Yahoo India Web Search

Search results

1. People also ask

   Why is HER2 a human gene?

   • This human gene encodes a protein that has a structure consistent with a growth factor receptor and has been designated HER2, due to its similarity to the human epidermal growth factor receptor [2, 3]. The HER2 receptor has an important role in normal cell growth and differentiation.

   The basic biology of HER2 - Annals of Oncology

   www.annalsofoncology.org/article/S0923-7534(19)54455-6/pdf

   See all results for this question

   Is HER2 a ligand?

   • The human protein is also frequently referred to as HER2 (human epidermal growth factor receptor 2) or CD340 ( cluster of differentiation 340). HER2 is a member of the human epidermal growth factor receptor (HER/EGFR/ERBB) family. But contrary to other members of the ERBB family, HER2 does not directly bind ligand.

   HER2 - Wikipedia

   en.wikipedia.org/wiki/HER2

   See all results for this question

   What is the structure of HER2 and Neu proteins?

   • Structure of the HER2 and Neu proteins. The domain structure is shown on the left consisting of two ligand binding regions (LD1 & LD2), two cysteine-rich regions (CR1 & CR2), a short transmembrane domain (TM), a catalytic tyrosine kinase domain (TK), and a carboxy terminal tail (CT).

   The oncogene HER2; Its signaling and transforming functions and its

   www.ncbi.nlm.nih.gov/pmc/articles/PMC3021475/

   See all results for this question

   What is the structure of the HER2–HER3 Fab complex?

   • Our structure of the HER2 (S310F)–HER3–NRG1β–trastuzumab Fab complex reveals that the receptor dimer undergoes a conformational change to accommodate trastuzumab. Thus, similar to oncogenic mutations, therapeutic agents exploit the intrinsic dynamics of the HER2–HER3 heterodimer.

   Structures of the HER2–HER3–NRG1β complex reveal a

   www.nature.com/articles/s41586-021-04084-z

   See all results for this question

2. Images

   • 
   • 
   • 
   • 

   View all

3. www.nature.com › articles › s41421/023/00523-5Structure and dynamics of the EGFR/HER2 heterodimer

   www.nature.com › articles › s41421/023/00523-5

   Feb 13, 2023 · 16 Citations. 11 Altmetric. Metrics. Abstract. HER2 belongs to the human epidermal growth factor receptor tyrosine kinase family. Its overexpression or hyperactivation is a leading cause for...

   • Metrics

     Metrics - Structure and dynamics of the EGFR/HER2...

   • Full Size Image

     Full Size Image - Structure and dynamics of the EGFR/HER2...

4. en.wikipedia.org › wiki › HER2HER2 - Wikipedia

   en.wikipedia.org › wiki › HER2

   • Cached

   HER2 is so named because it has a similar structure to human epidermal growth factor receptor, or HER1. Neu is so named because it was derived from a rodent glioblastoma cell line, a type of neural tumor.

5. www.ncbi.nlm.nih.gov › pmc › articlesHER 2: Biology, Detection, and Clinical Implications - PMC

   www.ncbi.nlm.nih.gov › pmc › articles

   HER2 is a membrane tyrosine kinase and oncogene that is overexpressed and gene amplified in about 20% of breast cancers. When activated it provides the cell with potent proliferative and anti-apoptosis signals and it is the major driver of tumor development and progression for this subset of breast cancer.

   • Author: Carolina Gutierrez, Rachel Schiff
   • DOI: 10.1043/2010-0454-RAR.1

   • Publish Year: 2011
   • Published: 2011/01

6. www.nature.com › articles › s41586/021/04084-zStructures of the HER2–HER3–NRG1β complex reveal a dynamic ...

   www.nature.com › articles › s41586/021/04084-z

   Nov 10, 2021 · Our structure of the HER2 (S310F)–HER3–NRG1β–trastuzumab Fab complex reveals that the receptor dimer undergoes a conformational change to accommodate trastuzumab. Thus, similar to...

   • Author: Devan Diwanji, Raphael Trenker, Tarjani M. Thaker, Tarjani M. Thaker, Feng Wang, David A. Agard, Kli...

   • Publish Year: 2021

7. www.ncbi.nlm.nih.gov › pmc › articlesThe oncogene HER2; Its signaling and transforming functions ...

   www.ncbi.nlm.nih.gov › pmc › articles

   Oct 4, 2007 · Structure of the HER2 and Neu proteins. The domain structure is shown on the left consisting of two ligand binding regions (LD1 & LD2), two cysteine-rich regions (CR1 & CR2), a short transmembrane domain (TM), a catalytic tyrosine kinase domain (TK), and a carboxy terminal tail (CT).

   • Author: Mark M. Moasser
   • DOI: 10.1038/sj.onc.1210477

   • Publish Year: 2007
   • Published: 2007/10/10

8. www.annalsofoncology.org › article › S0923-7534(19The basic biology of HER2 - Annals of Oncology

   www.annalsofoncology.org › article › S0923-7534(19

   Summary. Human epidermal growth factor receptors (HER/ erb B) constitute a family of four cell surface receptors involved in transmission of signals controlling normal cell growth and differentiation. A range of growth factors serve as ligands, but none is specific for the HER2 receptor.

9. www.annalsofoncology.org › article › S0923-7534(19The basic biology of HER2 - Annals of Oncology

   www.annalsofoncology.org › article › S0923-7534(19

   Structure of the HER2 protein and its transmembrane topology. and Drosophila melanogaster. These organisms only have one HER receptor. Although the receptor in C. elegans has one ligand, the receptor in fruit flies {Drosophila melanogaster) has four ligands.