following UV-induced DNA damage in Escherichia coli
    • J.R. Donaldson, C.T. Courcelle, and J. Courcelle RuvAB and RecG are not essential for the recovery of DNA synthesis following UV-induced DNA damage in Escherichia coli Genetics 166 2004 1631 1640
    • (2004) Genetics , vol.166 , pp. 1631-1640
    • Donaldson, J.R.1    Courcelle, C.T.2    Courcelle, J.3
  • 5
    • 1942453437 scopus 로고    scopus 로고
    • A dnaC mutation in Escherichia coli that affects copy number of ColE1-like plasmids and the PriA-PriB (but not Rep-PriC) pathway of chromosomal replication restart
    • R. Harinarayanan, and J. Gowrishankar A dnaC mutation in Escherichia coli that affects copy number of ColE1-like plasmids and the PriA-PriB (but not Rep-PriC) pathway of chromosomal replication restart Genetics 166 2004 1165 1176
    • (2004) Genetics , vol.166 , pp. 1165-1176
    • Harinarayanan, R.1    Gowrishankar, J.2
  • 6
    • 0028100686 scopus 로고
    • Primase couples leading- and lagging-strand DNA synthesis from oriC
    • H. Hiasa, and K.J. Marians Primase couples leading- and lagging-strand DNA synthesis from oriC J. Biol. Chem. 269 1994 6058 6063
    • (1994) J. Biol. Chem. , vol.269 , pp. 6058-6063
    • Hiasa, H.1    Marians, K.J.2
  • 7
    • 0029831664 scopus 로고    scopus 로고
    • Two distinct modes of strand unlinking during theta-type DNA replication
    • H. Hiasa, and K.J. Marians Two distinct modes of strand unlinking during theta-type DNA replication J. Biol. Chem. 271 1996 21529 21535
    • (1996) J. Biol. Chem. , vol.271 , pp. 21529-21535
    • Hiasa, H.1    Marians, K.J.2
  • 8
    • 0038365180 scopus 로고    scopus 로고
    • Fate of DNA replication fork encountering a single DNA lesion during oriC plasmid DNA replication in vitro
    • K. Higuchi, T. Katayama, S. Iwai, M. Hidaka, T. Horiuchi, and H. Maki Fate of DNA replication fork encountering a single DNA lesion during oriC plasmid DNA replication in vitro Genes Cells 8 2003 437 449
    • (2003) Genes Cells , vol.8 , pp. 437-449
    • Higuchi, K.1    Katayama, T.2    Iwai, S.3    Hidaka, M.4    Horiuchi, T.5    Maki, H.6
  • 9
    • 0030052444 scopus 로고    scopus 로고
    • Binding of Escherichia coli primary replicative helicase DnaB protein to single-stranded DNA. Long-range allosteric conformational changes within the protein hexamer
    • M.J. Jezewska, U.S. Kim, and W. Bujalowski Binding of Escherichia coli primary replicative helicase DnaB protein to single-stranded DNA. Long-range allosteric conformational changes within the protein hexamer Biochemistry 35 1996 2129 2145
    • (1996) Biochemistry , vol.35 , pp. 2129-2145
    • Jezewska, M.J.1    Kim, U.S.2    Bujalowski, W.3
  • 10
    • 0032562822 scopus 로고    scopus 로고
    • Does single-stranded DNA pass through the inner channel of the protein hexamer in the complex with the Escherichia coli DnaB Helicase? Fluorescence energy transfer studies
    • M.J. Jezewska, S. Rajendran, D. Bujalowska, and W. Bujalowski Does single-stranded DNA pass through the inner channel of the protein hexamer in the complex with the Escherichia coli DnaB Helicase? Fluorescence energy transfer studies J. Biol. Chem. 273 1998 10515 10529
    • (1998) J. Biol. Chem. , vol.273 , pp. 10515-10529
    • Jezewska, M.J.1    Rajendran, S.2    Bujalowska, D.3    Bujalowski, W.4
  • 11
    • 0034141871 scopus 로고    scopus 로고
    • DnaB helicase stimulates primer synthesis activity on short oligonucleotide templates
