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Record W2754993413 · doi:10.1117/3.862866.ch6

Bioluminescence and Fluorescence Imaging for

2010· book-chapter· en· W2754993413 on OpenAlex

Why this work is in the frame

A frame that forgets how it found something cannot be audited. These are the routes that admitted this work.

affAt least one author lists a Canadian institution in the pinned OpenAlex snapshot.

Bibliographic record

VenueSPIE eBooks · 2010
Typebook-chapter
Languageen
FieldBiochemistry, Genetics and Molecular Biology
TopicBiotin and Related Studies
Canadian institutionsUniversity of Guelph
Fundersnot available
KeywordsProtein–protein interactionIn vivoBimolecular fluorescence complementationCell biologyFörster resonance energy transferBiologyBioluminescencePreclinical imagingBiophysicsLuciferasesGreen fluorescent proteinComputational biologyChemistryLuciferaseTransfectionFluorescenceGeneBiochemistryGeneticsPhysics

Abstract

fetched live from OpenAlex

The <i>in vivo </i>monitoring and characterization of protein-protein interactions are essential to understanding cellular events in living organisms. Proteins never act alone in the cell; on the contrary, they associate with each other to form stable or transient complexes that execute certain cellular functions. Aberrant protein interactions were observed in many pathological conditions, and therefore <i>in vivo </i>investigation of protein-protein interactions-noninvasively with high temporal and spatial resolution-could shed new light on the mechanisms underlying these interactions and provide new insights for the development of new treatment strategies. To adapt existing <i>in vitro </i>and cell-culture-based techniques to study protein-protein interactions in a living organism, the signal of the event must be detected noninvasively from inside the living subject. Optical imaging is an ideal tool for such research, as it allows monitoring intracellular processes in real time, without interferences, and with high spatial and temporal resolution. Three major approaches were developed to monitor protein-protein interactions <i>in vivo </i>using optical reporters. These include the two-hybrid system, protein complementation assays based on luciferases and fluorescent proteins, and assays based on nonradiative energy transfer (FRET and BRET). <strong>6.1 Two-Hybrid System for In Vivo Monitoring of Protein-Protein Interactions</strong> The two-hybrid system exploits the ability of a pair of interacting proteins to bring a transcription activation domain into close proximity with a DNA-binding site, which regulates the expression of an adjacent reporter gene (Fig. 6.1). This method was originally developed for yeast. Two proteins of interest were expressed in yeast: one fused to a DNA-binding domain, and the other to a transcriptional activation domain. The first hybrid protein can bind to DNA, but will not activate transcription if it does not have an activation domain. Another hybrid protein, if present alone, does not activate transcription because it does not bind to the upstream activation system. When both hybrid proteins are present, they form a complex, thus bringing both the DNA-binding domain and the transcription activation domain together, which in turn triggers the transcription of the reporter gene. In early publications, &#946;-galactosidase was used as a reporter molecule generating blue colonies on plates or filters containing X-Gal. The two-hybrid system was shown to be highly sensitive; the level of induced transcriptional activity seemed to be proportional to the affinity of the investigated proteins. However, due to the nature of the signal (color), it was impossible to apply this method for real-time <i>in vivo </i>imaging.

Fetched live from OpenAlex and de-inverted. Abstracts are not stored in this database: the inverted indexes are 8.6 GB of the frame’s 9.3 GB of text, and the host has 13 GB free.

Full frame distilled prediction

Teacher imitation

Not calibrated prevalence, not ground truth. Human validation pending. Learned from the 10,348 direct Codex labels and 10,348 direct Gemma labels. Candidate is the union of thresholded teacher heads; consensus is their intersection. These outputs are machine_predicted_unvalidated and are not human labels or direct frontier model labels.

metaresearch head score (Codex)0.000
metaresearch head score (Gemma)0.000
Version: codex-gemma-dda1882f352aValidation status: machine_predicted_unvalidated
Candidate categoriesnone
Consensus categoriesnone
DomainCandidate signal: none · Consensus signal: none
Study designCandidate signal: Bench or experimental · Consensus signal: none
GenreCandidate signal: Other · Consensus signal: Other
Teacher disagreement score0.884
Threshold uncertainty score0.873

Codex and Gemma teacher scores by category

CategoryCodexGemma
Metaresearch0.0000.000
Meta-epidemiology (narrow)0.0000.000
Meta-epidemiology (broad)0.0000.000
Bibliometrics0.0000.000
Science and technology studies0.0000.000
Scholarly communication0.0000.000
Open science0.0000.000
Research integrity0.0000.000
Insufficient payload (model declined to judge)0.0000.000

Machine scores (provisional)

The two teacher heads of the student model, read on this work. A score orders the frame for review; it never asserts a category, and the validation status ships verbatim with every row.

Baseline scores from an immature model (maturity gate not passed, 7 training rounds). Scores rank; they never assert a category.

Opus teacher head0.008
GPT teacher head0.225
Teacher spread0.216 · how far apart the two teachers sit on this one work
Validation statusscore_only:v0-immature-baseline · verbatim from the scoring run: score_only means the number may rank works, and no category label ships from it