Nucleoside-phosphate kinase (English Wikipedia)

Analysis of information sources in references of the Wikipedia article "Nucleoside-phosphate kinase" in English language version.

refsWebsite

Global rank English rank

12doi.org

2^nd place

12nih.gov

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3semanticscholar.org

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8^th place

2harvard.edu

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1archive.org

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archive.org

Berg JM, Tymoczko JL, Stryer L (2002). Biochemistry. New York: W H Freeman. ISBN 0-7167-3051-0. Retrieved 2016-01-08.

doi.org

Ayengar P, Gibson DM, Sanadi DR (July 1956). "Transphosphorylations between nucleoside phosphates". Biochimica et Biophysica Acta. 21 (1): 86–91. doi:10.1016/0006-3002(56)90096-8. PMID 13363863.
Lieberman I, Kornberg A, Simms ES (July 1955). "Enzymatic synthesis of nucleoside diphosphates and triphosphates". The Journal of Biological Chemistry. 215 (1): 429–40. doi:10.1016/S0021-9258(18)66050-8. PMID 14392176.
Heppel LA, Strominger JL, Maxwell ES (April 1959). "Nucleoside monophosphate kinases. II. Transphosphorylation between adenosine monophosphate and nucleoside triphosphates". Biochimica et Biophysica Acta. 32: 422–30. doi:10.1016/0006-3002(59)90615-8. PMID 14401179.
Dreusicke D, Schulz GE (November 1986). "The glycine-rich loop of adenylate kinase forms a giant anion hole". FEBS Letters. 208 (2): 301–4. Bibcode:1986FEBSL.208..301D. doi:10.1016/0014-5793(86)81037-7. PMID 3023140. S2CID 11786335.
Byeon L, Shi Z, Tsai MD (March 1995). "Mechanism of adenylate kinase. The "essential lysine" helps to orient the phosphates and the active site residues to proper conformations". Biochemistry. 34 (10): 3172–82. doi:10.1021/bi00010a006. PMID 7880812.
Müller CW, Schlauderer GJ, Reinstein J, Schulz GE (February 1996). "Adenylate kinase motions during catalysis: an energetic counterweight balancing substrate binding". Structure. 4 (2): 147–56. doi:10.2210/pdb4ake/pdb. PMID 8805521.
Krishnamurthy H, Lou H, Kimple A, Vieille C, Cukier RI (January 2005). "Associative mechanism for phosphoryl transfer: a molecular dynamics simulation of Escherichia coli adenylate kinase complexed with its substrates". Proteins. 58 (1): 88–100. doi:10.1002/prot.20301. PMID 15521058. S2CID 20874015.
Pai EF, Sachsenheimer W, Schirmer RH, Schulz GE (July 1977). "Substrate positions and induced-fit in crystalline adenylate kinase". Journal of Molecular Biology. 114 (1): 37–45. doi:10.1016/0022-2836(77)90281-9. PMID 198550.
Müller CW, Schulz GE (March 1992). "Structure of the complex between adenylate kinase from Escherichia coli and the inhibitor Ap5A refined at 1.9 A resolution. A model for a catalytic transition state". Journal of Molecular Biology. 224 (1): 159–77. doi:10.2210/pdb1ake/pdb. PMID 1548697.
Schlauderer GJ, Proba K, Schulz GE (February 1996). "Structure of a mutant adenylate kinase ligated with an ATP-analogue showing domain closure over ATP". Journal of Molecular Biology. 256 (2): 223–7. doi:10.1006/jmbi.1996.0080. PMID 8594191.
Vonrhein C, Schlauderer GJ, Schulz GE (May 1995). "Movie of the structural changes during a catalytic cycle of nucleoside monophosphate kinases". Structure. 3 (5): 483–90. doi:10.1016/s0969-2126(01)00181-2. PMID 7663945.
Fukami-Kobayashi K, Nosaka M, Nakazawa A, Go M (May 1996). "Ancient divergence of long and short isoforms of adenylate kinase: molecular evolution of the nucleoside monophosphate kinase family". FEBS Letters. 385 (3): 214–20. Bibcode:1996FEBSL.385..214F. doi:10.1016/0014-5793(96)00367-5. PMID 8647254. S2CID 24934783.

harvard.edu

ui.adsabs.harvard.edu

Dreusicke D, Schulz GE (November 1986). "The glycine-rich loop of adenylate kinase forms a giant anion hole". FEBS Letters. 208 (2): 301–4. Bibcode:1986FEBSL.208..301D. doi:10.1016/0014-5793(86)81037-7. PMID 3023140. S2CID 11786335.
Fukami-Kobayashi K, Nosaka M, Nakazawa A, Go M (May 1996). "Ancient divergence of long and short isoforms of adenylate kinase: molecular evolution of the nucleoside monophosphate kinase family". FEBS Letters. 385 (3): 214–20. Bibcode:1996FEBSL.385..214F. doi:10.1016/0014-5793(96)00367-5. PMID 8647254. S2CID 24934783.

