Aspartate carbamoyltransferase (English Wikipedia)

Analysis of information sources in references of the Wikipedia article "Aspartate carbamoyltransferase" in English language version.

refsWebsite

Global rank English rank

25nih.gov

4^th place

16doi.org

2^nd place

6harvard.edu

18^th place

17^th place

1semanticscholar.org

11^th place

8^th place

1worldcat.org

5^th place

1proteinscience.org

low place

doi.org

Simmer JP, Kelly RE, Rinker AG, Zimmermann BH, Scully JL, Kim H, Evans DR (Jan 1990). "Mammalian dihydroorotase: nucleotide sequence, peptide sequences, and evolution of the dihydroorotase domain of the multifunctional protein CAD". Proceedings of the National Academy of Sciences of the United States of America. 87 (1): 174–8. Bibcode:1990PNAS...87..174S. doi:10.1073/pnas.87.1.174. PMC 53223. PMID 1967494.
Macol CP, Tsuruta H, Stec B, Kantrowitz ER (May 2001). "Direct structural evidence for a concerted allosteric transition in Escherichia coli aspartate transcarbamoylase". Nature Structural Biology. 8 (5): 423–6. doi:10.1038/87582. PMID 11323717. S2CID 35403933.
Helmstaedt K, Krappmann S, Braus GH (Sep 2001). "Allosteric regulation of catalytic activity: Escherichia coli aspartate transcarbamoylase versus yeast chorismate mutase". Microbiology and Molecular Biology Reviews. 65 (3): 404–21, table of contents. doi:10.1128/MMBR.65.3.404-421.2001. PMC 99034. PMID 11528003.
Ke HM, Honzatko RB, Lipscomb WN (July 1984). "Structure of unligated aspartate carbamoyltransferase of Escherichia coli at 2.6-Å resolution". Proceedings of the National Academy of Sciences of the United States of America. 81 (13): 4037–40. doi:10.1073/pnas.81.13.4037. PMC 345363. PMID 6377306.
Lipscomb WN (1994). "Aspartate transcarbamylase from Escherichia coli: activity and regulation". Advances in Enzymology and Related Areas of Molecular Biology. Advances in Enzymology – and Related Areas of Molecular Biology. Vol. 68. pp. 67–151. doi:10.1002/9780470123140.ch3. ISBN 9780470123140. PMID 8154326.
Kantrowitz ER, Lipscomb WN (Aug 1988). "Escherichia coli aspartate transcarbamylase: the relation between structure and function". Science. 241 (4866): 669–74. Bibcode:1988Sci...241..669K. doi:10.1126/science.3041592. PMID 3041592.
Krause KL, Volz KW, Lipscomb WN (Feb 1987). "2.5 A structure of aspartate carbamoyltransferase complexed with the bisubstrate analog N-(phosphonacetyl)-L-aspartate". Journal of Molecular Biology. 193 (3): 527–53. doi:10.1016/0022-2836(87)90265-8. PMID 3586030.
Wang J, Stieglitz KA, Cardia JP, Kantrowitz ER (Jun 2005). "Structural basis for ordered substrate binding and cooperativity in aspartate transcarbamoylase". Proceedings of the National Academy of Sciences of the United States of America. 102 (25): 8881–6. Bibcode:2005PNAS..102.8881W. doi:10.1073/pnas.0503742102. PMC 1157055. PMID 15951418.
Gouaux JE, Lipscomb WN (Jun 1988). "Three-dimensional structure of carbamoyl phosphate and succinate bound to aspartate carbamoyltransferase". Proceedings of the National Academy of Sciences of the United States of America. 85 (12): 4205–8. Bibcode:1988PNAS...85.4205G. doi:10.1073/pnas.85.12.4205. PMC 280395. PMID 3380787.
Kantrowitz ER, Lipscomb WN (Feb 1990). "Escherichia coli aspartate transcarbamoylase: the molecular basis for a concerted allosteric transition". Trends in Biochemical Sciences. 15 (2): 53–9. doi:10.1016/0968-0004(90)90176-C. PMID 2186515.
Fetler L, Vachette P, Hervé G, Ladjimi MM (Dec 1995). "Unlike the quaternary structure transition, the tertiary structure change of the 240s loop in allosteric aspartate transcarbamylase requires active site saturation by substrate for completion". Biochemistry. 34 (48): 15654–60. doi:10.1021/bi00048a008. PMID 7495794.
Middleton SA, Kantrowitz ER (Aug 1986). "Importance of the loop at residues 230–245 in the allosteric interactions of Escherichia coli aspartate carbamoyltransferase". Proceedings of the National Academy of Sciences of the United States of America. 83 (16): 5866–70. Bibcode:1986PNAS...83.5866M. doi:10.1073/pnas.83.16.5866. PMC 386397. PMID 3526342.
Newton CJ, Stevens RC, Kantrowitz ER (Mar 1992). "Importance of a conserved residue, aspartate-162, for the function of Escherichia coli aspartate transcarbamoylase". Biochemistry. 31 (11): 3026–32. doi:10.1021/bi00126a026. PMID 1550826.
Fetler L, Tauc P, Baker DP, Macol CP, Kantrowitz ER, Vachette P (May 2002). "Replacement of Asp-162 by Ala prevents the cooperative transition by the substrates while enhancing the effect of the allosteric activator ATP on E. coli aspartate transcarbamoylase". Protein Science. 11 (5): 1074–81. doi:10.1110/ps.4500102. PMC 2373563. PMID 11967364.
Marsh JA, Hernández H, Hall Z, Ahnert SE, Perica T, Robinson CV, Teichmann SA (Apr 2013). "Protein complexes are under evolutionary selection to assemble via ordered pathways". Cell. 153 (2): 461–470. doi:10.1016/j.cell.2013.02.044. PMC 4009401. PMID 23582331.
Evans DR, Pastra-Landis SC, Lipscomb WN (Apr 1974). "An intermediate complex in the dissociation of aspartate transcarbamylase". Proceedings of the National Academy of Sciences of the United States of America. 71 (4): 1351–5. Bibcode:1974PNAS...71.1351E. doi:10.1073/pnas.71.4.1351. PMC 388226. PMID 4598300.

