PIP(2) and proteins: interactions, organization, and information flow.

By S. McLaughlin, Jiyao Wang, A. Gambhir, D. Murray. Annual Review of Biophysics and Biomolecular Structure, 2002

773 citations recorded by the source corpus.

Subfields: Cell Biology, Molecular Biology, Physiology

View Paper: https://www.semanticscholar.org/paper/87cada811778af75ce207974b4967b3ce96cd2fc

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Cell Biology

1. M. Gerl
2. Jonathan C. Kagan
3. R. Medzhitov
4. K. Simons
5. G. Nicolson
6. C. Dart

In Molecular Biology

1. M. Gerl
2. Jonathan C. Kagan
3. R. Medzhitov
4. K. Simons
5. G. Nicolson
6. C. Dart
7. Kevin J. Tracey

In Physiology

1. Jonathan C. Kagan
2. R. Medzhitov
3. K. Simons
4. C. Dart

Citations in the corpus

• Revitalizing membrane rafts: new tools and insights (2010, background): “Why would a phospholipid with a polyunsaturated fatty acid be included in a raft domain? Proteins such as myristoylated Ala-rich C-kinase substrate (MARCKS) and growth-associated protein 43 (GAP43) that bind to PtdIns(4,5)P 2 have been proposed to polymerize and tightly cluster PtdIns(4,5)P 2 in t”
• Phosphoinositide-mediated adaptor recruitment controls Toll-like receptor signaling. (2006, positive): “PIP2 has multiple functions in cellular physiology, and its local concentrations are controlled by many signaling pathways (McLaughlin et al., 2002).”