Profiling the effects of short time‐course cold ischemia on tumor protein phosphorylation using a Bayesian approach

Profiling the effects of short time‐course cold ischemia on tumor protein phosphorylation using... IntroductionProtein tyrosine phosphorylation is considered to be a fundamental mechanism for regulating many cellular functions. In this specific phosphorylation, a phosphate group is added to the amino acid tyrosine on a protein. Disorders of tyrosine phosphorylation are believed to lead to many serious human diseases (Hunter, ). For example, protein tyrosine phosphorylation is tightly regulated in normal cells, but tyrosine kinases, whose activity controls tyrosine phosphorylation, are found to be mutated or over‐expressed in many human malignancies (Paul and Mukhopadhyay, ). Accurate and robust assessment of tyrosine phosphorylation in tumor biopsy samples is thus necessary for understanding intracellular signaling networks and for developing targeted therapies for cancer patients (Bonnas et al., ); Gajadhar et al., ).However, there may exist pre‐analytic variations due to inconsistencies during sample collection and processing in a clinical laboratory. One of these sources of variations is cold ischemia. Also known as freezing delay time, cold ischemia is the time between tissue specimen excision and the freezing of the sample. Although it has been shown that global protein levels do not change up to 1‐hour cold ischemia, significant changes are observed in phosphorylated proteins at the phosphorylation sites. Some of the phosphorylation sites even have rapid http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Biometrics Wiley

Profiling the effects of short time‐course cold ischemia on tumor protein phosphorylation using a Bayesian approach

Loading next page...
 
/lp/wiley/profiling-the-effects-of-short-time-course-cold-ischemia-on-tumor-AeKChPYgj6
Publisher
Wiley
Copyright
© 2018, The International Biometric Society
ISSN
0006-341X
eISSN
1541-0420
D.O.I.
10.1111/biom.12742
Publisher site
See Article on Publisher Site

Abstract

IntroductionProtein tyrosine phosphorylation is considered to be a fundamental mechanism for regulating many cellular functions. In this specific phosphorylation, a phosphate group is added to the amino acid tyrosine on a protein. Disorders of tyrosine phosphorylation are believed to lead to many serious human diseases (Hunter, ). For example, protein tyrosine phosphorylation is tightly regulated in normal cells, but tyrosine kinases, whose activity controls tyrosine phosphorylation, are found to be mutated or over‐expressed in many human malignancies (Paul and Mukhopadhyay, ). Accurate and robust assessment of tyrosine phosphorylation in tumor biopsy samples is thus necessary for understanding intracellular signaling networks and for developing targeted therapies for cancer patients (Bonnas et al., ); Gajadhar et al., ).However, there may exist pre‐analytic variations due to inconsistencies during sample collection and processing in a clinical laboratory. One of these sources of variations is cold ischemia. Also known as freezing delay time, cold ischemia is the time between tissue specimen excision and the freezing of the sample. Although it has been shown that global protein levels do not change up to 1‐hour cold ischemia, significant changes are observed in phosphorylated proteins at the phosphorylation sites. Some of the phosphorylation sites even have rapid

Journal

BiometricsWiley

Published: Jan 1, 2018

Keywords: ; ; ;

References

You’re reading a free preview. Subscribe to read the entire article.


DeepDyve is your
personal research library

It’s your single place to instantly
discover and read the research
that matters to you.

Enjoy affordable access to
over 18 million articles from more than
15,000 peer-reviewed journals.

All for just $49/month

Explore the DeepDyve Library

Search

Query the DeepDyve database, plus search all of PubMed and Google Scholar seamlessly

Organize

Save any article or search result from DeepDyve, PubMed, and Google Scholar... all in one place.

Access

Get unlimited, online access to over 18 million full-text articles from more than 15,000 scientific journals.

Your journals are on DeepDyve

Read from thousands of the leading scholarly journals from SpringerNature, Elsevier, Wiley-Blackwell, Oxford University Press and more.

All the latest content is available, no embargo periods.

See the journals in your area

DeepDyve

Freelancer

DeepDyve

Pro

Price

FREE

$49/month
$360/year

Save searches from
Google Scholar,
PubMed

Create lists to
organize your research

Export lists, citations

Read DeepDyve articles

Abstract access only

Unlimited access to over
18 million full-text articles

Print

20 pages / month

PDF Discount

20% off