Results 71 to 80 of about 5,149,379 (301)

Microbiome−host proteostasis crosstalk—An emerging perspective on mechanisms and interventions toward healthy longevity

FEBS Letters, EarlyView.
Proteostasis and the gut microbiota play a key role in shaping host physiology. Microbiota‐derived metabolites, vitamins, and RNA modulate host proteostasis. Findings from model systems, including C. elegans, indicate microbes can either stabilize or disrupt host proteostasis.
Abhishek Anil Dubey, Maria Ermolaeva
wiley   +1 more source

Binding behavior of receptor binding domain of the SARS-CoV-2 virus and ivermectin

Scientific Reports
The COVID-19 pandemic, caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), sparked an international debate on effective ways to prevent and treat the virus. Specifically, there were many varying opinions on the use of ivermectin (IVM)
Kasidy R. Gossen, Meiyi Zhang, Zivko L. Nikolov, Sandun D. Fernando, Maria D. King   +4 more
doaj   +1 more source

A dipeptide Insertion in Domain I of Exotoxin A That Impairs Receptor Binding

Journal of Biological Chemistry, 1989
Deletions within the structural exotoxin A gene of 27 or 119 amino acids in domain I of the mature polypeptide, or of 88 or 105 amino acids in domains I and II, resulted in the synthesis of exotoxin A (ETA) polypeptides that were not secreted from Pseudomonas aeruginosa hosts but were localized in the cell membrane.
G J, Chaudry, R B, Wilson, R K, Draper, R C, Clowes   +3 more
openaire   +2 more sources

Receptor binding specificities of Herstatin and its intron 8‐encoded domain [PDF]

FEBS Letters, 2004
Retention of intron 8 in alternative HER‐2 mRNA generates an inhibitory secreted ligand, Herstatin, with a novel receptor‐binding domain (RBD) encoded by the intron. This study examines binding interactions with several receptors and investigates sequence variations in intron 8.
Shamieh, Lara S, Evans, Adam J, Denton, Michael C, Clinton, Gail M   +3 more
openaire   +2 more sources

ABL kinase‐dependent phosphorylation of SH proteins promotes their direct interaction with CRK family SH2 domains

FEBS Letters, EarlyView.
CT10 regulator of kinase (CRK) and CRK‐Like (CRKL) are signaling adaptors driving cell adhesion, motility, differentiation, and proliferation. SH2‐domain containing (SH) proteins are enriched in YXXP motifs which when phosphorylated create preferred binding sites for CRK family SH2 domains.
Phoebe M. Cousens, Brendan W. Chandler, Anna M. Schmoker, Jaye L. Weinert, Charlotte A. Kearns, Warren T. Yacawych, Amila Šemić, Alicia M. Ebert, Bryan A. Ballif   +8 more
wiley   +1 more source

3D model of amphioxus steroid receptor complexed with estradiol [PDF]

, 2009
The origins of signaling by vertebrate steroids are not fully understood. An important advance was the report that an estrogen-binding steroid receptor [SR] is present in amphioxus, a basal chordate with a similar body plan as vertebrates.
Michael E. Baker, David J. Chang
core  

Role of phenylalanine 150 in the receptor-binding domain of the K88 fibrillar subunit [PDF]

Journal of Bacteriology, 1987
Recently, we reported the isolation of three peptides, Ile-83-Ala-Phe-85, Ser-148-Leu-Phe-150, and Ala-156-Ile-Phe-158, derived from the K88 fibrillar subunit and found to inhibit the binding of K88 fibrillae to cavia erythrocytes or pig intestinal epithelial cells (A. A. C. Jacobs, J. Venema, R. Leeven, H. van Pelt-Heerschap, and F. K.
JACOBS, AAC, ROOSENDAAL, B, VANBREEMEN, JFL, DEGRAAF, FK   +3 more
openaire   +3 more sources

Investigating transcription factor dynamics in health and disease using FRAP

FEBS Letters, EarlyView.
FRAP analysis of GFP‐tagged transcription factors reveals how molecular mobility and target engagement change in response to drug treatment. By combining live‐cell imaging, quantitative model fitting, and statistical analysis, this approach uncovers transcription factor dynamics linked to disease mechanisms, providing a powerful framework for ...
Kannan Govindaraj, Carolina Vazquez Garzon, Jose Joaquin Velasco, Janine N. Post   +3 more
wiley   +1 more source

Dss1 Is a 26S Proteasome Ubiquitin Receptor [PDF]

, 2014
The ubiquitin-proteasome system is the major pathway for protein degradation in eukaryotic cells. Proteins to be degraded are conjugated to ubiquitin chains that act as recognition signals for the 26S proteasome.
Hardwick, Kevin G., Hay, Ronald T., Larsen, Ida B., Kragelund, Birthe B., Tatham, Michael H, Rösner, Heike I, Kragelund, Birthe Brandt, Hay, Ronald T, Kragelund, Birthe B, Kriegenburg, Franziska, Tatham, Michael H., Rösner, Heike Ilona, Paraskevopoulos, Konstantinos, Brandstrup, Rikke, Larsen, Ida B, Medina, Bethan; id_orcid, Hartmann-Petersen, Rasmus, Gordon, Colin, Rösner, Heike I., Hardwick, Kevin G, Medina, Bethan   +20 more
core   +1 more source

Structure‐forward targeting of claudins with synthetic binders

FEBS Letters, EarlyView.
Claudins form the paracellular barriers between epithelial and endothelial tissues at tight junctions and are targets for molecular binders with the goal of modulating barrier permeability. Claudin‐binding molecules are relevant in drug delivery or in altering claudin interactions with disease‐causing proteins.
Alex J. Vecchio
wiley   +1 more source