Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Sampling Continuous Time Signal01:11

Sampling Continuous Time Signal

857
In signal processing, a continuous-time signal can be sampled using an impulse-train sampling technique, followed by the zero-order hold method. Impulse-train sampling involves the use of a periodic impulse train, which consists of a series of delta functions spaced at regular intervals determined by the sampling period. When a continuous-time signal is multiplied by this impulse train, it generates impulses with amplitudes corresponding to the signal's values at the sampling points.
In the...
857
Reconstruction of Signal using Interpolation01:10

Reconstruction of Signal using Interpolation

871
Signal processing techniques are essential for accurately converting continuous signals to digital formats and vice versa. When a continuous signal is sampled with a period T, the resulting sampled signal exhibits replicas of the original spectrum in the frequency domain, spaced at intervals equal to the sampling frequency. To handle this sampled signal, a zero-order hold method can be applied, which creates a piecewise constant signal by retaining each sample's value until the next...
871
Aliasing01:18

Aliasing

824
Accurate signal sampling and reconstruction are crucial in various signal-processing applications. A time-domain signal's spectrum can be revealed using its Fourier transform. When this signal is sampled at a specific frequency, it results in multiple scaled replicas of the original spectrum in the frequency domain. The spacing of these replicas is determined by the sampling frequency.
If the sampling frequency is below the Nyquist rate, these replicas overlap, preventing the original...
824
Upsampling01:22

Upsampling

713
Managing signal sampling rates is essential in digital signal processing to maintain signal integrity. A decimated signal, characterized by a reduced frequency range due to its lower sampling rate, can be upsampled by inserting zeros between each sample. This upsampling process expands the original spectrum and introduces repeated spectral replicas at intervals dictated by the new Nyquist frequency. To refine this zero-inserted sequence, it is passed through a lowpass filter with a cutoff...
713
Signal Transduction: Overview01:26

Signal Transduction: Overview

12.8K
Cells respond to many types of information, often through receptor proteins positioned on the membrane. They respond to chemical signals, such as hormones, neurotransmitters, and other signaling molecules, initiating a series of molecular reactions to produce an appropriate response. This is called signal transduction. Cells also coordinate different responses elicited by the same signaling molecule via mediators, allowing molecular cross-talk.
Typically, signal transduction involves three...
12.8K
Amplifying Signals via Enzymatic Cascade01:22

Amplifying Signals via Enzymatic Cascade

19.5K
When a ligand binds to a cell-surface receptor, the receptor's intracellular domain changes shape, which may either activate its enzyme function or allow its binding to other molecules. The initial signal is amplified by most signal transduction pathways. This means that a single ligand molecule can activate multiple molecules of a downstream target. Proteins that relay a signal are most commonly phosphorylated at one or more sites, activating or inactivating the protein. Kinases catalyze...
19.5K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

The structure of the lipid II flippase from monoderm bacteria.

bioRxiv : the preprint server for biology·2026
Same author

Structural basis of metalloid transport by the arsenite efflux pump ArsB.

Nature communications·2026
Same author

Structures of Bacterial and Human Phosphoglycosyltransferases Bound to a Common Inhibitor Inform Selective Therapeutics.

ACS chemical biology·2026
Same author

Convergent MurJ flippase inhibition by phage lysis proteins.

Nature·2026
Same author

Structures of bacterial and human phosphoglycosyltransferases bound to a common inhibitor inform selective therapeutics.

bioRxiv : the preprint server for biology·2025
Same author

Nucleotide- and metalloid-driven conformational changes in the arsenite efflux ATPase ArsA.

Proceedings of the National Academy of Sciences of the United States of America·2025
Same journal

Canonical and phosphoribosyl ubiquitination coordinate to stabilize a proteinaceous structure surrounding the <i>Legionella</i>-containing vacuole.

eLife·2026
Same journal

Celldetective, an AI-enhanced image analysis tool for unraveling dynamic cell interactions.

eLife·2026
Same journal

Dynamic assembly of malate dehydrogenase-citrate synthase multienzyme complex in the mitochondria.

eLife·2026
Same journal

Autosomal allelic inactivation at loci with variable replication timing and dosage sensitivity.

eLife·2026
Same journal

Cribriform plate microenvironment assembles a suppressive myeloid network during EAE-induced neuroinflammation.

eLife·2026
Same journal

Proteomic composition and mutual assembly of the C2a projection in vertebrate motile cilia.

eLife·2026
See all related articles

Related Experiment Video

Updated: Apr 7, 2026

One-channel Cell-attached Patch-clamp Recording
13:07

One-channel Cell-attached Patch-clamp Recording

Published on: June 9, 2014

25.7K

Capturing the signal.

Jee-Young Mock1, William M Clemons1

  • 1Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, United States.

Elife
|July 10, 2015
PubMed
Summary
This summary is machine-generated.

High-resolution structures reveal how an RNA-protein complex identifies signals for targeting membrane proteins to the endoplasmic reticulum, preventing aggregation.

Keywords:
biochemistrybiophysicscryo-EMmembrane protein biogenesisprotein targetingrabbitsignal recognition particlestructural biology

More Related Videos

Long-term Behavioral Tracking of Freely Swimming Weakly Electric Fish
10:56

Long-term Behavioral Tracking of Freely Swimming Weakly Electric Fish

Published on: March 6, 2014

13.1K
Studying Cavitation Enhanced Therapy
07:36

Studying Cavitation Enhanced Therapy

Published on: April 9, 2021

6.0K

Related Experiment Videos

Last Updated: Apr 7, 2026

One-channel Cell-attached Patch-clamp Recording
13:07

One-channel Cell-attached Patch-clamp Recording

Published on: June 9, 2014

25.7K
Long-term Behavioral Tracking of Freely Swimming Weakly Electric Fish
10:56

Long-term Behavioral Tracking of Freely Swimming Weakly Electric Fish

Published on: March 6, 2014

13.1K
Studying Cavitation Enhanced Therapy
07:36

Studying Cavitation Enhanced Therapy

Published on: April 9, 2021

6.0K

Area of Science:

  • Molecular biology
  • Cellular biology
  • Structural biology

Background:

  • Membrane protein targeting is crucial for cellular function.
  • The endoplasmic reticulum (ER) is a key organelle for protein synthesis and modification.
  • Protein aggregation can lead to cellular dysfunction and disease.

Purpose of the Study:

  • To elucidate the molecular mechanism of signal recognition by the RNA-protein complex.
  • To understand how this complex directs membrane proteins to the ER.
  • To investigate the structural basis for preventing protein aggregation.

Main Methods:

  • High-resolution structural analysis (e.g., cryo-EM, X-ray crystallography).
  • Biochemical assays to study RNA-protein interactions.
  • Cellular imaging to observe protein targeting in vivo.

Main Results:

  • Detailed structures of the RNA-protein complex bound to the targeting signal.
  • Identification of key residues and structural features involved in signal recognition.
  • Demonstration of the complex's role in facilitating co-translational translocation to the ER.

Conclusions:

  • The RNA-protein complex utilizes specific structural elements to accurately recognize the targeting signal.
  • This recognition mechanism is essential for efficient and correct delivery of membrane proteins to the ER.
  • The findings provide a structural basis for understanding protein homeostasis and preventing aggregation-related disorders.