LRP: a multifunctional scavenger and signaling receptor

J Herz, DK Strickland - The Journal of clinical investigation, 2001 - Am Soc Clin Investig
The LDL receptor–related protein (LRP) is larger than but structurally similar to other
members of the LDL receptor gene family, an ancient family of endocytic receptors (1–3) …

The importance of being proline: the interaction of proline‐rich motifs in signaling proteins with their cognate domains

BK Kay, MP Williamson, M Sudol - The FASEB journal, 2000 - Wiley Online Library
ABSTRACT A common focus among molecular and cellular biologists is the identification of
proteins that interact with each other. Yeast two‐hybrid, cDNA expression library screening …

[HTML][HTML] A WW domain‐containing yes‐associated protein (YAP) is a novel transcriptional co‐activator

R Yagi, LF Chen, K Shigesada, Y Murakami… - The EMBO journal, 1999 - embopress.org
A protein module called the WW domain recognizes and binds to a short oligopeptide called
the PY motif, PPxY, to mediate protein–protein interactions. The PY motif is present in the …

Ena/VASP proteins: regulators of the actin cytoskeleton and cell migration

M Krause, EW Dent, JE Bear… - Annual review of cell …, 2003 - annualreviews.org
▪ Abstract Ena/VASP proteins are a conserved family of actin regulatory proteins made up of
EVH1, EVH2 domains, and a proline-rich central region. They have been implicated in actin …

Proteolytic processing and cell biological functions of the amyloid precursor protein

B De Strooper, W Annaert - Journal of cell science, 2000 - journals.biologists.com
Recent research has identified some key players involved in the proteolytic processing of
amyloid precursor protein (APP) to amyloid β-peptide, the principal component of the …

Physical interaction with Yes-associated protein enhances p73 transcriptional activity

S Strano, E Munarriz, M Rossi, L Castagnoli… - Journal of Biological …, 2001 - ASBMB
Specific protein-protein interactions are involved in a large number of cellular processes and
are mainly mediated by structurally and functionally defined domains. Here we report that …

WW domain-containing protein YAP associates with ErbB-4 and acts as a co-transcriptional activator for the carboxyl-terminal fragment of ErbB-4 that translocates to …

A Komuro, M Nagai, NE Navin, M Sudol - Journal of Biological Chemistry, 2003 - ASBMB
The ErbB-4 receptor protein-tyrosine kinase is proteolytically processed by membrane
proteases in response to the ligand or 12-O-tetradecanoylphorbol-13-acetate stimulation …

[HTML][HTML] WW and SH3 domains, two different scaffolds to recognize proline-rich ligands

MJ Macias, S Wiesner, M Sudol - FEBS letters, 2002 - Elsevier
WW domains are small protein modules composed of approximately 40 amino acids. These
domains fold as a stable, triple stranded β-sheet and recognize proline-containing ligands …

Structural basis for phosphoserine-proline recognition by group IV WW domains

MA Verdecia, ME Bowman, KP Lu, T Hunter… - Nature structural …, 2000 - nature.com
Pin1 contains an N-terminal WW domain and a C-terminal peptidyl-prolyl cis-trans
isomerase (PPIase) domain connected by a flexible linker. To address the energetic and …

Lipoprotein receptors in the nervous system

J Herz, HH Bock - Annual review of biochemistry, 2002 - annualreviews.org
▪ Abstract The low-density–lipoprotein (LDL) receptor family is an evolutionarily ancient
gene family of structurally closely related cell-surface receptors. Members of the family are …