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

The Ras Gene02:38

The Ras Gene

7.5K
The Ras-gene-encoded proteins are regulators of signaling pathways controlling cell proliferation, differentiation, or cell survival. The Ras-gene family in humans constitutes three primary members—the HRas, NRas, and KRas. These genes code for four functionally distinct yet closely related proteins—the HRas, NRas, KRas4A, and KRas4B. The involvement of mutant Ras genes in human cancer was first discovered in 1982 and is among the most common causes of human tumorigenesis.
Ras is a...
7.5K
Regulation of Nuclear Protein Sorting01:45

Regulation of Nuclear Protein Sorting

3.4K
Nuclear protein sorting regulates nucleus composition and gene expression, crucial for determining the fate of a eukaryotic cell. Hence, the entry and exit of molecules across the nuclear envelope is a tightly controlled process. Nuclear protein sorting can be inhibited by one of the following ways: 1) masking cargo signal sequences, 2) modifying the nuclear receptor's affinity for cargo, 3) controlling the nuclear pore size, 4) retaining the cargo during its transit to the cytosol or the...
3.4K
Nuclear Localization Signals and Import01:46

Nuclear Localization Signals and Import

8.2K
Proteins targeted to the nucleus carry short stretches of amino acid sequences called the nuclear localization signal or NLS. Classical nuclear localization signals are of two types: monopartite and bipartite NLS. Monopartite classical NLS (cNLS) consists of a single cluster of 4-8 amino acids. Bipartite cNLS consists of two clusters of  2-3 amino acids and a 9-12 residue long proline-rich linker bridging the two clusters. Signal clusters are rich in positively charged amino acids such as...
8.2K
Transducer Mechanism: Nuclear Receptors01:31

Transducer Mechanism: Nuclear Receptors

5.3K
Nuclear receptors, or NRs, are unique transcription factors that regulate gene transcription and affect the cellular pathways involved in reproduction, development, or metabolism. Their ability to be stimulated by small lipophilic ligands and control vital cellular processes makes them ideal drug targets. Nearly 10-15% of currently prescribed drugs target these receptors.
About 48 different soluble family members of nuclear receptors are identified that can be divided into two main classes:
5.3K
Directing Proteins to the Rough Endoplasmic Reticulum01:34

Directing Proteins to the Rough Endoplasmic Reticulum

18.3K
The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
18.3K
Ribosomal RNA Synthesis02:53

Ribosomal RNA Synthesis

15.1K
Ribosome synthesis is a highly complex and coordinated process involving more than 200 assembly factors. The synthesis and processing of ribosomal components occurs not only in the nucleolus but also in the nucleoplasm and the cytoplasm of eukaryotic cells.
Ribosome biogenesis begins with the synthesis of 5S and 45S pre-rRNAs by distinct RNA polymerases. The primary transcripts are extensively processed and modified before they are bound and folded by ribosomal proteins and assembly factors,...
15.1K

You might also read

Related Articles

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

Sort by
Same author

Inflammatory immune modulators of AML lung infiltration and respiratory failure.

Nature immunology·2026
Same author

Prognostic and therapeutic implications of BRAF mutations in acute myeloid leukemia.

Leukemia·2026
Same author

A gene signature derived from leukemia associated macrophages provides a compelling risk stratification for human AML patients.

Biomarker research·2026
Same author

RAS pathway activation and microenvironmental adaptation as hallmarks of myeloid sarcoma.

Blood cancer discovery·2026
Same author

Leukemic stem cell subtypes determine venetoclax resistance and therapeutic vulnerabilities in AML.

Cell stem cell·2026
Same author

Implementation of surface-guided radiotherapy for motion management in liver SBRT: A scoping review and clinical workflow development.

Technical innovations & patient support in radiation oncology·2026

Related Experiment Video

Updated: Mar 24, 2026

Nitrogen Cavitation and Differential Centrifugation Allows for Monitoring the Distribution of Peripheral Membrane Proteins in Cultured Cells
08:24

Nitrogen Cavitation and Differential Centrifugation Allows for Monitoring the Distribution of Peripheral Membrane Proteins in Cultured Cells

Published on: August 18, 2017

17.3K

Structural characterization of NRAS isoform 5.

Joseph Markowitz1,2, Tapas K Mal3, Chunhua Yuan3

  • 1Moffitt Cancer Center Department of Cutaneous Oncology, The Ohio State University, Columbus, Ohio.

Protein Science : a Publication of the Protein Society
|March 8, 2016
PubMed
Summary
This summary is machine-generated.

A newly discovered NRAS isoform 5 drives aggressive melanoma by increasing cell proliferation and phosphorylation of key targets. Its structure reveals flexibility in solution and a helix-turn-coil formation in TFE.

Keywords:
NMRNRASisoformmelanoma

More Related Videos

Fully Processed Recombinant KRAS4b: Isolating and Characterizing the Farnesylated and Methylated Protein
07:08

Fully Processed Recombinant KRAS4b: Isolating and Characterizing the Farnesylated and Methylated Protein

Published on: January 16, 2020

6.2K
Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae
09:15

Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae

Published on: January 10, 2018

10.4K

Related Experiment Videos

Last Updated: Mar 24, 2026

Nitrogen Cavitation and Differential Centrifugation Allows for Monitoring the Distribution of Peripheral Membrane Proteins in Cultured Cells
08:24

Nitrogen Cavitation and Differential Centrifugation Allows for Monitoring the Distribution of Peripheral Membrane Proteins in Cultured Cells

Published on: August 18, 2017

17.3K
Fully Processed Recombinant KRAS4b: Isolating and Characterizing the Farnesylated and Methylated Protein
07:08

Fully Processed Recombinant KRAS4b: Isolating and Characterizing the Farnesylated and Methylated Protein

Published on: January 16, 2020

6.2K
Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae
09:15

Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae

Published on: January 10, 2018

10.4K

Area of Science:

  • Molecular biology
  • Biochemistry
  • Cancer research

Background:

  • A novel NRAS isoform 5 (20 amino acids) is expressed in melanoma.
  • This isoform is associated with a more aggressive cancer cell phenotype.

Purpose of the Study:

  • To determine the NMR solution structure of NRAS isoform 5.
  • To provide a foundation for understanding its biophysical interactions.

Main Methods:

  • Nuclear Magnetic Resonance (NMR) spectroscopy was used to determine the solution structure.
  • Circular Dichroism (CD) spectroscopy was employed to analyze structural changes.

Main Results:

  • NRAS isoform 5 exhibits high flexibility in aqueous solution.
  • In the presence of trifluoroethanol (TFE), the isoform adopts a helix-turn-coil structure.

Conclusions:

  • The structural characterization of NRAS isoform 5 is crucial for understanding its role in melanoma.
  • Further studies can leverage this structural information to explore therapeutic strategies targeting this aggressive isoform.