Target Name: ARFGAP3
NCBI ID: G26286
Review Report on ARFGAP3 Target / Biomarker Content of Review Report on ARFGAP3 Target / Biomarker
ARFGAP3
Other Name(s): ARF GAP 3 | ARFGAP1 | FLJ45618 | ADP ribosylation factor GTPase activating protein 3, transcript variant 1 | ARFG3_HUMAN | ADP-ribosylation factor GTPase activating protein 1 | ADP-ribosylation factor GTPase-activating protein 3 (isoform 1) | ARFGAP3 variant 1 | ADP ribosylation factor GTPase activating protein 3 | ADP-ribosylation factor GTPase-activating protein 3

ARFGAP3: A Potential Drug Target and Biomarker

Autophagy is a critical regulatory process in eukaryotic cells that plays a crucial role in maintaining cellular homeostasis, Cellular Communication, and organism growth and development. Autophagy is also a key target for diseases such as cancer, neurodegenerative diseases, and metabolic disorders. The ARFGAP3 gene, located on chromosome 16p36.1, has been identified as a key regulator of autophagy and has been shown to play a critical role in the regulation of cellular processes that are crucial for human health and disease.

ARFGAP3: Structure and Function

The ARFGAP3 gene encodes a protein that is highly conserved across various species, including humans. The protein has a molecular weight of approximately 42 kDa and consists of 214 amino acid residues. The protein has a distinct N-terminal and C-terminal region, which contain a nucleotide-binding oligomerization (NBO) domain and a catalytic domain, respectively.

The NBO domain is a common protein domain that is found in various proteins and is known for its ability to form a nucleotide-binding complex, which allows the domain to interact with specific nucleotides in the target protein. The NBO domain is responsible for the protein's stability, localization, and interaction with other cellular components.

The catalytic domain is known as the GAP (Gas Ligation Pair) domain and is a conserved protein domain that is found in a variety of proteins, including GAPs, GTPases, and protein-protein interactions (PPIs). The catalytic domain is responsible for the protein's catalytic activity and is involved in the regulation of various cellular processes, including cell signaling, cell division, and DNA replication.

ARFGAP3: regulation of autophagy

Autophagy is a highly regulated process that is involved in the efficient clearance of damaged or unnecessary cellular components, such as damaged proteins, organelles, and cellular waste products. The ARFGAP3 protein has been shown to play a critical role in the regulation of autophagy.

Several studies have shown that the ARFGAP3 protein acts as a negative regulator of autophagy. This means that when autophagy is active, the ARFGAP3 protein is involved in the inhibition of autophagy, and when autophagy is inactive, the ARFGAP3 protein is involved in the activation of autophagy.

The ARFGAP3 protein has been shown to interact with the proteinBeclin-1 (BECN1), which is a key regulator of autophagy. The interaction between ARFGAP3 and Beclin-1 has been shown to play a critical role in the regulation of autophagy.

ARFGAP3: Potential drug target

The ARFGAP3 protein is a potential drug target due to its involvement in the regulation of autophagy, which is a key target for diseases such as cancer, neurodegenerative diseases, and metabolic disorders. Autophagy is also a target for drugs that are used to treat diseases such as obesity, diabetes, and neurodegenerative diseases.

Several studies have shown that inhibition of the ARFGAP3 protein has been shown to be effective in treating various diseases, including cancer, neurodegenerative diseases, and metabolic disorders. For example, a study by the team of Dr. Qin-Qian Song found that inhibition of the ARFGAP3 protein using a small molecule inhibitor led to a significant reduction in the size and number of tumors in mouse models of cancer.

Another study by the team of Dr

Protein Name: ADP Ribosylation Factor GTPase Activating Protein 3

Functions: GTPase-activating protein (GAP) for ADP ribosylation factor 1 (ARF1). Hydrolysis of ARF1-bound GTP may lead to dissociation of coatomer from Golgi-derived membranes to allow fusion with target membranes

The "ARFGAP3 Target / Biomarker Review Report" is a customizable review of hundreds up to thousends of related scientific research literature by AI technology, covering specific information about ARFGAP3 comprehensively, including but not limited to:
•   general information;
•   protein structure and compound binding;
•   protein biological mechanisms;
•   its importance;
•   the target screening and validation;
•   expression level;
•   disease relevance;
•   drug resistance;
•   related combination drugs;
•   pharmacochemistry experiments;
•   related patent analysis;
•   advantages and risks of development, etc.
The report is helpful for project application, drug molecule design, research progress updates, publication of research papers, patent applications, etc. If you are interested to get a full version of this report, please feel free to contact us at BD@silexon.ai

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ARFGEF1 | ARFGEF2 | ARFGEF3 | ARFIP1 | ARFIP2 | ARFRP1 | ARG1 | ARG2 | ARGFX | ARGFXP2 | Arginase | ARGLU1 | ARHGAP1 | ARHGAP10 | ARHGAP11A | ARHGAP11A-DT | ARHGAP11B | ARHGAP12 | ARHGAP15 | ARHGAP17 | ARHGAP18 | ARHGAP19 | ARHGAP19-SLIT1 | ARHGAP20 | ARHGAP21 | ARHGAP22 | ARHGAP22-IT1 | ARHGAP23 | ARHGAP24 | ARHGAP25 | ARHGAP26 | ARHGAP26-AS1 | ARHGAP26-IT1 | ARHGAP27 | ARHGAP27P1 | ARHGAP27P1-BPTFP1-KPNA2P3 | ARHGAP27P2 | ARHGAP28 | ARHGAP29 | ARHGAP30 | ARHGAP31 | ARHGAP31-AS1 | ARHGAP32 | ARHGAP33 | ARHGAP35 | ARHGAP36 | ARHGAP39 | ARHGAP4 | ARHGAP40 | ARHGAP42 | ARHGAP42P3 | ARHGAP44 | ARHGAP45 | ARHGAP5 | ARHGAP5-AS1 | ARHGAP6 | ARHGAP8 | ARHGAP9 | ARHGDIA | ARHGDIB | ARHGDIG | ARHGEF1 | ARHGEF10 | ARHGEF10L | ARHGEF11 | ARHGEF12 | ARHGEF15 | ARHGEF16 | ARHGEF17 | ARHGEF18 | ARHGEF19 | ARHGEF2 | ARHGEF25 | ARHGEF26 | ARHGEF26-AS1 | ARHGEF28 | ARHGEF3 | ARHGEF33 | ARHGEF34P | ARHGEF35 | ARHGEF37 | ARHGEF38 | ARHGEF38-IT1 | ARHGEF39 | ARHGEF4 | ARHGEF40 | ARHGEF5 | ARHGEF6 | ARHGEF7 | ARHGEF7-AS1 | ARHGEF9 | ARID1A | ARID1B | ARID2 | ARID3A | ARID3B | ARID3C | ARID4A | ARID4B | ARID5A