harvard.edu

ui.adsabs.harvard.edu

Simmer JP, Kelly RE, Rinker AG, Zimmermann BH, Scully JL, Kim H, Evans DR (Jan 1990). "Mammalian dihydroorotase: nucleotide sequence, peptide sequences, and evolution of the dihydroorotase domain of the multifunctional protein CAD". Proceedings of the National Academy of Sciences of the United States of America. 87 (1): 174–8. Bibcode:1990PNAS...87..174S. doi:10.1073/pnas.87.1.174. PMC 53223. PMID 1967494.
Kantrowitz ER, Lipscomb WN (Aug 1988). "Escherichia coli aspartate transcarbamylase: the relation between structure and function". Science. 241 (4866): 669–74. Bibcode:1988Sci...241..669K. doi:10.1126/science.3041592. PMID 3041592.
Wang J, Stieglitz KA, Cardia JP, Kantrowitz ER (Jun 2005). "Structural basis for ordered substrate binding and cooperativity in aspartate transcarbamoylase". Proceedings of the National Academy of Sciences of the United States of America. 102 (25): 8881–6. Bibcode:2005PNAS..102.8881W. doi:10.1073/pnas.0503742102. PMC 1157055. PMID 15951418.
Gouaux JE, Lipscomb WN (Jun 1988). "Three-dimensional structure of carbamoyl phosphate and succinate bound to aspartate carbamoyltransferase". Proceedings of the National Academy of Sciences of the United States of America. 85 (12): 4205–8. Bibcode:1988PNAS...85.4205G. doi:10.1073/pnas.85.12.4205. PMC 280395. PMID 3380787.
Middleton SA, Kantrowitz ER (Aug 1986). "Importance of the loop at residues 230–245 in the allosteric interactions of Escherichia coli aspartate carbamoyltransferase". Proceedings of the National Academy of Sciences of the United States of America. 83 (16): 5866–70. Bibcode:1986PNAS...83.5866M. doi:10.1073/pnas.83.16.5866. PMC 386397. PMID 3526342.
Evans DR, Pastra-Landis SC, Lipscomb WN (Apr 1974). "An intermediate complex in the dissociation of aspartate transcarbamylase". Proceedings of the National Academy of Sciences of the United States of America. 71 (4): 1351–5. Bibcode:1974PNAS...71.1351E. doi:10.1073/pnas.71.4.1351. PMC 388226. PMID 4598300.