    • S.K. Johnson, S. Bhattacharyya, and M.A. Griep DnaB helicase stimulates primer synthesis activity on short oligonucleotide templates Biochemistry 39 2000 736 744
    • (2000) Biochemistry , vol.39 , pp. 736-744
    • Johnson, S.K.1    Bhattacharyya, S.2    Griep, M.A.3
  • 12
    • 0030070356 scopus 로고    scopus 로고
    • Coupling of a replicative polymerase and helicase: A τ-DnaB interaction mediates rapid replication fork movement
    • S. Kim, H.G. Dallmann, C.S. McHenry, and K.J. Marians Coupling of a replicative polymerase and helicase: a τ-DnaB interaction mediates rapid replication fork movement Cell 84 1996 643 650
    • (1996) Cell , vol.84 , pp. 643-650
    • Kim, S.1    Dallmann, H.G.2    McHenry, C.S.3    Marians, K.J.4
  • 13
    • 0029863634 scopus 로고    scopus 로고
    • The DNA replication priming protein, PriA, is required for homologous recombination and double-strand break repair
    • T. Kogoma, G.W. Cadwell, K.G. Barnard, and T. Asai The DNA replication priming protein, PriA, is required for homologous recombination and double-strand break repair J. Bacteriol. 178 1996 1258 1264
    • (1996) J. Bacteriol. , vol.178 , pp. 1258-1264
    • Kogoma, T.1    Cadwell, G.W.2    Barnard, K.G.3    Asai, T.4
  • 15
    • 0022977660 scopus 로고
    • The Escherichia coli dnaB replication protein is a DNA helicase
    • J.H. LeBowitz, and R. McMacken The Escherichia coli dnaB replication protein is a DNA helicase J. Biol. Chem. 261 1986 4738 4748
    • (1986) J. Biol. Chem. , vol.261 , pp. 4738-4748
    • Lebowitz, J.H.1    McMacken, R.2
  • 16
    • 0026356063 scopus 로고
    • Replication deficiencies in priA mutants of Escherichia coli lacking the primosomal replication n' protein
    • E.H. Lee, and A. Kornberg Replication deficiencies in priA mutants of Escherichia coli lacking the primosomal replication n' protein Proc. Natl. Acad. Sci. USA 88 1991 3029 3032
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 3029-3032
    • Lee, E.H.1    Kornberg, A.2
  • 17
    • 0033609892 scopus 로고    scopus 로고
    • PriA-directed assembly of a primosome on D loop DNA
    • J. Liu, and K.J. Marians PriA-directed assembly of a primosome on D loop DNA J. Biol. Chem. 274 1999 25033 25041
    • (1999) J. Biol. Chem. , vol.274 , pp. 25033-25041
    • Liu, J.1    Marians, K.J.2
  • 18
    • 0033616683 scopus 로고    scopus 로고
    • Replication fork assembly at recombination intermediates is required for bacterial growth
    • J. Liu, L. Xu, S.J. Sandler, and K.J. Marians Replication fork assembly at recombination intermediates is required for bacterial growth Proc. Natl. Acad. Sci. USA 96 1999 3552 3555
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 3552-3555
    • Liu, J.1    Xu, L.2    Sandler, S.J.3    Marians, K.J.4
  • 19
    • 0026777126 scopus 로고
    • Prokaryotic DNA replication
    • K.J. Marians Prokaryotic DNA replication Annu. Rev. Biochem. 61 1992 673 719
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 673-719
    • Marians, K.J.1
  • 20
    • 0028868621 scopus 로고
    • θx174-type primosomal proteins: Purification and assay
    • K.J. Marians θX174-type primosomal proteins: purification and assay Methods Enzymol. 262 1995 507 521
    • (1995) Methods Enzymol. , vol.262 , pp. 507-521
    • Marians, K.J.1
  • 21
    • 0028148226 scopus 로고
    • Escherichia coli PriA protein is essential for inducible and constitutive stable DNA replication
