Abstracts - faqs.org

Abstracts

Biological sciences

Search abstracts:
Abstracts » Biological sciences

EphA receptors regulate growth cone dynamics through the novel guanine nucleotide exchange factor ephexin

Article Abstract:

Research has been conducted on the Eph receptors transducing repulsive short-range signals for axon guidance via actin dynamics modulation within growth cones. The cloning and characterization of the Eph receptor-interacting protein ephexin have been carried out and the results indicate the creation of the molecular link between Eph receptors and the actin cytoskeleton providing a localized regulation of the growth cone motility.

Author: Lin, Michael Z., Greenberg, Michael E., Debant, Anne, Shamah, Steven M., Hu, Linda, Goldberg, Jeffrey L., Estrach, Soline, Sahin, Mustafa, Bazalakova, Mihaela, Neve, Rachel L., Corfas, Gabriel
Publisher: Elsevier B.V.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 2001
France, Cloning, Actin, Guanine, Nucleotides

User Contributions:

Comment about this article or add new information about this topic:

CAPTCHA


Multiple tumor suppressor pathways negatively regulate telomerase

Article Abstract:

Research has been conducted on telomerase regulation. The study of this genetic regulation has been carried out via the use of general genetic screen, and the results demonstrate that multiple tumor suppressor/oncogene pathways repress telomerase protein component expression, and that telomerase is reactivated via oncogenic mutations in human tumors.

Author: Elledge, Stephen J., Lin, Shiaw-Yih
Publisher: Elsevier B.V.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 2003
Causes of, Gene mutations, Gene mutation, Gene expression, Tumors, Tumor suppressor genes, Telomerase, Tumours, Tumour suppressor genes

User Contributions:

Comment about this article or add new information about this topic:

CAPTCHA


An E3-like factor that promotes SUMO conjugation to the yeast septins

Article Abstract:

Research has been conducted on the ubiquitin-related protein SUMO. Results indicate that the covalent attachment of this protein to the other proteins participates in such processes as transcriptional regulation and growth control and that the Siz1 has been characterized as an E3-like factor in the SUMO pathway.

Author: Johnson, Erica S., Gupta, Aseem A.
Publisher: Elsevier B.V.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 2001
Genetic transcription, Transcription (Genetics), Metabolic regulation, Yeast, Yeast (Food product), Growth (Physiology)

User Contributions:

Comment about this article or add new information about this topic:

CAPTCHA


Subjects list: Statistical Data Included, United States, Analysis, Physiological aspects, Genetic aspects, Proteins, Cell research, Cytological research, Genetic regulation
Similar abstracts:
  • Abstracts: Mimicry grasps reality in translation termination. A posttermination ribosomal complex is the guanine nucleotide exchange factor for peptide release factor RF3
  • Abstracts: Molecular cloning and analysis of the ptsHI operon in Lactobacillus sake. Development of genetic tools for Lactobacillus sakei: disruption of the beta-galactosidase gene and use of lacZ as a reporter gene to study regulation of the putative copper ATPase, AtkB
  • Abstracts: The Evi5 oncogene regulates cyclin accumulation by stabilizing the anaphase-promoting complex inhibitor Emi1. Emi1 is a mitotic regulator that interacts with Cdc20 and inhibits the anaphase promoting complex
  • Abstracts: Cdc13 deliveres separate complexes to the telomere for end protection and replication. Switching and signaling at the telomere
  • Abstracts: Nucleosome sliding via TBP DNA binding in vivo. A murine model of Holt-Oram syndrome defines roles of the T-box transcription factor Tbx5 in cardiogenesis and disease
This website is not affiliated with document authors or copyright owners. This page is provided for informational purposes only. Unintentional errors are possible.
Some parts © 2025 Advameg, Inc.