nih.gov

pubmed.ncbi.nlm.nih.gov

Ayengar P, Gibson DM, Sanadi DR (July 1956). "Transphosphorylations between nucleoside phosphates". Biochimica et Biophysica Acta. 21 (1): 86–91. doi:10.1016/0006-3002(56)90096-8. PMID 13363863.
Lieberman I, Kornberg A, Simms ES (July 1955). "Enzymatic synthesis of nucleoside diphosphates and triphosphates". The Journal of Biological Chemistry. 215 (1): 429–40. doi:10.1016/S0021-9258(18)66050-8. PMID 14392176.
Heppel LA, Strominger JL, Maxwell ES (April 1959). "Nucleoside monophosphate kinases. II. Transphosphorylation between adenosine monophosphate and nucleoside triphosphates". Biochimica et Biophysica Acta. 32: 422–30. doi:10.1016/0006-3002(59)90615-8. PMID 14401179.
Dreusicke D, Schulz GE (November 1986). "The glycine-rich loop of adenylate kinase forms a giant anion hole". FEBS Letters. 208 (2): 301–4. Bibcode:1986FEBSL.208..301D. doi:10.1016/0014-5793(86)81037-7. PMID 3023140. S2CID 11786335.
Byeon L, Shi Z, Tsai MD (March 1995). "Mechanism of adenylate kinase. The "essential lysine" helps to orient the phosphates and the active site residues to proper conformations". Biochemistry. 34 (10): 3172–82. doi:10.1021/bi00010a006. PMID 7880812.
Müller CW, Schlauderer GJ, Reinstein J, Schulz GE (February 1996). "Adenylate kinase motions during catalysis: an energetic counterweight balancing substrate binding". Structure. 4 (2): 147–56. doi:10.2210/pdb4ake/pdb. PMID 8805521.
Krishnamurthy H, Lou H, Kimple A, Vieille C, Cukier RI (January 2005). "Associative mechanism for phosphoryl transfer: a molecular dynamics simulation of Escherichia coli adenylate kinase complexed with its substrates". Proteins. 58 (1): 88–100. doi:10.1002/prot.20301. PMID 15521058. S2CID 20874015.
Pai EF, Sachsenheimer W, Schirmer RH, Schulz GE (July 1977). "Substrate positions and induced-fit in crystalline adenylate kinase". Journal of Molecular Biology. 114 (1): 37–45. doi:10.1016/0022-2836(77)90281-9. PMID 198550.
Müller CW, Schulz GE (March 1992). "Structure of the complex between adenylate kinase from Escherichia coli and the inhibitor Ap5A refined at 1.9 A resolution. A model for a catalytic transition state". Journal of Molecular Biology. 224 (1): 159–77. doi:10.2210/pdb1ake/pdb. PMID 1548697.
Schlauderer GJ, Proba K, Schulz GE (February 1996). "Structure of a mutant adenylate kinase ligated with an ATP-analogue showing domain closure over ATP". Journal of Molecular Biology. 256 (2): 223–7. doi:10.1006/jmbi.1996.0080. PMID 8594191.
Vonrhein C, Schlauderer GJ, Schulz GE (May 1995). "Movie of the structural changes during a catalytic cycle of nucleoside monophosphate kinases". Structure. 3 (5): 483–90. doi:10.1016/s0969-2126(01)00181-2. PMID 7663945.
Fukami-Kobayashi K, Nosaka M, Nakazawa A, Go M (May 1996). "Ancient divergence of long and short isoforms of adenylate kinase: molecular evolution of the nucleoside monophosphate kinase family". FEBS Letters. 385 (3): 214–20. Bibcode:1996FEBSL.385..214F. doi:10.1016/0014-5793(96)00367-5. PMID 8647254. S2CID 24934783.

semanticscholar.org

api.semanticscholar.org

Dreusicke D, Schulz GE (November 1986). "The glycine-rich loop of adenylate kinase forms a giant anion hole". FEBS Letters. 208 (2): 301–4. Bibcode:1986FEBSL.208..301D. doi:10.1016/0014-5793(86)81037-7. PMID 3023140. S2CID 11786335.
Krishnamurthy H, Lou H, Kimple A, Vieille C, Cukier RI (January 2005). "Associative mechanism for phosphoryl transfer: a molecular dynamics simulation of Escherichia coli adenylate kinase complexed with its substrates". Proteins. 58 (1): 88–100. doi:10.1002/prot.20301. PMID 15521058. S2CID 20874015.
Fukami-Kobayashi K, Nosaka M, Nakazawa A, Go M (May 1996). "Ancient divergence of long and short isoforms of adenylate kinase: molecular evolution of the nucleoside monophosphate kinase family". FEBS Letters. 385 (3): 214–20. Bibcode:1996FEBSL.385..214F. doi:10.1016/0014-5793(96)00367-5. PMID 8647254. S2CID 24934783.