    • H. Masai, T. Asai, Y. Kubota, K. Arai, and T. Kogoma Escherichia coli PriA protein is essential for inducible and constitutive stable DNA replication EMBO J. 13 1994 5338 5345
    • (1994) EMBO J. , vol.13 , pp. 5338-5345
    • Masai, H.1    Asai, T.2    Kubota, Y.3    Arai, K.4    Kogoma, T.5
  • 22
    • 4444224780 scopus 로고    scopus 로고
    • Measurement of SOS expression in individual Escherichia coli K-12 cells using fluorescence microscopy
    • J.D. McCool, E. Long, J.F. Petrosino, H.A. Sandler, S.M. Rosenberg, and S.J. Sandler Measurement of SOS expression in individual Escherichia coli K-12 cells using fluorescence microscopy Mol. Microbiol. 53 2004 1343 1357
    • (2004) Mol. Microbiol. , vol.53 , pp. 1343-1357
    • McCool, J.D.1    Long, E.2    Petrosino, J.F.3    Sandler, H.A.4    Rosenberg, S.M.5    Sandler, S.J.6
  • 23
    • 0035834755 scopus 로고    scopus 로고
    • Action of RuvAB at replication fork structures
    • P. McGlynn, and R.G. Lloyd Action of RuvAB at replication fork structures J. Biol. Chem. 276 2001 41938 41944
    • (2001) J. Biol. Chem. , vol.276 , pp. 41938-41944
    • McGlynn, P.1    Lloyd, R.G.2
  • 24
    • 0035902591 scopus 로고    scopus 로고
    • Rescue of stalled replication forks by RecG: Simultaneous translocation on the leading and lagging strand templates supports an active DNA unwinding model of fork reversal and Holliday junction formation
    • P. McGlynn, and R.G. Lloyd Rescue of stalled replication forks by RecG: simultaneous translocation on the leading and lagging strand templates supports an active DNA unwinding model of fork reversal and Holliday junction formation Proc. Natl. Acad. Sci. USA 98 2001 8227 8234
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 8227-8234
    • McGlynn, P.1    Lloyd, R.G.2
  • 25
    • 0030852247 scopus 로고    scopus 로고
    • The DNA replication protein PriA and the recombination protein RecG bind D-loops
    • P. McGlynn, A.A. Al-Deib, J. Liu, K.J. Marians, and R.G. Lloyd The DNA replication protein PriA and the recombination protein RecG bind D-loops J. Mol. Biol. 270 1997 212 221
    • (1997) J. Mol. Biol. , vol.270 , pp. 212-221
    • McGlynn, P.1    Al-Deib, A.A.2    Liu, J.3    Marians, K.J.4    Lloyd, R.G.5
  • 26
    • 0036844340 scopus 로고    scopus 로고
    • Recombinational repair and restart of damaged replication forks
    • P. McGlynn, and R.G. Lloyd Recombinational repair and restart of damaged replication forks Nat. Rev. Mol. Cell Biol. 3 2002 859 870
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 859-870
    • McGlynn, P.1    Lloyd, R.G.2
  • 27
    • 0031025093 scopus 로고    scopus 로고
    • DNA double-strand breaks caused by replication arrest
    • B. Michel, S.D. Ehrlich, and M. Uzest DNA double-strand breaks caused by replication arrest EMBO J. 16 1997 430 438
    • (1997) EMBO J. , vol.16 , pp. 430-438
    • Michel, B.1    Ehrlich, S.D.2    Uzest, M.3
  • 29
    • 0142180093 scopus 로고    scopus 로고
    • A critical role of the 3′ terminus of nascent DNA chains in recognition of stalled replication forks
    • T. Mizukoshi, T. Tanaka, K. Arai, D. Kohda, and H. Masai A critical role of the 3′ terminus of nascent DNA chains in recognition of stalled replication forks J. Biol. Chem. 278 2003 42234 42239
    • (2003) J. Biol. Chem. , vol.278 , pp. 42234-42239
    • Mizukoshi, T.1    Tanaka, T.2    Arai, K.3    Kohda, D.4    Masai, H.5
