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) …

[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 …

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 …

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 …

The SUMO modification pathway is involved in the BRCA1 response to genotoxic stress

JR Morris, C Boutell, M Keppler, R Densham… - Nature, 2009 - nature.com
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 …

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 …

Protein-tyrosine phosphatase 1B expression is induced by inflammation in vivo

JM Zabolotny, YB Kim, LA Welsh, EE Kershaw… - Journal of Biological …, 2008 - ASBMB
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 …

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 …

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 …

[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 …