Human protein tyrosine phosphatase 1B (PTP1B): from structure to clinical inhibitor perspectives
R Liu, C Mathieu, J Berthelet, W Zhang… - International Journal of …, 2022 - mdpi.com
Phosphorylation is an essential process in biological events and is considered critical for
biological functions. In tissues, protein phosphorylation mainly occurs on tyrosine (Tyr) …
biological functions. In tissues, protein phosphorylation mainly occurs on tyrosine (Tyr) …
[HTML][HTML] The post-translational modification, SUMOylation, and cancer
ZJ Han, YH Feng, BH Gu, YM Li… - … journal of oncology, 2018 - spandidos-publications.com
SUMOylation is a reversible post-translational modification which has emerged as a crucial
molecular regulatory mechanism, involved in the regulation of DNA damage repair, immune …
molecular regulatory mechanism, involved in the regulation of DNA damage repair, immune …
Concepts in sumoylation: a decade on
R Geiss-Friedlander, F Melchior - Nature reviews Molecular cell biology, 2007 - nature.com
A decade has passed since SUMO (small ubiquitin-related modifier) was discovered to be a
reversible post-translational protein modifier. During this time many enzymes that participate …
reversible post-translational protein modifier. During this time many enzymes that participate …
Mechanisms, regulation and consequences of protein SUMOylation
KA Wilkinson, JM Henley - Biochemical Journal, 2010 - portlandpress.com
The post-translational modification SUMOylation is a major regulator of protein function that
plays an important role in a wide range of cellular processes. SUMOylation involves the …
plays an important role in a wide range of cellular processes. SUMOylation involves the …
The SUMO modification pathway is involved in the BRCA1 response to genotoxic stress
Mutations in BRCA1 are associated with a high risk of breast and ovarian cancer. BRCA1
participates in the DNA damage response and acts as a ubiquitin ligase. However, its …
participates in the DNA damage response and acts as a ubiquitin ligase. However, its …
MAPL is a new mitochondrial SUMO E3 ligase that regulates mitochondrial fission
E Braschi, R Zunino, HM McBride - EMBO reports, 2009 - embopress.org
The modification of proteins by the small ubiquitin‐like modifier (SUMO) is known to regulate
an increasing array of cellular processes. SUMOylation of the mitochondrial fission GTPase …
an increasing array of cellular processes. SUMOylation of the mitochondrial fission GTPase …
Protein-tyrosine phosphatase 1B expression is induced by inflammation in vivo
Protein-tyrosine phosphatase 1B (PTP1B) is a major negative regulator of insulin and leptin
sensitivity. PTP1B overexpression in adipose tissue and skeletal muscle of humans and …
sensitivity. PTP1B overexpression in adipose tissue and skeletal muscle of humans and …
PTP1B: a simple enzyme for a complex world
M Feldhammer, N Uetani… - Critical reviews in …, 2013 - Taylor & Francis
Our understanding of the fundamental regulatory roles that tyrosine phosphatases play
within cells has advanced significantly in the last two decades. Out-dated ideas that tyrosine …
within cells has advanced significantly in the last two decades. Out-dated ideas that tyrosine …
PTP1B: a double agent in metabolism and oncogenesis
SC Yip, S Saha, J Chernoff - Trends in biochemical sciences, 2010 - cell.com
PTP1B, a non-transmembrane protein tyrosine phosphatase that has long been studied as a
negative regulator of insulin and leptin signaling, has received renewed attention as an …
negative regulator of insulin and leptin signaling, has received renewed attention as an …
[HTML][HTML] Protein tyrosine phosphatase 1B (PTP1B) as a potential therapeutic target for neurological disorders
J Olloquequi, A Cano, E Sanchez-López… - Biomedicine & …, 2022 - Elsevier
Protein tyrosine phosphatase 1B (PTP1B) is a typical member of the PTP family, considered
a direct negative regulator of several receptor and receptor-associated tyrosine kinases …
a direct negative regulator of several receptor and receptor-associated tyrosine kinases …