  • 30
    • 0029666277 scopus 로고    scopus 로고
    • The ordered assembly of the θx174-type primosome. I. Isolation and identification of intermediate protein-DNA complexes
    • J.Y. Ng, and K.J. Marians The ordered assembly of the θX174-type primosome. I. Isolation and identification of intermediate protein-DNA complexes J. Biol. Chem. 271 1996 15642 15648
    • (1996) J. Biol. Chem. , vol.271 , pp. 15642-15648
    • Ng, J.Y.1    Marians, K.J.2
  • 31
    • 0029666279 scopus 로고    scopus 로고
    • The ordered assembly of the θx174-type primosome. II. Preservation of primosome composition from assembly through replication
    • J.Y. Ng, and K.J. Marians The ordered assembly of the θX174-type primosome. II. Preservation of primosome composition from assembly through replication J. Biol. Chem. 271 1996 15649 15655
    • (1996) J. Biol. Chem. , vol.271 , pp. 15649-15655
    • Ng, J.Y.1    Marians, K.J.2
  • 32
    • 0025836589 scopus 로고
    • Inactivation of the Escherichia coli priA DNA replication protein induces the SOS response
    • P. Nurse, K.H. Zavitz, and K.J. Marians Inactivation of the Escherichia coli priA DNA replication protein induces the SOS response J. Bacteriol. 173 1991 6686 6693
    • (1991) J. Bacteriol. , vol.173 , pp. 6686-6693
    • Nurse, P.1    Zavitz, K.H.2    Marians, K.J.3
  • 33
    • 0033609883 scopus 로고    scopus 로고
    • Two modes of PriA binding to DNA
    • P. Nurse, J. Liu, and K.J. Marians Two modes of PriA binding to DNA J. Biol. Chem. 274 1999 25026 25032
    • (1999) J. Biol. Chem. , vol.274 , pp. 25026-25032
    • Nurse, P.1    Liu, J.2    Marians, K.J.3
  • 34
    • 0037799191 scopus 로고    scopus 로고
    • Uncoupling of leading- and lagging-strand DNA replication during lesion bypass in vivo
    • V. Pages, and R.P. Fuchs Uncoupling of leading- and lagging-strand DNA replication during lesion bypass in vivo Science 300 2003 1300 1303
    • (2003) Science , vol.300 , pp. 1300-1303
    • Pages, V.1    Fuchs, R.P.2
  • 35
    • 0034123356 scopus 로고    scopus 로고
    • Multiple genetic pathways for restarting DNA replication forks in Escherichia coli K-12
    • S.J. Sandler Multiple genetic pathways for restarting DNA replication forks in Escherichia coli K-12 Genetics 155 2000 487 497
    • (2000) Genetics , vol.155 , pp. 487-497
    • Sandler, S.J.1
  • 36
    • 0033988501 scopus 로고    scopus 로고
    • Role of PriA in replication fork reactivation in Escherichia coli
    • S.J. Sandler, and K.J. Marians Role of PriA in replication fork reactivation in Escherichia coli J. Bacteriol. 182 2000 9 13
    • (2000) J. Bacteriol. , vol.182 , pp. 9-13
    • Sandler, S.J.1    Marians, K.J.2
  • 37
    • 0029960337 scopus 로고    scopus 로고
    • Differential suppression of priA2::kan phenotypes in Escherichia coli K-12 by mutations in priA, lexA, and dnaC
    • S.J. Sandler, H.S. Samra, and A.J. Clark Differential suppression of priA2::kan phenotypes in Escherichia coli K-12 by mutations in priA, lexA, and dnaC Genetics 143 1996 5 13
    • (1996) Genetics , vol.143 , pp. 5-13
    • Sandler, S.J.1    Samra, H.S.2    Clark, A.J.3
  • 38
    • 0032870793 scopus 로고    scopus 로고
    • DnaC mutations suppress defects in DNA replication- and recombination-associated functions in priB and priC double mutants in Escherichia coli K-12
