Search Results - (Author, Cooperation:K. P. Lu)

2015-01-28

Nature Publishing Group (NPG)

0028-0836

1476-4687

Biology

Chemistry and Pharmacology

Medicine

Natural Sciences in General

Physics

Animals ; Cattle ; Cell Line ; *Cell Transformation, Neoplastic/drug effects ; Drug Resistance/genetics ; *Host-Parasite Interactions ; Humans ; Leukocytes/drug effects/parasitology/*pathology ; Naphthoquinones/pharmacology ; Parasites/drug effects/enzymology/pathogenicity ; Peptidylprolyl Isomerase/antagonists & inhibitors/genetics/*metabolism/*secretion ; Protein Stability ; Proto-Oncogene Proteins c-jun/metabolism ; SKP Cullin F-Box Protein Ligases/metabolism ; Signal Transduction/drug effects ; Theileria/drug effects/*enzymology/genetics/*pathogenicity ; Transcription Factor AP-1/metabolism ; Ubiquitination ; Xenograft Model Antitumor Assays ; Zebrafish/embryology

2015-07-16

Nature Publishing Group (NPG)

0028-0836

1476-4687

Biology

Chemistry and Pharmacology

Medicine

Natural Sciences in General

Physics

Alzheimer Disease/complications/prevention & control ; Animals ; Antibodies, Monoclonal/*immunology/*pharmacology/therapeutic use ; Antibody Affinity ; Axons/metabolism/pathology ; Brain/metabolism/pathology ; Brain Injuries/complications/metabolism/*pathology/*prevention & control ; Disease Models, Animal ; Epitopes/chemistry/immunology ; Female ; Humans ; Male ; Mice ; Phosphoproteins/antagonists & inhibitors/biosynthesis/immunology/toxicity ; Stress, Physiological ; Tauopathies/complications/metabolism/pathology/*prevention & control ; tau Proteins/*antagonists & ; inhibitors/biosynthesis/*chemistry/immunology/toxicity

2014-03-29

Nature Publishing Group (NPG)

0028-0836

1476-4687

Biology

Chemistry and Pharmacology

Medicine

Natural Sciences in General

Physics

Animals ; Apoptosis/genetics ; Cell Cycle/*physiology ; Cell Proliferation ; Cyclin A2/metabolism ; Cyclin-Dependent Kinase 2/metabolism ; Embryonic Stem Cells/cytology/metabolism ; Enzyme Activation ; Male ; Mice ; Multiprotein Complexes/metabolism ; Neoplasms/enzymology/pathology ; Olfactory Bulb/cytology/enzymology/metabolism ; Oncogene Protein v-akt/chemistry/metabolism ; Phosphorylation ; Phosphoserine/metabolism ; Phosphothreonine/metabolism ; Proto-Oncogene Proteins c-akt/*chemistry/*metabolism ; TOR Serine-Threonine Kinases/metabolism

1089-7550

AIP Digital Archive

Physics

The transient transmittance of gamma-ray irradiated poly(methyl methacrylate) at elevated temperatures is investigated. The transmittance in the ultraviolet and visible range decreases with an increase of radiation dose. We propose that the color center is responsible for the reduction of transmittance in the irradiated specimen. Then the concentration of the color center decreases with increasing annealing time at elevated temperatures. The transmittance data at 407 nm are in excellent agreement with the theoretical model in which the color center is annihilated by a second order kinetic process. The rate constant follows the Arrhenius equation. The activation energy in the range of 44.27–51.52 kJ/mol decreases with increased dose. © 2000 American Institute of Physics.

Electronic Resource

1089-7550

AIP Digital Archive

Physics

The decrease in hardness induced by gamma irradiation in poly(methyl methacrylate) (PMMA) has been investigated. The hardness is assumed to decrease linearly with the concentration of radiation-induced defects. Annealing at high temperatures induces defect annihilation as tracked by an increase in hardness. The annihilation follows first-order kinetics during isothermal annealing. The dependence of hardness on the reciprocal of the time constant satisfies the Arrhenius equation, and the corresponding activation energy of the kinetic process decreases with increasing dose. The hardness of postannealed PMMA decreases linearly with increasing dose. © 2001 American Institute of Physics.

Electronic Resource

1476-4687

Nature Archives 1869 - 2009

Biology

Chemistry and Pharmacology

Medicine

Natural Sciences in General

Physics

[Auszug] Nature 440, 528–534 (2006) During editing to meet Nature’s limits on length, we removed a reference to an earlier paper1 reporting that the prolyl isomerase Pin1 promotes production of Alzheimer’s ...

Electronic Resource

1420-9071

Key words. Alzheimer’s disease; mitotic regulation; Pin1; peptidyl-prolyl isomerase; prolyl isomerization; protein phosphorylation.

Springer Online Journal Archives 1860-2000

Biology

Medicine

Abstract. Protein phosphorylation on serine or threonine residues preceding proline (Ser/Thr-Pro) plays an essential role for regulating various cellular processes, including cell cycle progression. Although phosphorylation has been proposed to regulate the function of a protein by inducing conformational changes, much less is known about what phosphate additions actually do and how the functions of phosphoproteins are coordinated. Proline is important for determining protein structure because it exists in cis or trans conformation and can put kinks into a polypeptide chain. We have shown that phosphorylation on Ser/Thr-Pro motifs reduces the cis/trans isomerization rate of Ser/Thr-Pro bonds. At the same time, proteins containing phosphorylated Ser/Thr-Pro motifs are substrates for the prolyl isomerase Pin1. The WW domain of Pin1 acts as a phosphoserine/threonine-binding module binding a defined subset of mitosis-specific phosphoproteins, such as Cdc25 and tau. These interactions target the enzymatic activity of Pin1 close to its substrates. In contrast to other prolyl isomerases (peptidyl-prolyl isomerases, PPIases), Pin1 has an extremely high degree of substrate specificity, specifically isomerizing phosphorylated Ser/Thr-Pro bonds. Therefore, Pin1 binds and regulates the function of a defined subset of phosphoproteins. Furthermore, inhibiting Pin1 function is lethal for dividing cells. Interestingly, Pin1, which can restore the biological function of phosphorylated tau, is sequestered in the neurofibrillary tangles in Alzheimer’s brains. Thus, we have proposed a novel signaling regulatory mechanism, where protein phosphorylation creates binding sites for Pin1, which can then latch on to and isomerize the phosphorylated Ser/Thr-Pro peptide bond. In turn, this may change the shape of the protein, regulating its activity, dephosphorylation, degradation or location in the cell. This new post-phosphorylation regulatory mechanism appears to play an important role in normal cell function, such as mitotic progression, and in the pathogenesis of some human pathologies, such as Alzheimer’s disease.

Electronic Resource