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Scholar Results 1 - 10 of about 63 citing Ladiges: Pancreatic β-cell failure and diabetes in mice with a deletion mutation of the.... (0.10 sec) 

[PDF] The human obesity gene map: the 2005 update


T Rankinen, A Zuberi, YC Chagnon, SJ Weisnagel, G … - Obesity, 2006 - pbrc.edu
Abstract RANKINEN, TUOMO, AAMIR ZUBERI, YVON C. CHAGNON, S. JOHN
WEISNAGEL, GEORGE ARGYROPOULOS, BRANDON WALTS, LOUIS PE´RUSSE, AND CLAUDE
BOUCHARD. The human obesity gene map: the 2005 update. Obesity. 2006;14: ...
Cited by 335 - Related articles - View as HTML - All 6 versions

Mediators of endoplasmic reticulum stress-induced apoptosis


E Szegezdi, SE Logue, AM Gorman, A Samali - EMBO reports, 2006 - pubmedcentral.nih.gov
The efficient functioning of the endoplasmic reticulum (ER) is essential for most cellular activities
and survival. Conditions that interfere with ER function lead to the accumulation and aggregation
of unfolded proteins. ER transmembrane receptors detect the onset of ER stress and ...
Cited by 207 - Related articles - BL Direct - All 6 versions

[PDF] From acute ER stress to physiological roles of the unfolded protein response


J Wu, RJ Kaufman - Cell death and differentiation, 2006 - microbio.uab.edu
When protein folding in the endoplasmic reticulum (ER) is disrupted by alterations in homeostasis
in the ER lumen, eucaryotic cells activate a series of signal transduction cascades that are collectively
termed the unfolded protein response (UPR). Here we summarize our current ...
Cited by 190 - Related articles - View as HTML - BL Direct - All 6 versions

Endoplasmic reticulum stress signaling in disease

- physiology.org
SJ Marciniak, D Ron - Physiological reviews, 2006 - Am Physiological Soc
The extracellular space is an environment hostile to unmodified polypeptides. For this
reason, many eukaryotic proteins destined for exposure to this environment through secretion
or display at the cell surface require maturation steps within a specialized organelle, the ...
Cited by 182 - Related articles - BL Direct - All 6 versions

[PDF] ER stress and diseases


H Yoshida - FEBS journal, 2007 - human.cornell.edu
Proteins synthesized in the endoplasmic reticulum (ER) are properly folded with the assistance
of ER chaperones. Malfolded proteins are disposed of by ER-associated protein degradation
(ERAD). When the amount of unfolded protein exceeds the folding capacity of the ER, ...
Cited by 155 - Related articles - View as HTML - BL Direct - All 7 versions

Endoplasmic reticulum stress in health and disease

- wustl.edu [PDF] 
L Zhao, SL Ackerman - Current opinion in cell biology, 2006 - Elsevier
Unfolded proteins and other conditions affecting endoplasmic reticulum (ER) homeostasis cause
ER stress. The cell reacts to ER stress by activation of the unfolded protein response (UPR),
which induces profound changes in cellular metabolism including general translation ...
Cited by 101 - Related articles - All 6 versions

ER chaperones in mammalian development and human diseases

- nih.gov
M Ni, AS Lee - FEBS letters, 2007 - Elsevier
The field of endoplasmic reticulum (ER) stress in mammalian cells has expanded rapidly during
the past decade, contributing to understanding of the molecular pathways that allow cells to adapt
to perturbations in ER homeostasis. One major mechanism is mediated by molecular ER ...
Cited by 101 - Related articles - All 10 versions

The role for endoplasmic reticulum stress in diabetes mellitus

- endojournals.org
DL Eizirik, AK Cardozo, M Cnop - Endocrine Reviews, 2008 - Endocrine Soc
Accumulating evidence suggests that endoplasmic reticulum (ER) stress plays a role in the pathogenesis
of diabetes, contributing to pancreatic β-cell loss and insulin resistance. Components of the unfolded
protein response (UPR) play a dual role in β-cells, acting as beneficial regulators under ...
Cited by 93 - Related articles - BL Direct - All 5 versions

Cotranslocational degradation protects the stressed endoplasmic reticulum from …

- cell.com
S Oyadomari, C Yun, EA Fisher, N Kreglinger, G … - Cell, 2006 - Elsevier
The ER's capacity to process proteins is limited, and stress caused by accumulation of unfolded
and misfolded proteins (ER stress) contributes to human disease. ER stress elicits the unfolded
protein response (UPR), whose components attenuate protein synthesis, increase folding ...
Cited by 74 - Related articles - All 16 versions

Endoplasmic reticulum stress gene induction and protection from ischemia/ …

- ahajournals.org
JJ Martindale, R Fernandez, D Thuerauf, R … - Circulation …, 2006 - Am Heart Assoc
Ischemia/reperfusion (I/R) affects the integrity of the endoplasmic reticulum (ER), the site of synthesis
and folding of numerous proteins. Therefore, I/R may activate the unfolded protein response
(UPR), resulting in the induction of a collection of ER stress proteins, many of which are ...
Cited by 48 - Related articles - All 9 versions


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