nih.gov

pubmed.ncbi.nlm.nih.gov

Simmer JP, Kelly RE, Rinker AG, Zimmermann BH, Scully JL, Kim H, Evans DR (Jan 1990). "Mammalian dihydroorotase: nucleotide sequence, peptide sequences, and evolution of the dihydroorotase domain of the multifunctional protein CAD". Proceedings of the National Academy of Sciences of the United States of America. 87 (1): 174–8. Bibcode:1990PNAS...87..174S. doi:10.1073/pnas.87.1.174. PMC 53223. PMID 1967494.
Macol CP, Tsuruta H, Stec B, Kantrowitz ER (May 2001). "Direct structural evidence for a concerted allosteric transition in Escherichia coli aspartate transcarbamoylase". Nature Structural Biology. 8 (5): 423–6. doi:10.1038/87582. PMID 11323717. S2CID 35403933.
Helmstaedt K, Krappmann S, Braus GH (Sep 2001). "Allosteric regulation of catalytic activity: Escherichia coli aspartate transcarbamoylase versus yeast chorismate mutase". Microbiology and Molecular Biology Reviews. 65 (3): 404–21, table of contents. doi:10.1128/MMBR.65.3.404-421.2001. PMC 99034. PMID 11528003.
Ke HM, Honzatko RB, Lipscomb WN (July 1984). "Structure of unligated aspartate carbamoyltransferase of Escherichia coli at 2.6-Å resolution". Proceedings of the National Academy of Sciences of the United States of America. 81 (13): 4037–40. doi:10.1073/pnas.81.13.4037. PMC 345363. PMID 6377306.
Lipscomb WN (1994). "Aspartate transcarbamylase from Escherichia coli: activity and regulation". Advances in Enzymology and Related Areas of Molecular Biology. Advances in Enzymology – and Related Areas of Molecular Biology. Vol. 68. pp. 67–151. doi:10.1002/9780470123140.ch3. ISBN 9780470123140. PMID 8154326.
Kantrowitz ER, Lipscomb WN (Aug 1988). "Escherichia coli aspartate transcarbamylase: the relation between structure and function". Science. 241 (4866): 669–74. Bibcode:1988Sci...241..669K. doi:10.1126/science.3041592. PMID 3041592.
Krause KL, Volz KW, Lipscomb WN (Feb 1987). "2.5 A structure of aspartate carbamoyltransferase complexed with the bisubstrate analog N-(phosphonacetyl)-L-aspartate". Journal of Molecular Biology. 193 (3): 527–53. doi:10.1016/0022-2836(87)90265-8. PMID 3586030.
Wang J, Stieglitz KA, Cardia JP, Kantrowitz ER (Jun 2005). "Structural basis for ordered substrate binding and cooperativity in aspartate transcarbamoylase". Proceedings of the National Academy of Sciences of the United States of America. 102 (25): 8881–6. Bibcode:2005PNAS..102.8881W. doi:10.1073/pnas.0503742102. PMC 1157055. PMID 15951418.
Gouaux JE, Lipscomb WN (Jun 1988). "Three-dimensional structure of carbamoyl phosphate and succinate bound to aspartate carbamoyltransferase". Proceedings of the National Academy of Sciences of the United States of America. 85 (12): 4205–8. Bibcode:1988PNAS...85.4205G. doi:10.1073/pnas.85.12.4205. PMC 280395. PMID 3380787.
Kantrowitz ER, Lipscomb WN (Feb 1990). "Escherichia coli aspartate transcarbamoylase: the molecular basis for a concerted allosteric transition". Trends in Biochemical Sciences. 15 (2): 53–9. doi:10.1016/0968-0004(90)90176-C. PMID 2186515.
Fetler L, Vachette P, Hervé G, Ladjimi MM (Dec 1995). "Unlike the quaternary structure transition, the tertiary structure change of the 240s loop in allosteric aspartate transcarbamylase requires active site saturation by substrate for completion". Biochemistry. 34 (48): 15654–60. doi:10.1021/bi00048a008. PMID 7495794.
Middleton SA, Kantrowitz ER (Aug 1986). "Importance of the loop at residues 230–245 in the allosteric interactions of Escherichia coli aspartate carbamoyltransferase". Proceedings of the National Academy of Sciences of the United States of America. 83 (16): 5866–70. Bibcode:1986PNAS...83.5866M. doi:10.1073/pnas.83.16.5866. PMC 386397. PMID 3526342.
Newton CJ, Stevens RC, Kantrowitz ER (Mar 1992). "Importance of a conserved residue, aspartate-162, for the function of Escherichia coli aspartate transcarbamoylase". Biochemistry. 31 (11): 3026–32. doi:10.1021/bi00126a026. PMID 1550826.
Fetler L, Tauc P, Baker DP, Macol CP, Kantrowitz ER, Vachette P (May 2002). "Replacement of Asp-162 by Ala prevents the cooperative transition by the substrates while enhancing the effect of the allosteric activator ATP on E. coli aspartate transcarbamoylase". Protein Science. 11 (5): 1074–81. doi:10.1110/ps.4500102. PMC 2373563. PMID 11967364.
Marsh JA, Hernández H, Hall Z, Ahnert SE, Perica T, Robinson CV, Teichmann SA (Apr 2013). "Protein complexes are under evolutionary selection to assemble via ordered pathways". Cell. 153 (2): 461–470. doi:10.1016/j.cell.2013.02.044. PMC 4009401. PMID 23582331.
Evans DR, Pastra-Landis SC, Lipscomb WN (Apr 1974). "An intermediate complex in the dissociation of aspartate transcarbamylase". Proceedings of the National Academy of Sciences of the United States of America. 71 (4): 1351–5. Bibcode:1974PNAS...71.1351E. doi:10.1073/pnas.71.4.1351. PMC 388226. PMID 4598300.

