|1.||Neckers, Len: 26 articles (09/2015 - 01/2002)|
|2.||Workman, Paul: 21 articles (06/2014 - 01/2002)|
|3.||Calderwood, Stuart K: 19 articles (03/2015 - 04/2003)|
|4.||Carver, John A: 9 articles (02/2015 - 07/2004)|
|5.||Gong, Jianlin: 9 articles (12/2014 - 09/2003)|
|6.||Blagg, Brian S J: 8 articles (09/2015 - 09/2006)|
|7.||Mollapour, Mehdi: 8 articles (04/2015 - 06/2010)|
|8.||MacRae, Thomas H: 7 articles (01/2016 - 02/2002)|
|9.||Morimoto, Richard I: 7 articles (09/2015 - 02/2004)|
|10.||Proia, David A: 7 articles (07/2014 - 02/2012)|
|1.||Neurodegenerative Diseases (Neurodegenerative Disease)
03/01/2011 - "Mounting evidence from studies in neurodegenerative disease models shows that molecular chaperones, key regulators of protein aggregation and degradation, play critical roles in the progression of neurodegeneration. "
01/01/2011 - "Not surprisingly, studies involving cell-based and animal models of the neurodegenerative diseases have shown that overexpression of molecular chaperones can provide neuroprotection. "
08/01/2005 - "An increasing number of studies point to important roles for molecular chaperones in the biology of neurodegenerative diseases. "
07/03/2002 - "Here we review recent studies that have revealed a critical role for molecular chaperones in several neurodegenerative disorders."
12/01/1999 - "Our studies indicate that HSP70 or related molecular chaperones may provide a means of treating these and other neurodegenerative diseases associated with abnormal protein conformation and toxicity."
03/05/2010 - "In this study, we report an identification of molecular chaperone Hsc70 (Heat shock cognate protein 70) as a critical mediator of RGS9-2 expression that is specifically recruited to the intrinsically disordered C-terminal domain of RGS9-2 following its dissociation from R7BP. "
06/01/1994 - "Our studies identify EPF as a member of the highly conserved heat-shock family of molecules and demonstrate a molecular chaperone performing an extracellular role."
08/31/2015 - "Here, we identify the molecular chaperone heat shock cognate protein 70 (Hsc70) as a novel Trio regulator. "
05/12/2015 - "The heat shock response (HSR), a transcriptional response that up-regulates molecular chaperones upon heat shock, is necessary for cell survival in a stressful environment to maintain protein homeostasis (proteostasis). "
04/15/2015 - "Heat shock cognate protein 70 (HSC70) is a molecular chaperone that plays essential roles in maintaining the cellular protein homeostasis. "
12/01/2011 - "In this short review, we focus on the molecular interplay between the macroautophagy system and molecular chaperones and highlight the relevance of the pathway mediated by BAG3 to aging and age-associated protein-misfolding diseases."
01/01/2011 - "The molecular chaperone network plays an important defensive role against cellular protein misfolding and has been identified as protective in experimental models of protein misfolding diseases like PD. "
02/01/2004 - "Roles of molecular chaperones in protein misfolding diseases."
01/01/2001 - "It is also characteristic for self-assembly of protein molecules from their unfolded fragments as well as for interaction of molecular chaperones with their substrates and it can be the origin of 'protein misfolding' diseases. "
08/21/2012 - "These data further implicate Hsp70-like molecular chaperones in protein misfolding disorders such as prion disease."
01/01/2012 - "However, most research explores the performance of those molecular chaperones during immune responses or pathological conditions like cancer, whereas the number of studies related to the performance of HSPs in the skin during diverse natural or physiopathological conditions is very low. "
01/01/2010 - "The molecular chaperone Hsp90 is a promising new target in cancer therapy and selective Hsp90 inhibitors are currently in clinical trials. "
02/01/2005 - "This approach builds on recent studies showing that the molecular chaperone Hsp70 can act at multiple stages during tumor antigen presentation to enhance the generation of CD8(+) T lymphocyte-mediated immunity and lead to regression of primary and metastatic tumors."
01/01/2016 - "Hsp60 is a molecular chaperone implicated in carcinogenesis by, for instance, modulating the immune reaction against the tumor. "
10/01/2015 - "The involvement of the molecular chaperone TRAP1 in the regulation of cell motility, although still controversial, has been recently investigated along with some well-characterized roles in cancer cell survival and drug resistance in several tumour types. "
12/01/2004 - "For the molecular chaperones, the consensus gained is that up-regulation of each of the HSPs in the heart is protective against insults such as ischemia/reperfusion (I/R) injury. "
05/01/2000 - "Although future studies of irp94 will be required to clarify the interactions with other intracellular factors inducing ischemia or showing molecular chaperone activity, what is offered here is an insight into its functional role as a component of stress response in neurons that should be considered as a new therapeutic approach for the treatment of ischemia."
03/01/2012 - "These results demonstrated that pre-activation of autophagy by ischemic preconditioning can boost endogenous defense mechanisms to upregulate molecular chaperones, and hence reduce excessive ER stress during fatal ischemia."
09/15/2000 - "In addition, molecular chaperones, especially Hsp70, protect the brain and heart from severe ischemia. "
05/01/2000 - "The results suggest that irp94, like a molecular chaperone, may play a role in protecting the cell against external stimulation, especially after a transient forebrain ischemia. "
|1.||Proteins (Proteins, Gene)
|2.||Heat-Shock Proteins (Heat-Shock Protein)
|6.||Untranslated Regions (Untranslated Region)
|1.||Photochemotherapy (Photodynamic Therapy)
|4.||Heterologous Transplantation (Xenotransplantation)
|5.||Drug Therapy (Chemotherapy)