Analysis of Ubiquitin Degradation and Phosphorylation of Proteins

2009 ◽  
pp. 169-190 ◽  
Author(s):  
Pearl Gray
Keyword(s):  
Phosphorylation Of Proteins

Analysis of state-specific phosphorylation of proteins by two-dimensional gel electrophoresis approach

2003 ◽  
Vol 787 (1) ◽  
pp. 53-61 ◽  
Author(s):  
H KOVAROVA ◽  
M HAJDUCH ◽  
M LIVINGSTONE ◽  
P DZUBAK ◽  
I LEFKOVITS
Keyword(s):  
Gel Electrophoresis ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis ◽  
Phosphorylation Of Proteins

The effect of IL-5 treatment on the stimulation-induced phosphorylation of proteins in blood eosinophils

Cytokine ◽  
2004 ◽  
Vol 28 (3) ◽  
pp. 137-148 ◽  
Author(s):  
C WOSCHNAGG ◽  
P VENGE ◽  
R GARCIA
Keyword(s):  
Phosphorylation Of Proteins ◽  
Blood Eosinophils

hCG increased phosphorylation of proteins in primary cultures of porcine Leydig cells

1982 ◽  
Vol 105 (1) ◽  
pp. 334-340 ◽  
Author(s):  
A. Gonzalez-Martinez ◽  
M. Benahmed ◽  
M.C. Bommelaer ◽  
F. Haour ◽  
J.M. Saez ◽  
...  
Keyword(s):  
Leydig Cells ◽  
Primary Cultures ◽  
Phosphorylation Of Proteins

Comparison of tyrosine phosphorylation of proteins by membrane fractions from mouse liver, ehrlich ascites tumor and MH134 hepatoma

FEBS Letters ◽  
1985 ◽  
Vol 184 (1) ◽  
pp. 60-64 ◽  
Author(s):  
Hirofumi Usui ◽  
Kazunori Yoshikawa ◽  
Michinori Imazu ◽  
Haruhisa Tsukamoto ◽  
Masao Takeda
Keyword(s):  
Tyrosine Phosphorylation ◽  
Mouse Liver ◽  
Ehrlich Ascites Tumor ◽  
Ascites Tumor ◽  
Phosphorylation Of Proteins ◽  
Ehrlich Ascites

scholarly journals EMBER: Multi-label prediction of kinase-substrate phosphorylation events through deep learning

2020 ◽  
Author(s):  
Kathryn E. Kirchoff ◽  
Shawn M. Gomez
Keyword(s):  
Deep Learning ◽  
Experimental Studies ◽  
Classification Model ◽  
Learning Method ◽  
Kinase Substrate ◽  
Phosphorylation Of Proteins ◽  
Separate Model ◽  
Label Prediction ◽  
Substrate Phosphorylation ◽  
Vector Representations

AbstractKinase-catalyzed phosphorylation of proteins forms the backbone of signal transduction within the cell, enabling the coordination of numerous processes such as the cell cycle, apoptosis, and differentiation. While on the order of 105 phosphorylation events have been described, we know the specific kinase performing these functions for less than 5% of cases. The ability to predict which kinases initiate specific individual phosphorylation events has the potential to greatly enhance the design of downstream experimental studies, while simultaneously creating a preliminary map of the broader phosphorylation network that controls cellular signaling. To this end, we describe EMBER, a deep learning method that integrates kinase-phylogeny information and motif-dissimilarity information into a multi-label classification model for the prediction of kinase-motif phosphorylation events. Unlike previous deep learning methods that perform single-label classification, we restate the task of kinase-motif phosphorylation prediction as a multi-label problem, allowing us to train a single unified model rather than a separate model for each of the 134 kinase families. We utilize a Siamese network to generate novel vector representations, or an embedding, of motif sequences, and we compare our novel embedding to a previously proposed peptide embedding. Our motif vector representations are used, along with one-hot encoded motif sequences, as input to a classification network while also leveraging kinase phylogenetic relationships into our model via a kinase phylogeny-based loss function. Results suggest that this approach holds significant promise for improving our map of phosphorylation relations that underlie kinome signaling.Availabilityhttps://github.com/gomezlab/EMBER

scholarly journals Quantificação de [32P] fosfoproteínas em gel de pollacrilamida pela Radiação Cerenkov: vantagens sobre outros procedimentos

1997 ◽  
Vol 19 (19) ◽  
pp. 21
Author(s):  
Carlos A. Gonçalves ◽  
Guido Lenz ◽  
Christianne Salbego ◽  
Carmem Gottfried
Keyword(s):  
Liquid Scintillation Counting ◽  
Gel Electrophoresis ◽  
Liquid Scintillation ◽  
Polyacrylamide Gel Electrophoresis ◽  
Scintillation Counting ◽  
Polyacrylamide Gel ◽  
Cerenkov Counting ◽  
Phosphorylation Of Proteins ◽  
Phosphate Incorporation

The phosphorylation of proteins has been recognized as an important mechanism for controlling cellular activities. There are many ways to measure 32P-labellingof phosphoproteins resolved by polyacrylamide gel electrophoresis, including densitometry of autoradiographs, liquid scintillation counting and Cerenkov counting. This report compares such different procedures and indicates the advantages of Cerenkov counting to determine radioactive phosphate incorporation into proteins.

Tyrosine phosphorylation of specific proteins after mitogen stimulation of chicken embryo fibroblasts

1983 ◽  
Vol 3 (3) ◽  
pp. 380-390
Author(s):  
K D Nakamura ◽  
R Martinez ◽  
M J Weber
Keyword(s):  
Growth Factor ◽  
Tyrosine Phosphorylation ◽  
Chicken Embryo ◽  
Sodium Dodecyl ◽  
Biological Response ◽  
Egf Receptors ◽  
Phosphorylation Of Proteins ◽  
Embryo Fibroblasts ◽  
Chicken Embryo Fibroblasts ◽  
Stimulation Of

We found that stimulation of density-inhibited chicken embryo fibroblasts with serum, epidermal growth factor (EGF), platelet-derived growth factor, (PDGF), or multiplication-stimulating activity (MSA) leads to an increase in tyrosine phosphorylation of proteins in the region of Mr 40,000 (40K) to 42K. The increase in tyrosine phosphorylation after serum or EGF stimulation was transient, reaching a maximum at about 5 min and then declining. By fine-resolution analysis of proteins separated on sodium dodecyl sulfate-polyacrylamide gels, we found that after EGF stimulation, the major increase in phosphotyrosine content was in a 42K Mr protein, with a smaller increase in a 40K Mr protein. The increased phosphorylation in the 40K to 42K Mr region accounted for almost all of the increase in phosphotyrosine observed in these cells. These phosphotyrosine-containing proteins were different from the major phosphotyrosine-containing protein of Rous sarcoma virus-transformed chicken embryo fibroblasts, which migrates at an approximate Mr of 36K. Increased tyrosine phosphorylation of proteins of similar Mr was found in 3T3 cells treated with EGF, but not in NR-6 cells, which lack detectable EGF receptors. It is possible that the 40K to 42K Mr phosphotyrosine-containing proteins are involved in the integration of the biological response to a number of different growth factors.

Sign in / Sign up

Export Citation Format

Share Document