    • S.J. Sandler, K.J. Marians, K.H. Zavitz, J. Coutu, M.A. Parent, and A.J. Clark dnaC mutations suppress defects in DNA replication- and recombination-associated functions in priB and priC double mutants in Escherichia coli K-12 Mol. Microbiol. 34 1999 91 101
    • (1999) Mol. Microbiol. , vol.34 , pp. 91-101
    • Sandler, S.J.1    Marians, K.J.2    Zavitz, K.H.3    Coutu, J.4    Parent, M.A.5    Clark, A.J.6
  • 39
    • 0034893101 scopus 로고    scopus 로고
    • PriA mutations that affect PriA-PriC function during replication restart
    • S.J. Sandler, J.D. McCool, T.T. Do, and R.U. Johansen PriA mutations that affect PriA-PriC function during replication restart Mol. Microbiol. 41 2001 697 704
    • (2001) Mol. Microbiol. , vol.41 , pp. 697-704
    • Sandler, S.J.1    McCool, J.D.2    Do, T.T.3    Johansen, R.U.4
  • 40
    • 0016737258 scopus 로고
    • Ten proteins required for conversion of θx174 single-stranded DNA to duplex form in vitro. Resolution and reconstitution
    • R. Schekman, J.H. Weiner, A. Weiner, and A. Kornberg Ten proteins required for conversion of θX174 single-stranded DNA to duplex form in vitro. Resolution and reconstitution J. Biol. Chem. 250 1975 5859 5865
    • (1975) J. Biol. Chem. , vol.250 , pp. 5859-5865
    • Schekman, R.1    Weiner, J.H.2    Weiner, A.3    Kornberg, A.4
  • 41
    • 0018867465 scopus 로고
    • An Escherichia coli replication protein that recognizes a unique sequence within a hairpin region in θx174 DNA
    • J. Shlomai, and A. Kornberg An Escherichia coli replication protein that recognizes a unique sequence within a hairpin region in θX174 DNA Proc. Natl. Acad. Sci. USA 77 1980 799 803
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 799-803
    • Shlomai, J.1    Kornberg, A.2
  • 42
    • 0027160455 scopus 로고
    • Primase from Escherichia coli primes single-stranded templates in the absence of single-stranded DNA-binding protein or other auxiliary proteins. Template sequence requirements based on the bacteriophage G4 complementary strand origin and Okazaki fragment initiation sites
    • J.R. Swart, and M.A. Griep Primase from Escherichia coli primes single-stranded templates in the absence of single-stranded DNA-binding protein or other auxiliary proteins. Template sequence requirements based on the bacteriophage G4 complementary strand origin and Okazaki fragment initiation sites J. Biol. Chem. 268 1993 12970 12976
    • (1993) J. Biol. Chem. , vol.268 , pp. 12970-12976
    • Swart, J.R.1    Griep, M.A.2
  • 43
    • 0028049949 scopus 로고
    • Identification of a domain of Escherichia coli primase required for functional interaction with the DnaB helicase at the replication fork
    • K. Tougu, H. Peng, and K.J. Marians Identification of a domain of Escherichia coli primase required for functional interaction with the DnaB helicase at the replication fork J. Biol. Chem. 269 1994 4675 4682
    • (1994) J. Biol. Chem. , vol.269 , pp. 4675-4682
    • Tougu, K.1    Peng, H.2    Marians, K.J.3
  • 44
    • 0037673943 scopus 로고    scopus 로고
    • The Srs2 helicase prevents recombination by disrupting Rad51 nucleoprotein filaments
    • X. Veaute, J. Jeusset, C. Soustelle, S.C. Kowalczykowski, E. Le Cam, and F. Fabre The Srs2 helicase prevents recombination by disrupting Rad51 nucleoprotein filaments Nature 423 2003 309 312
    • (2003) Nature , vol.423 , pp. 309-312
    • Veaute, X.1    Jeusset, J.2    Soustelle, C.3    Kowalczykowski, S.C.4    Le Cam, E.5    Fabre, F.6
