Institution
Amgen
Company•Thousand Oaks, California, United States•
About: Amgen is a company organization based out in Thousand Oaks, California, United States. It is known for research contribution in the topics: Population & Receptor. The organization has 11948 authors who have published 13790 publications receiving 804432 citations. The organization is also known as: Applied Molecular Genetics & Amgen Inc..
Topics: Population, Receptor, Denosumab, Cancer, Osteoporosis
Papers published on a yearly basis
Papers
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TL;DR: Discovery of the RANK signalling pathway in the osteoclast has provided insight into the mechanisms of osteoporosis and activation of bone resorption, and how hormonal signals impact bone structure and mass.
Abstract: Osteoclasts are specialized cells derived from the monocyte/macrophage haematopoietic lineage that develop and adhere to bone matrix, then secrete acid and lytic enzymes that degrade it in a specialized, extracellular compartment. Discovery of the RANK signalling pathway in the osteoclast has provided insight into the mechanisms of osteoclastogenesis and activation of bone resorption, and how hormonal signals impact bone structure and mass. Further study of this pathway is providing the molecular basis for developing therapeutics to treat osteoporosis and other diseases of bone loss.
5,760 citations
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TL;DR: The effects of OPGL are blocked in vitro and in vivo by OPG, suggesting that OPGl and OPG are key extracellular regulators of osteoclast development.
5,334 citations
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TL;DR: Data show that OPG can act as a soluble factor in the regulation of bone mass and imply a utility for OPG in the treatment of osteoporosis associated with increased osteoclast activity.
5,050 citations
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TL;DR: The data suggest that the OB protein regulates body weight and fat deposition through effects on metabolism and appetite.
Abstract: C57BL/6J mice with a mutation in the obese (ob) gene are obese, diabetic, and exhibit reduced activity, metabolism, and body temperature. Daily intraperitoneal injection of these mice with recombinant OB protein lowered their body weight, percent body fat, food intake, and serum concentrations of glucose and insulin. In addition, metabolic rate, body temperature, and activity levels were increased by this treatment. None of these parameters was altered beyond the level observed in lean controls, suggesting that the OB protein normalized the metabolic status of the ob/ob mice. Lean animals injected with OB protein maintained a smaller weight loss throughout the 28-day study and showed no changes in any of the metabolic parameters. These data suggest that the OB protein regulates body weight and fat deposition through effects on metabolism and appetite.
4,302 citations
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TL;DR: The identification and cloning of an apoptosis-inducing factor, AIF, which is sufficient to induce apoptosis of isolated nuclei is reported, indicating that AIF is a mitochondrial effector of apoptotic cell death.
Abstract: Mitochondria play a key part in the regulation of apoptosis (cell death). Their intermembrane space contains several proteins that are liberated through the outer membrane in order to participate in the degradation phase of apoptosis. Here we report the identification and cloning of an apoptosis-inducing factor, AIF, which is sufficient to induce apoptosis of isolated nuclei. AIF is a flavoprotein of relative molecular mass 57,000 which shares homology with the bacterial oxidoreductases; it is normally confined to mitochondria but translocates to the nucleus when apoptosis is induced. Recombinant AIF causes chromatin condensation in isolated nuclei and large-scale fragmentation of DNA. It induces purified mitochondria to release the apoptogenic proteins cytochrome c and caspase-9. Microinjection of AIF into the cytoplasm of intact cells induces condensation of chromatin, dissipation of the mitochondrial transmembrane potential, and exposure of phosphatidylserine in the plasma membrane. None of these effects is prevented by the wide-ranging caspase inhibitor known as Z-VAD.fmk. Overexpression of Bcl-2, which controls the opening of mitochondrial permeability transition pores, prevents the release of AIF from the mitochondrion but does not affect its apoptogenic activity. These results indicate that AIF is a mitochondrial effector of apoptotic cell death.
4,095 citations
Authors
Showing all 11966 results
Name | H-index | Papers | Citations |
---|---|---|---|
Kari Stefansson | 206 | 794 | 174819 |
Rakesh K. Jain | 200 | 1467 | 177727 |
David L. Kaplan | 177 | 1944 | 146082 |
Unnur Thorsteinsdottir | 167 | 444 | 121009 |
Naveed Sattar | 155 | 1326 | 116368 |
Josef M. Penninger | 154 | 700 | 107295 |
Howard I. Scher | 151 | 944 | 101737 |
Robert O. Bonow | 149 | 808 | 114836 |
Eugene C. Butcher | 146 | 446 | 72849 |
Tasuku Honjo | 141 | 712 | 88428 |
Augustine Kong | 134 | 237 | 89818 |
Ian Ford | 134 | 678 | 85769 |
Christie M. Ballantyne | 132 | 1012 | 77651 |
Bruce R. Blazar | 132 | 1001 | 69622 |
Luigi Tavazzi | 122 | 650 | 71515 |