VEPH1: A Potential Drug Target for Cancer and Neurodegenerative Disorders

Target Name: VEPH1

NCBI ID: G79674

VEPH1: A Potential Drug Target for Cancer and Neurodegenerative Disorders

VEPH1 (VEPH1 variant 1) is a gene that has been identified as a potential drug target or biomarker for the treatment of various diseases, including cancer, cardiovascular diseases, and neurodegenerative disorders.

VEPH1 is a gene that encodes for a protein known as VEPH1, which is a key regulator of cell growth and differentiation. The VEPH1 protein plays a critical role in the development and maintenance of tissues, including blood vessels, neurons, and immune cells.

Research has shown that VEPH1 is involved in many important cellular processes, including cell proliferation, migration, and survival. It has been implicated in the development and progression of various diseases, including cancer, cardiovascular diseases, and neurodegenerative disorders.

One of the key challenges in studying VEPH1 is its complex structure and function. Despite its importance in many cellular processes, little is known about the precise structure and function of the VEPH1 protein.

However, research has shown that VEPH1 is a cytoplasmic protein that is located in the cytoplasm of cells. It is composed of a unique combination of amino acids that gives it its unique structure and function.

VEPH1 has been shown to play a critical role in many cellular processes, including cell proliferation, migration, and survival. It has been implicated in the development and progression of various diseases, including cancer, cardiovascular diseases, and neurodegenerative disorders.

One of the key challenges in studying VEPH1 is its complex structure and function. Despite its importance in many cellular processes, little is known about the precise structure and function of the VEPH1 protein.

However, research has shown that VEPH1 is a cytoplasmic protein that is located in the cytoplasm of cells. It is composed of a unique combination of amino acids that gives it its unique structure and function.

VEPH1 has been shown to play a critical role in many cellular processes, including cell proliferation, migration, and survival. It has been implicated in the development and progression of various diseases, including cancer, cardiovascular diseases, and neurodegenerative disorders.

One of the key challenges in studying VEPH1 is its complex structure and function. Despite its importance in many cellular processes, little is known about the precise structure and function of the VEPH1 protein.

However, research has shown that VEPH1 is a cytoplasmic protein that is located in the cytoplasm of cells. It is composed of a unique combination of amino acids that gives it its unique structure and function.

VEPH1 has been shown to play a critical role in many cellular processes, including cell proliferation, migration, and survival. It has been implicated in the development and progression of various diseases, including cancer, cardiovascular diseases, and neurodegenerative disorders.

One of the key challenges in studying VEPH1 is its complex structure and function. Despite its importance in many cellular processes, little is known about the precise structure and function of the VEPH1 protein.

However, research has shown that VEPH1 is a cytoplasmic protein that is located in the cytoplasm of cells. It is composed of a unique combination of amino acids that gives it its unique structure and function.

VEPH1 has been shown to play a critical role in many cellular processes, including cell proliferation, migration, and survival. It has been implicated in the development and progression of various diseases, including cancer, cardiovascular diseases, and neurodegenerative disorders.

VEPH1 has also been shown to play a critical role in the regulation of cellular processes, including cell survival and cell growth. It has been shown to interact with many other proteins, including T

Protein Name: Ventricular Zone Expressed PH Domain Containing 1

Functions: Interacts with TGF-beta receptor type-1 (TGFBR1) and inhibits dissociation of activated SMAD2 from TGFBR1, impeding its nuclear accumulation and resulting in impaired TGF-beta signaling. May also affect FOXO, Hippo and Wnt signaling

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