Results 11 to 20 of about 28,252 (277)

Conformational Stability of Calreticulin [PDF]

open access: yesProtein & Peptide Letters, 2005
The conformational stability of calreticulin was investigated. Apparent unfolding temperatures (Tm) increased from 31 degrees C at pH 5 to 51 degrees C at pH 9, but electrophoretic analysis revealed that calreticulin oligomerized instead of unfolding.
Jørgensen, Charlotte S   +8 more
openaire   +4 more sources

Calreticulin: Challenges Posed by the Intrinsically Disordered Nature of Calreticulin to the Study of Its Function [PDF]

open access: yesFrontiers in Cell and Developmental Biology, 2017
Calreticulin is a Ca2+-binding chaperone protein, which resides mainly in the endoplasmic reticulum but also found in other cellular compartments including the plasma membrane. In addition to Ca2+, calreticulin binds and regulates almost all proteins and
Lilian Varricchio   +8 more
doaj   +3 more sources

Distinct clinical characteristics of myeloproliferative neoplasms with calreticulin mutations [PDF]

open access: yesHaematologica, 2014
Somatic insertions/deletions in the calreticulin gene have recently been discovered to be causative alterations in myeloproliferative neoplasms. A combination of qualitative and quantitative allele-specific polymerase chain reaction, fragment-sizing ...
Hajnalka Andrikovics   +13 more
doaj   +3 more sources

Calreticulin Is Essential for Cardiac Development [PDF]

open access: yesThe Journal of Cell Biology, 1999
Calreticulin is a ubiquitous Ca2+ binding protein, located in the endoplasmic reticulum lumen, which has been implicated in many diverse functions including: regulation of intracellular Ca2+ homeostasis, chaperone activity, steroid-mediated gene regulation, and cell adhesion.
Mesaeli, N.   +8 more
openaire   +5 more sources

Chemical and Thermal Unfolding of Calreticulin [PDF]

open access: yesProtein & Peptide Letters, 2013
Calreticulin is a soluble endoplasmic reticulum chaperone, which has a relatively low melting point due to its remarkable structure with a relatively high content of flexible structural elements. Using far ultraviolet circular dichroism (CD) spectroscopy and a fluorescent dye binding thermal shift assay, we have investigated the chemical and thermal ...
Duus, K.   +7 more
openaire   +3 more sources

INS-1E with Calreticulin-YFP [PDF]

open access: yes, 2016
CLEM and ECT<strong>Tilt Series Date:</strong> 2016-04-17</p> <strong>Data Taken By:</strong> Shrawan kumar Mageswaran</p> <strong>Species / Specimen:</strong> INS-1E Pancreatic Cells expressing ...
Mageswaran, Shrawan Kumar
core   +19 more sources

Calreticulin and cancer [PDF]

open access: yesCell Research, 2020
Calreticulin (CALR) is an endoplasmic reticulum (ER)-resident protein involved in a spectrum of cellular processes. In healthy cells, CALR operates as a chaperone and Ca2+ buffer to assist correct protein folding within the ER. Besides favoring the maintenance of cellular proteostasis, these cell-intrinsic CALR functions support Ca2+-dependent ...
Jitka Fucikova   +3 more
openaire   +2 more sources

Molecular cloning and transcriptional activity of a new Petunia calreticulin gene involved in pistil transmitting tract maturation, progamic phase, and double fertilization [PDF]

open access: yes, 2013
Calreticulin (CRT) is a highly conserved and ubiquitously expressed Ca2+-binding protein in multicellular eukaryotes. As an endoplasmic reticulum-resident protein, CRT plays a key role in many cellular processes including Ca2+ storage and release ...
Gumowski, Krzysztof   +9 more
core   +1 more source

Calreticulin Regulates VEGF-A in Neuroblastoma Cells [PDF]

open access: yes, 2017
Calreticulin (CRT) has been previously correlated with the differentiation of neuroblastoma (NB), implying a favorable prognostic factor. Vascular endothelial growth factor (VEGF) has been reported to participate in the behavior of NB.
Weng, Wen-Chin;Lin, Kuan-Hung;Wu, Pei-Yi;Lu, Yi-Chien;Weng, Yi-Cheng;Wang, Bo-Jeng;Liao, Yung-Feng;Hsu, Wen-Ming;Lee, Wang-Tso;Lee, Hsinyu   +1 more
core   +1 more source

Calreticulin expression in human cardiac myocytes induces ER stress‐associated apoptosis

open access: yesPhysiological Reports, 2020
The global burden of heart failure following myocardial ischemia‐reperfusion (IR) injury is a growing problem. One pathway that is key to understanding the progression of myocardial infarction and IR injury is the endoplasmic reticulum (ER) stress ...
Michael W. Stoner   +3 more
doaj   +1 more source

Home - About - Disclaimer - Privacy