2010
DOI: 10.1002/bmb.20383
|View full text |Cite
|
Sign up to set email alerts
|

Response to review of Fundamental Laboratory Approaches for Biochemistry and Biotechnology

Abstract: John Markwell presented a comprehensive review [1] of the second edition of our laboratory manual, Fundamental Laboratory Approaches for Biochemistry and Biotechnology, which we fondly refer to as FLABBe2 ([2]. Markwell's review was fair and provided valuable information for us to consider in future editions.

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1
1

Citation Types

0
2
0

Year Published

2019
2019
2023
2023

Publication Types

Select...
4
1
1

Relationship

0
6

Authors

Journals

citations
Cited by 7 publications
(2 citation statements)
references
References 2 publications
0
2
0
Order By: Relevance
“…The disruptive SNVs were our main focus in this study due to their high potential to be associated with drug resistance. Due to the fact that available experimentally measured ligand binding affinity change data are highly limited (Benore, 2010), it is not practical to train a supervised learning model based on experimental data. Therefore, in our method we circumvented this issue by constructing a calculated binding affinity change set as our pseudo gold standard using molecular docking programs.…”
Section: Introductionmentioning
confidence: 99%
“…The disruptive SNVs were our main focus in this study due to their high potential to be associated with drug resistance. Due to the fact that available experimentally measured ligand binding affinity change data are highly limited (Benore, 2010), it is not practical to train a supervised learning model based on experimental data. Therefore, in our method we circumvented this issue by constructing a calculated binding affinity change set as our pseudo gold standard using molecular docking programs.…”
Section: Introductionmentioning
confidence: 99%
“…65 Because it features high protein separation capacity for a wide range of protein sizes, visualizes protein patterns and is semi-quantitative, it is widely used in protein and proteomics analyses. The control and studied sample are digested in 16 O and 18 O separately, and equal amounts of the unlabeled control and isotope-labeled sample are mixed and analyzed by tandem mass spectrometry.…”
Section: Gel Electrophoresismentioning
confidence: 99%