Pyruvate kinase (French Wikipedia)

Analysis of information sources in references of the Wikipedia article "Pyruvate kinase" in French language version.

refsWebsite

Global rank French rank

3nih.gov

4^th place

12^th place

3doi.org

2^nd place

3^rd place

2acs.org

1,248^th place

778^th place

1harvard.edu

18^th place

118^th place

1asm.org

3,555^th place

1,209^th place

1ashpublications.org

low place

1jci.org

low place

3,702^nd place

1thelancet.com

2,393^rd place

506^th place

acs.org (Global: 1,248^th place; French: 778^th place)

pubs.acs.org

(en) Todd M. Larsen, L. Timothy Laughlin, Hazel M. Holden, Ivan Rayment et George H. Reed, « Structure of Rabbit Muscle Pyruvate Kinase Complexed with Mn2+, K+, and Pyruvate », Biochemistry, vol. 33, n^o 20,‎ mai 1994, p. 6301-6309 (PMID 8193145, DOI 10.1021/bi00186a033, lire en ligne)
(en) David J. Pocalyko, Lawrence J. Carroll, Brian M. Martin, Patricia C. Babbitt et Debra Dunaway-Mariano, « Analysis of sequence homologies in plant and bacterial pyruvate phosphate dikinase, enzyme I of the bacterial phospoenolpyruvate:sugar phosphotransferase system and other PEP-utilizing enzymes. Identification of potential catalytic and regulatory motifs », Biochemistry, vol. 29, n^o 48,‎ décembre 1990, p. 10757-10765 (PMID 2176881, DOI 10.1021/bi00500a006, lire en ligne)

ashpublications.org (Global: low place; French: low place)

Kung C, Hixon J, Kosinski PA et al. AG-348 enhances pyruvate kinase activity in red blood cells from patients with pyruvate kinase deficiency, Blood, 2017;130:1347-1356

asm.org (Global: 3,555^th place; French: 1,209^th place)

ec.asm.org

(en) Natalia A. Liapounova, Vladimir Hampl, Paul M. K. Gordon, Christoph W. Sensen, Lashitew Gedamu et Joel B. Dacks, « Reconstructing the Mosaic Glycolytic Pathway of the Anaerobic Eukaryote Monocercomonoides », Eucaryotic Cell, vol. 5, n^o 12,‎ décembre 2006, p. 2138-2146 (PMID 17071828, PMCID 1694820, DOI 10.1128/EC.00258-06, lire en ligne)

doi.org (Global: 2^nd place; French: 3^rd place)

dx.doi.org

(en) Todd M. Larsen, L. Timothy Laughlin, Hazel M. Holden, Ivan Rayment et George H. Reed, « Structure of Rabbit Muscle Pyruvate Kinase Complexed with Mn2+, K+, and Pyruvate », Biochemistry, vol. 33, n^o 20,‎ mai 1994, p. 6301-6309 (PMID 8193145, DOI 10.1021/bi00186a033, lire en ligne)
(en) David J. Pocalyko, Lawrence J. Carroll, Brian M. Martin, Patricia C. Babbitt et Debra Dunaway-Mariano, « Analysis of sequence homologies in plant and bacterial pyruvate phosphate dikinase, enzyme I of the bacterial phospoenolpyruvate:sugar phosphotransferase system and other PEP-utilizing enzymes. Identification of potential catalytic and regulatory motifs », Biochemistry, vol. 29, n^o 48,‎ décembre 1990, p. 10757-10765 (PMID 2176881, DOI 10.1021/bi00500a006, lire en ligne)
(en) Natalia A. Liapounova, Vladimir Hampl, Paul M. K. Gordon, Christoph W. Sensen, Lashitew Gedamu et Joel B. Dacks, « Reconstructing the Mosaic Glycolytic Pathway of the Anaerobic Eukaryote Monocercomonoides », Eucaryotic Cell, vol. 5, n^o 12,‎ décembre 2006, p. 2138-2146 (PMID 17071828, PMCID 1694820, DOI 10.1128/EC.00258-06, lire en ligne)

harvard.edu (Global: 18^th place; French: 118^th place)

kirschner.med.harvard.edu

(en) Variation d'enthalpie libre, sur le site de Marc Kirschner, Harvard Medical School.

jci.org (Global: low place; French: 3,702^nd place)

Matte A, Federti E, Kung C et al. The pyruvate kinase activator mitapivat reduces hemolysis and improves anemia in a β-thalassemia mouse model, J Clin Invest, 2021;131e144206

nih.gov (Global: 4^th place; French: 12^th place)

ncbi.nlm.nih.gov

(en) Todd M. Larsen, L. Timothy Laughlin, Hazel M. Holden, Ivan Rayment et George H. Reed, « Structure of Rabbit Muscle Pyruvate Kinase Complexed with Mn2+, K+, and Pyruvate », Biochemistry, vol. 33, n^o 20,‎ mai 1994, p. 6301-6309 (PMID 8193145, DOI 10.1021/bi00186a033, lire en ligne)
(en) David J. Pocalyko, Lawrence J. Carroll, Brian M. Martin, Patricia C. Babbitt et Debra Dunaway-Mariano, « Analysis of sequence homologies in plant and bacterial pyruvate phosphate dikinase, enzyme I of the bacterial phospoenolpyruvate:sugar phosphotransferase system and other PEP-utilizing enzymes. Identification of potential catalytic and regulatory motifs », Biochemistry, vol. 29, n^o 48,‎ décembre 1990, p. 10757-10765 (PMID 2176881, DOI 10.1021/bi00500a006, lire en ligne)
(en) Natalia A. Liapounova, Vladimir Hampl, Paul M. K. Gordon, Christoph W. Sensen, Lashitew Gedamu et Joel B. Dacks, « Reconstructing the Mosaic Glycolytic Pathway of the Anaerobic Eukaryote Monocercomonoides », Eucaryotic Cell, vol. 5, n^o 12,‎ décembre 2006, p. 2138-2146 (PMID 17071828, PMCID 1694820, DOI 10.1128/EC.00258-06, lire en ligne)

thelancet.com (Global: 2,393^rd place; French: 506^th place)

Kuo KHM, Layton MD, Lal A et al. Safety and efficacy of mitapivat, an oral pyruvate kinase activator, in adults with non-transfusion dependent α- thalassaemia or β-thalassaemia: an open-label, multicentre, phase 2 study, Lancet, 2022;400:493-501

Pyruvate kinase (French Wikipedia)

acs.org (Global: 1,248th place; French: 778th place)

pubs.acs.org

ashpublications.org (Global: low place; French: low place)

asm.org (Global: 3,555th place; French: 1,209th place)

ec.asm.org

doi.org (Global: 2nd place; French: 3rd place)