  • 45
    • 0016295369 scopus 로고
    • Conversion of θx174 viral DNA to double-stranded form by purified Escherichia coli proteins
    • S. Wickner, and J. Hurwitz Conversion of θX174 viral DNA to double-stranded form by purified Escherichia coli proteins Proc. Natl. Acad. Sci. USA 71 1974 4120 4124
    • (1974) Proc. Natl. Acad. Sci. USA , vol.71 , pp. 4120-4124
    • Wickner, S.1    Hurwitz, J.2
  • 46
    • 0000579776 scopus 로고
    • Interaction of Escherichia coli dnaB and dnaC(D) gene products in vitro
    • S. Wickner, and J. Hurwitz Interaction of Escherichia coli dnaB and dnaC(D) gene products in vitro Proc. Natl. Acad. Sci. USA 72 1975 921 925
    • (1975) Proc. Natl. Acad. Sci. USA , vol.72 , pp. 921-925
    • Wickner, S.1    Hurwitz, J.2
  • 47
    • 0026706674 scopus 로고
    • Coordinated leading- and lagging-strand synthesis at the Escherichia coli DNA replication fork. I. Multiple effectors act to modulate Okazaki fragment size
    • C.A. Wu, E.L. Zechner, and K.J. Marians Coordinated leading- and lagging-strand synthesis at the Escherichia coli DNA replication fork. I. Multiple effectors act to modulate Okazaki fragment size J. Biol. Chem. 267 1992 4030 4044
    • (1992) J. Biol. Chem. , vol.267 , pp. 4030-4044
    • Wu, C.A.1    Zechner, E.L.2    Marians, K.J.3
  • 48
    • 0034677944 scopus 로고    scopus 로고
    • Purification and characterization of DnaC810, a primosomal protein capable of bypassing PriA function
    • L. Xu, and K.J. Marians Purification and characterization of DnaC810, a primosomal protein capable of bypassing PriA function J. Biol. Chem. 275 2000 8196 8205
    • (2000) J. Biol. Chem. , vol.275 , pp. 8196-8205
    • Xu, L.1    Marians, K.J.2
  • 49
    • 0037352498 scopus 로고    scopus 로고
    • PriA mediates DNA replication pathway choice at recombination intermediates
    • L. Xu, and K.J. Marians PriA mediates DNA replication pathway choice at recombination intermediates Mol. Cell 11 2003 817 826
    • (2003) Mol. Cell , vol.11 , pp. 817-826
    • Xu, L.1    Marians, K.J.2
  • 50
    • 0027078134 scopus 로고
    • Bound Lac repressor protein differentially inhibits the unwinding reactions catalyzed by DNA helicases
    • J.E. Yancey-Wrona, and S.W. Matson Bound Lac repressor protein differentially inhibits the unwinding reactions catalyzed by DNA helicases Nucleic Acids Res. 20 1992 6713 6721
    • (1992) Nucleic Acids Res. , vol.20 , pp. 6713-6721
    • Yancey-Wrona, J.E.1    Matson, S.W.2
  • 51
    • 0030595331 scopus 로고    scopus 로고
    • Replisome assembly reveals the basis for asymmetric function in leading and lagging strand replication
    • A. Yuzhakov, J. Turner, and M. O'Donnell Replisome assembly reveals the basis for asymmetric function in leading and lagging strand replication Cell 86 1996 877 886
    • (1996) Cell , vol.86 , pp. 877-886
    • Yuzhakov, A.1    Turner, J.2    O'Donnell, M.3
  • 52
    • 0026726616 scopus 로고
    • ATPase-deficient mutants of the Escherichia coli DNA replication protein PriA are capable of catalyzing the assembly of active primosomes
    • K.H. Zavitz, and K.J. Marians ATPase-deficient mutants of the Escherichia coli DNA replication protein PriA are capable of catalyzing the assembly of active primosomes J. Biol. Chem. 267 1992 6933 6940
    • (1992) J. Biol. Chem. , vol.267 , pp. 6933-6940
    • Zavitz, K.H.1    Marians, K.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.