Target Name: INIP
NCBI ID: G58493
Review Report on INIP Target / Biomarker Content of Review Report on INIP Target / Biomarker
INIP
Other Name(s): SOSSC | sensor of single-strand DNA complex subunit C | SOSS complex subunit C (isoform a) | INTS3 and NABP interacting protein, transcript variant 1 | INIP variant 1 | SOSS complex subunit C | SOSS-C | minute INTS3/hSSB-associated element | HSSB-interacting protein 1 | Sensor of single-strand DNA complex subunit C | HSPC043 | HSSBIP1 | hSSBIP1 | hSSB-interacting protein 1 | SSB-interacting protein 1 | INTS3- and NABP-interacting protein | single-stranded DNA-binding protein-interacting protein 1 | OTTHUMP00000021941 | Minute INTS3/hSSB-associated element | SSBIP1 | MISE | sensor of ssDNA subunit C | INTS3 and NABP interacting protein | RP11-276E15.2 | SOSSC_HUMAN | Single-stranded DNA-binding protein-interacting protein 1 | C9orf80 | Sensor of ssDNA subunit C

The Importance of INIP (Insulin-like Growth Factor-1)

INIP is a protein that plays a crucial role in the regulation of various physiological processes in the body. It is a member of the insulin-like growth factor family, which includes proteins that regulate cell growth, differentiation, and survival. INIP is a potent growth factor that has been shown to promote the growth and survival of various cell types, including cancer cells.

The Identification of INIP as a Potential Drug Target

The potential to target INIP as a drug has been identified through a variety of studies. INIP has been shown to promote the growth and survival of various cancer cells, including breast, ovarian, and prostate cancer cells. It has also been shown to enhance the sensitivity of cancer cells to chemotherapy drugs. These findings suggest that INIP may be an effective target for cancer treatment.

The Structure and Function of INIP

INIP is a transmembrane protein that consists of four distinct domains: an extracellular domain, a transmembrane domain, an intracellular domain, and a C-terminal region that contains a conserved amino acid sequence. The extracellular domain of INIP consists of a catalytic tyrosine residue , which is responsible for the protein's ability to interact with other proteins. The transmembrane domain of INIP is responsible for the regulation of the protein's trafficking and localization to the cell surface. The intracellular domain of INIP is responsible for the regulation of the protein's stability and interactions with various cellular signaling pathways.

The INIP-Cancer Connection

INIP has been shown to promote the growth and survival of various cancer cells. It has been shown to enhance the sensitivity of cancer cells to chemotherapy drugs and to promote the formation of cancer stem cells. These findings suggest that INIP may be a potential drug target for cancer treatment.

The Potential therapeutic benefits of INIP are enormous. It has the potential to be used in the treatment of various types of cancer, including breast, ovarian, and prostate cancer. It has also been shown to have potential therapeutic applications in the treatment of other diseases , including cardiovascular disease and neurodegenerative diseases.

The Future of INIP Research

The future of INIP research is promising. With the identification of INIP as a potential drug target, there is a growing interest in the development of INIP-based therapies for cancer treatment. Researchers are currently working to develop INIP-based drugs that can selectively target INIP and to evaluate the efficacy of these drugs in a variety of cancer models.

Conclusion

INIP is a protein that has been shown to play a crucial role in the regulation of various physiological processes in the body. Its potential as a drug target has been identified through a variety of studies, and it has the potential to be used in the treatment of various types of cancer. Further research is needed to fully understand the therapeutic potential of INIP and to develop effective INIP-based therapies for cancer treatment.

Protein Name: INTS3 And NABP Interacting Protein

Functions: Component of the SOSS complex, a multiprotein complex that functions downstream of the MRN complex to promote DNA repair and G2/M checkpoint. The SOSS complex associates with single-stranded DNA at DNA lesions and influences diverse endpoints in the cellular DNA damage response including cell-cycle checkpoint activation, recombinational repair and maintenance of genomic stability. Required for efficient homologous recombination-dependent repair of double-strand breaks (DSBs) and ATM-dependent signaling pathways

The "INIP 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 INIP 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

More Common Targets

INKA1 | INKA2 | INKA2-AS1 | INMT | INMT-MINDY4 | Innate Repair Receptor (IRR) | INO80 | INO80 complex | INO80B | INO80B-WBP1 | INO80C | INO80D | INO80E | Inositol 1,4,5-Trisphosphate Receptor (InsP3R) | Inositol hexakisphosphate kinase | Inositol Monophosphatase | INPP1 | INPP4A | INPP4B | INPP5A | INPP5B | INPP5D | INPP5E | INPP5F | INPP5J | INPP5K | INPPL1 | INS | INS-IGF2 | INSC | INSIG1 | INSIG2 | INSL3 | INSL4 | INSL5 | INSL6 | INSM1 | INSM2 | INSR | INSRR | Insulin-like growth factor | Insulin-like growth factor 2 mRNA binding protein | Insulin-like growth factor 2 mRNA-binding protein 1 (isoform 2) | Insulin-like growth factor-binding protein | INSYN1 | INSYN2A | INSYN2B | Integrator complex | Integrin alpha1beta1 (VLA-1) receptor | Integrin alpha2beta1 (VLA-2) receptor | Integrin alpha2beta3 Receptor | Integrin alpha3beta1 receptor | Integrin alpha4beta1 (VLA-4) receptor | Integrin alpha4beta7 (LPAM-1) receptor | Integrin alpha5beta1 (VLA-5) receptor | Integrin alpha5beta3 receptor | Integrin alpha6beta1 Receptor | Integrin alpha6beta4 receptor | Integrin alpha7beta1 Receptor | Integrin alpha9beta1 receptor | Integrin alphaEbeta7 receptor | Integrin alphaLbeta2 (LFA-1) receptor | Integrin alphaMbeta2 (MAC-1) Receptor | Integrin alphavbeta1 | Integrin alphavbeta3 (vitronectin) receptor | Integrin alphavbeta5 receptor | Integrin alphavbeta6 receptor | Integrin alphavbeta8 Receptor | Integrin Receptor | Integrin-linked kinase | Interferon | Interferon-alpha (IFN-alpha) | Interferon-gamma Receptor | Interleukin 17 | Interleukin 21 receptor complex | Interleukin 23 complex (IL-23) | Interleukin 35 | Interleukin-1 | Interleukin-1 receptor-associated kinase (IRAK) | Interleukin-12 (IL-12) | Interleukin-18 Receptor Complex | Interleukin-27 (IL-27) Complex | Interleukin-39 (IL-39) | Interleukin-7 receptor | Intraflagellar transport complex | Intraflagellar transport complex A | Intraflagellar transport complex B | Intrinsic Tenase Complex | INTS1 | INTS10 | INTS11 | INTS12 | INTS13 | INTS14 | INTS15 | INTS2 | INTS3 | INTS4 | INTS4P1 | INTS4P2