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Table representation of search results timeline featuring number of search results per year.

Year Number of Results
1946 1
1947 1
1948 5
1949 3
1950 3
1952 1
1953 7
1954 16
1955 12
1956 10
1957 18
1958 31
1959 79
1960 93
1961 84
1962 109
1963 189
1964 195
1965 160
1966 209
1967 244
1968 274
1969 264
1970 251
1971 259
1972 230
1973 238
1974 239
1975 209
1976 171
1977 143
1978 107
1979 113
1980 107
1981 92
1982 80
1983 86
1984 78
1985 91
1986 70
1987 75
1988 72
1989 62
1990 89
1991 74
1992 69
1993 70
1994 56
1995 69
1996 56
1997 62
1998 43
1999 53
2000 63
2001 66
2002 55
2003 62
2004 68
2005 63
2006 68
2007 68
2008 72
2009 58
2010 47
2011 59
2012 67
2013 51
2014 67
2015 53
2016 39
2017 58
2018 51
2019 31
2020 0
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6,483 results
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Page 1
Fructose-1,6-bisphosphate and aldolase mediate glucose sensing by AMPK.
Zhang CS, et al. Nature 2017. PMID 28723898 Free PMC article.
Here, we describe an AMP/ADP-independent mechanism that triggers AMPK activation by sensing the absence of fructose-1,6-bisphosphate (FBP), with AMPK being progressively activated as extracellular glucose and intracellular FBP decrease. ...These results establish that aldolase, as well as being a glycolytic enzyme, is a sensor of glucose availability that regulates AMPK....
Here, we describe an AMP/ADP-independent mechanism that triggers AMPK activation by sensing the absence of fructose-1,6-bisphospha
The metabolic enzyme fructose-1,6-bisphosphate aldolase acts as a transcriptional regulator in pathogenic Francisella.
Ziveri J, et al. Nat Commun 2017. PMID 29021545 Free PMC article.
Here, we address the role of fructose-bisphosphate aldolase in the bacterial pathogen Francisella novicida. We demonstrate that fructose-bisphosphate aldolase is important for bacterial multiplication in macrophages in the presence of gluconeogenic substrates. ...We propose a model in which fructose-bisphosphate aldolase participates in the control of host redox homeostasis and the inflammatory immune response.The enzyme fructose-bisphosphate aldolase (FBA) plays central roles in glycolysis and gluconeogenesis. ...
Here, we address the role of fructose-bisphosphate aldolase in the bacterial pathogen Francisella novicida. We demonstr …
Fructose-1,6-bisphosphate aldolase of Mycoplasma bovis is a plasminogen-binding adhesin.
Gao X, et al. Microb Pathog 2018. PMID 30142464
Fructose-1,6-bisphosphate aldolase (FBA), a key enzyme in the glycolytic pathway, is a multifunctional protein in several pathogenic bacterial species, but its role in M. bovis remains unknown. ...
Fructose-1,6-bisphosphate aldolase (FBA), a key enzyme in the glycolytic pathway, is a multifunctional protein in sever
High expression of fructose-bisphosphate aldolase A induces progression of renal cell carcinoma.
Huang Z, et al. Oncol Rep 2018. PMID 29693182
Aldolase A (fructose-bisphosphate aldolase A, ALDOA) is a glycolytic enzyme that catalyzes reversible conversion of fructose‑1,6-bisphosphate to glyceraldehyde 3-phosphate and dihydroxyacetone phosphate. ...
Aldolase A (fructose-bisphosphate aldolase A, ALDOA) is a glycolytic enzyme that catalyzes reversible conversion
Aldolase B-Mediated Fructose Metabolism Drives Metabolic Reprogramming of Colon Cancer Liver Metastasis.
Bu P, et al. Cell Metab 2018. PMID 29706565 Free PMC article.
In particular, via GATA6, metastatic cells in the liver upregulate the enzyme aldolase B (ALDOB), which enhances fructose metabolism and provides fuel for major pathways of central carbon metabolism during tumor cell proliferation. Targeting ALDOB or reducing dietary fructose significantly reduces liver metastatic growth but has little effect on the primary tumor. ...
In particular, via GATA6, metastatic cells in the liver upregulate the enzyme aldolase B (ALDOB), which enhances fructose meta …
Fructose-1,6-bisphosphate aldolase encoded by a core gene of Mycoplasma hyopneumoniae contributes to host cell adhesion.
Yu Y, et al. Vet Res 2018. PMID 30454073 Free PMC article.
The most differentially abundant of the seven, fructose-1,6-bisphosphate aldolase (FBA), was successfully cloned, expressed and purified. ...
The most differentially abundant of the seven, fructose-1,6-bisphosphate aldolase (FBA), was successfully cloned, expre …
Pcal_0111, a highly thermostable bifunctional fructose-1,6-bisphosphate aldolase/phosphatase from Pyrobaculum calidifontis.
Aziz I, et al. Extremophiles 2017. PMID 28299451
Pyrobaculum calidifontis genome harbors an open reading frame Pcal_0111 annotated as fructose bisphosphate aldolase. Although the gene is annotated as fructose bisphosphate aldolase, it exhibits a high homology with previously reported fructose-1,6-bisphosphate aldolase/phosphatase from Thermoproteus neutrophilus. ...High thermostability and inhibition by ATP make Pcal_0111 a unique fructose 1,6-bisphosphatase/aldolase....
Pyrobaculum calidifontis genome harbors an open reading frame Pcal_0111 annotated as fructose bisphosphate aldolase. Al …
Fructose-1,6-bisphosphate aldolase is involved in Mycoplasma bovis colonization as a fibronectin-binding adhesin.
Huang J, et al. Res Vet Sci 2019. PMID 30852357
The aims of this study were to investigate the Fn-binding properties of M. bovis fructose-1,6-bisphosphate aldolase (FBA) and evaluate its role as a cell adhesion factor during mycoplasma colonization. ...The purified recombinant FBA (rFBA) was shown to have fructose bisphosphate aldolase activity. Western blot indicated that FBA was an antigenically conserved protein in several M. bovis strains. ...
The aims of this study were to investigate the Fn-binding properties of M. bovis fructose-1,6-bisphosphate aldolase (FB …
Fructose 1,6-Bisphosphate Aldolase, a Novel Immunogenic Surface Protein on Listeria Species.
Mendonça M, et al. PLoS One 2016. PMID 27489951 Free PMC article.
In the present work, using mass spectrometry and genetic cloning, we show that fructose-1,6-bisphosphate aldolase (FBA) class II in Listeria species is the antigen target of the previously described mAb-3F8. ...
In the present work, using mass spectrometry and genetic cloning, we show that fructose-1,6-bisphosphate aldolase (FBA) …
Characterization and localization of Opisthorchis viverrini fructose-1,6-bisphosphate aldolase.
Prompipak J, et al. Parasitol Int 2017. PMID 27265876
In this study, an important enzyme in the Ov glycolytic pathway, fructose-1,6-bisphosphate aldolase (FBPA), that had been obtained from a previous study was characterized and immunolocalized. ...
In this study, an important enzyme in the Ov glycolytic pathway, fructose-1,6-bisphosphate aldolase (FBPA), that had be …
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