Yoke Chen Chang
Rutgers University
Messenger RNACCL3Analytical chemistryQuenching (fluorescence)Downregulation and upregulationChemokineCell migrationMolecular biologyProinflammatory cytokineMacrophage inflammatory proteinAmplitudeChemistryImmunologyBasement membraneWestern blotTryptophanImmunofluorescenceIodideMacrophage elastaseQ valueNeutrophil collagenaseAcrylamideFluorescence spectrometryCXCL10MyosinStereochemistryMyofibrilCrystallographyIn situ hybridizationAnisotropyFluorescenceEmission spectrumCancer cellCXCL1
4Publications
3H-index
19Citations
Publications 4
Newest
#1Yoke Chen Chang (RU: Rutgers University)H-Index: 3
#2James D. Wang (RU: Rutgers University)H-Index: 2
Last. Donald R. Gerecke (RU: Rutgers University)H-Index: 18
view all 8 authors...
: Laminin-332 is a basement membrane protein composed of three genetically distinct polypeptide chains that actively promote both skin epidermal cell adhesion and migration. Proteolytic fragments of the laminin γ2 chain stimulate migration and scattering of keratinocytes and cancer cells. Sulfur mustard (SM) is a bifunctional alkylating agent that induces separation of basal keratinocytes from the dermal-epidermal junction and invokes a strong inflammatory response leading to delayed wound repai...
1 CitationsSource
#1Yoke Chen Chang (RU: Rutgers University)H-Index: 3
#2Melannie Soriano (RU: Rutgers University)H-Index: 1
Last. Donald R. Gerecke (RU: Rutgers University)H-Index: 18
view all 7 authors...
Abstract Sulfur mustard (2,2′-dichlorodiethyl sulfide, SM) is a chemical warfare agent that generates an inflammatory response in the skin and causes severe tissue damage and blistering. In earlier studies, we identified cutaneous damage induced by SM in mouse ear skin including edema, erythema, epidermal hyperplasia and microblistering. The present work was focused on determining if SM-induced injury was associated with alterations in mRNA and protein expression of specific cytokines and chemok...
6 CitationsSource
#1Yoke Chen Chang (RU: Rutgers University)H-Index: 3
Rabbit skeletal myosin rod contains two tryptophan residues per chain (four per coiled-coil) that are located about 50 and 175 A from the N-terminus of the light meromyosin (LMM) region of rod. We have characterized the local polarity, excited-state photophysics, solvent accessibility, and rotational dynamics of these tryptophans in myosin rod filaments at 125 mM HCl using steady-state and time-resolved fluorescence techniques. The fluorescence decays were described using a complex bimodal distr...
7 CitationsSource
#1Yoke Chen Chang (New Jersey Agricultural Experiment Station)H-Index: 3
#2Richard D. Ludescher (New Jersey Agricultural Experiment Station)H-Index: 25
Abstract The solvent accessibility of the four tryptophans of rabbit skeletal muscle myosin rod was investigated using steady-state and time-resolved fluorescence quenching by iodide, acrylamide, and cesium. The quenching by iodide and acrylamide was biphasic; the discrete, long lifetime component was quenched with bimolecular collision constants ( k q ) of 1 × 10 9 M −1 s −1 and 1.6 × 10 9 M −1 s −1 , respectively, while the Gaussian distributed, short lifetime component was quenched with a k q...
6 CitationsSource