Results 311 to 320 of about 16,586,228 (338)

Survivin does not inhibit caspase-3 activity

Blood, 2000
Conway et al recently reported that alternatively spliced forms of mouse survivin exhibit different antiapoptotic properties.[1][1] This was inferred from inhibition of recombinant caspase-3 catalytic activity using a standard chromogenic assay in the presence of increasing concentrations ...
Dario C. Altieri, Damon Banks, Janet Plescia, Haichao Zhang, Shi-Chung Ng, Jun Chen, Saul H. Rosenberg   +6 more
openaire   +3 more sources

Differential regulation of caspase-3 by pharmacological and developmental stimuli as demonstrated using humanised caspase-3 mice

Apoptosis, 2004
Caspase-3 is a potential therapeutic target for a number of degenerative diseases. However the development of specific caspase-3 inhibitors has been hampered by inter-species differences and the high degree of homology shared by different caspases.
J Sharkey, N Logan, G Carlson, A Simon, J-L A Birse-Archbold, Lorraine E. Kerr, Donald W. Nicholson, John S. Kelly, F Scott   +8 more
openaire   +3 more sources

Active caspase‐3 is required for osteoclast differentiation

Journal of Cellular Physiology, 2006
AbstractBased on our earlier observation that caspase‐3 is present in osteoclasts that are not undergoing apoptosis, we investigated the role of this protein in the differentiation of primary osteoclasts and RAW264.7 cells (Szymczyk KH, et al., 2005, Caspase‐3 activity is necessary for RANKL‐induced osteoclast differentiation.
Szymczyk, K. H., Freeman, T. A., Adams, Christopher S., Srinivas, V., Steinbeck, M. J.   +4 more
openaire   +3 more sources

Caspase-3 as a therapeutic target for heart failure

Expert Opinion on Therapeutic Targets, 2013
Heart failure is a condition with significant morbidity and high mortality. It is likely to become unmanageable in the rapidly increasing aging population, due mainly to lack of effective treatment. Apoptosis is one of the major mechanisms causing cardiomyocyte loss in the failing hearts of both human patients and animal models.
Yang, B, Ye, D, Wang, Y
openaire   +5 more sources

FITC–quencher based caspase 3-activatable nanoprobes for effectively sensing caspase 3 in vitro and in cells

Nanoscale, 2013
By employing fluorescence resonance energy transfer (FRET) quenching, we rationally designed two new FITC-quencher based nanoprobes for effectively sensing caspase 3 (Casp3) in vitro and in cells. Our nanoprobes hold promise for assessing the chemotherapeutic effect of cancer treatment.
Gaolin Liang, Anming Tang, Fang Li, Mian Wu, Hua Cui, Weijuan Wang, Qing Yang, Wanglai Hu, Jun Zhou, Bin Mei   +9 more
openaire   +3 more sources

Blockade of processing/activation of caspase-3 by hypoxia

Biochemical and Biophysical Research Communications, 2008
Tumor hypoxia, which is caused by the rapid proliferation of tumor cells and aberrant vasculature in tumors, results in inadequate supplies of oxygen and nutrients to tumor cells. Paradoxically, these unfavorable growth conditions benefit tumor cell survival, although the mechanism is poorly understood.
Dai-Wu Seol, Sang Hee Han, Tae-Hyoung Kim, Moonil Kim, Kyoungsook Park   +4 more
openaire   +3 more sources

Detecting Cleaved Caspase-3 in Apoptotic Cells by Flow Cytometry.

Cold Spring Harbor Protocols, 2016
Apoptosis is orchestrated by caspases, a family of cysteine proteases that cleave their substrates on the carboxy-terminal side of specific aspartic acid residues.
L. C. Crowley, N. Waterhouse
semanticscholar   +1 more source

Overexpression of Survivin and Caspase 3 in Oral Carcinogenesis

Applied Immunohistochemistry & Molecular Morphology, 2014
Survivin is an inhibitor of apoptosis protein that inhibits caspase 3 function. While cytoplasmic survivin suppresses apoptosis, nuclear survivin regulates cell division. Little is known about the subcellular localization of survivin in oral carcinogenesis.
Sopee Poomsawat, Jirapa Punyasingh, Paisarn Vejchapipat   +2 more
openaire   +3 more sources

Electrochemiluminescent Sensing for Caspase-3 Activity Based on Ru(bpy)3(2+)-Doped Silica Nanoprobe.

Analytical Chemistry, 2016
Caspase-3 is one of the most frequently activated cysteine proteases during the apoptosis process and has been identified as a well-established cellular marker of apoptosis.
Yongping Dong, Gang Chen, Ying Zhou, Jun‐Jie Zhu   +3 more
semanticscholar   +1 more source

Kinetic comparison of procaspase-3 and caspase-3

Archives of Biochemistry and Biophysics, 2005
Caspases, the key enzymes in apoptosis, are synthesized as proenzymes and converted into active form by proteolytic cleavage. The residues on active site reorganize during the activation process as shown in the comparative studies of crystallographic structures of procaspase-7 and its mature form.
Pratap Karki, Song Yub Shin, Il-Seon Park, Byungyun Cho, Jung-Sup Lee   +4 more
openaire   +2 more sources