ncbi.nlm.nih.gov

Simmer JP, Kelly RE, Rinker AG, Zimmermann BH, Scully JL, Kim H, Evans DR (Jan 1990). "Mammalian dihydroorotase: nucleotide sequence, peptide sequences, and evolution of the dihydroorotase domain of the multifunctional protein CAD". Proceedings of the National Academy of Sciences of the United States of America. 87 (1): 174–8. Bibcode:1990PNAS...87..174S. doi:10.1073/pnas.87.1.174. PMC 53223. PMID 1967494.
Helmstaedt K, Krappmann S, Braus GH (Sep 2001). "Allosteric regulation of catalytic activity: Escherichia coli aspartate transcarbamoylase versus yeast chorismate mutase". Microbiology and Molecular Biology Reviews. 65 (3): 404–21, table of contents. doi:10.1128/MMBR.65.3.404-421.2001. PMC 99034. PMID 11528003.
Ke HM, Honzatko RB, Lipscomb WN (July 1984). "Structure of unligated aspartate carbamoyltransferase of Escherichia coli at 2.6-Å resolution". Proceedings of the National Academy of Sciences of the United States of America. 81 (13): 4037–40. doi:10.1073/pnas.81.13.4037. PMC 345363. PMID 6377306.
Wang J, Stieglitz KA, Cardia JP, Kantrowitz ER (Jun 2005). "Structural basis for ordered substrate binding and cooperativity in aspartate transcarbamoylase". Proceedings of the National Academy of Sciences of the United States of America. 102 (25): 8881–6. Bibcode:2005PNAS..102.8881W. doi:10.1073/pnas.0503742102. PMC 1157055. PMID 15951418.
Gouaux JE, Lipscomb WN (Jun 1988). "Three-dimensional structure of carbamoyl phosphate and succinate bound to aspartate carbamoyltransferase". Proceedings of the National Academy of Sciences of the United States of America. 85 (12): 4205–8. Bibcode:1988PNAS...85.4205G. doi:10.1073/pnas.85.12.4205. PMC 280395. PMID 3380787.
Middleton SA, Kantrowitz ER (Aug 1986). "Importance of the loop at residues 230–245 in the allosteric interactions of Escherichia coli aspartate carbamoyltransferase". Proceedings of the National Academy of Sciences of the United States of America. 83 (16): 5866–70. Bibcode:1986PNAS...83.5866M. doi:10.1073/pnas.83.16.5866. PMC 386397. PMID 3526342.
Fetler L, Tauc P, Baker DP, Macol CP, Kantrowitz ER, Vachette P (May 2002). "Replacement of Asp-162 by Ala prevents the cooperative transition by the substrates while enhancing the effect of the allosteric activator ATP on E. coli aspartate transcarbamoylase". Protein Science. 11 (5): 1074–81. doi:10.1110/ps.4500102. PMC 2373563. PMID 11967364.
Marsh JA, Hernández H, Hall Z, Ahnert SE, Perica T, Robinson CV, Teichmann SA (Apr 2013). "Protein complexes are under evolutionary selection to assemble via ordered pathways". Cell. 153 (2): 461–470. doi:10.1016/j.cell.2013.02.044. PMC 4009401. PMID 23582331.
Evans DR, Pastra-Landis SC, Lipscomb WN (Apr 1974). "An intermediate complex in the dissociation of aspartate transcarbamylase". Proceedings of the National Academy of Sciences of the United States of America. 71 (4): 1351–5. Bibcode:1974PNAS...71.1351E. doi:10.1073/pnas.71.4.1351. PMC 388226. PMID 4598300.

proteinscience.org

Fetler L, Tauc P, Baker DP, Macol CP, Kantrowitz ER, Vachette P (May 2002). "Replacement of Asp-162 by Ala prevents the cooperative transition by the substrates while enhancing the effect of the allosteric activator ATP on E. coli aspartate transcarbamoylase". Protein Science. 11 (5): 1074–81. doi:10.1110/ps.4500102. PMC 2373563. PMID 11967364.

semanticscholar.org

api.semanticscholar.org

Macol CP, Tsuruta H, Stec B, Kantrowitz ER (May 2001). "Direct structural evidence for a concerted allosteric transition in Escherichia coli aspartate transcarbamoylase". Nature Structural Biology. 8 (5): 423–6. doi:10.1038/87582. PMID 11323717. S2CID 35403933.

worldcat.org

Alberts, Bruce, author. Molecular biology of the cell. ISBN 978-1-315-73536-8. OCLC 1082214404. {{cite book}}: |last= has generic name (help)CS1 maint: multiple names: authors list (link)