Results 11 to 20 of about 2,652,154 (287)

Parasitic nematode fatty acid- and retinol-binding proteins compromise host immunity by interfering with host lipid signaling pathways [PDF]

PLoS Pathogens, 2021
Parasitic nematodes cause significant morbidity and mortality globally. Excretory/secretory products (ESPs) such as fatty acid- and retinol- binding proteins (FARs) are hypothesized to suppress host immunity during nematode infection, yet little is known
Sophia C. Parks, Susan Nguyen, Shyon Nasrolahi, Chaitra Bhat, Damian Juncaj, Dihong Lu, Raghavendran Ramaswamy, Harpal Dhillon, Hideji Fujiwara, Anna Buchman, Omar S. Akbari, Naoki Yamanaka, Martin J. Boulanger, Adler R. Dillman   +13 more
doaj   +3 more sources

Serum amyloid A is a retinol binding protein that transports retinol during bacterial infection

eLife, 2014
Retinol plays a vital role in the immune response to infection, yet proteins that mediate retinol transport during infection have not been identified.
Mehabaw G Derebe, Clare M Zlatkov, Sureka Gattu, Kelly A Ruhn, Shipra Vaishnava, Gretchen E Diehl, John B MacMillan, Noelle S Williams, Lora V Hooper   +8 more
doaj   +2 more sources

Structure-guided screening of FAR-1 antagonists with multi-stage anthelmintic activity [PDF]

Antimicrobial Agents and Chemotherapy
Fatty acid and retinol binding proteins (FARs) are nematode-specific proteins that orchestrate lipid metabolism, development, and host immune response.
Juan Wen, Wenmin Qi, Jinwei Lv, Yu Lin, Fei Shen, Yu Li, Ziding Zhang, Lihua Xiao, Yaoyu Feng, Dongjuan Yuan   +9 more
doaj   +2 more sources

Retinol-binding protein 3 in ophthalmology: current evidence, research progress, and future perspectives. [PDF]

Front Immunol
Li M, Liang R, Guo S, Zhou X.
europepmc   +3 more sources

The FAR protein family of parasitic nematodes.

PLoS Pathogens, 2022
Fatty acid-and retinol-binding proteins (FARs) belong to a unique family of excreted/secreted proteins (ESPs) found exclusively in nematodes. Much of our understanding of these proteins, however, is limited to their in vitro binding characteristics ...
Sophia C Parks, Susan Nguyen, Martin J Boulanger, Adler R Dillman   +3 more
doaj   +2 more sources

The Impact of Physical Training on Circulating Retinol-Binding Protein 4: A Systematic Review. [PDF]

Physiol Res
Alsahafi Z, Baashar A.
europepmc   +2 more sources

Structural and functional studies of intrinsically disordered fibronectin-binding proteins [PDF]

, 2009
Bacterial fibronectin-binding proteins (FnBPs) mediate adhesion of bacteria to host tissues through binding to the human protein fibronectin (Fn). FnBPs are predicted to contain a series of intrinsically disordered Fn-binding repeats (FnBRs), which ...
Norris, Nicole Catherine
core   +6 more sources

Identification of Transthyretin Tetramer Kinetic Stabilizers That Are Capable of Inhibiting the Retinol-Dependent Retinol Binding Protein 4-Transthyretin Interaction [PDF]

, 2021
Dissociation of transthyretin (TTR) tetramers may lead to misfolding and aggregation of pro-amyloidogenic monomers, which underlies TTR amyloidosis (ATTR) pathophysiology.
Arun, Raja, Andras, Varadi, Aravindan, Jayaraman, Christopher L., Cioffi, Parthasarathy, Muthuraman, Konstantin, Petrukhin, Srinivasan, Jayakumar, Boglarka, Racz   +7 more
core   +1 more source

Dynamic changes in serum albumin, prealbumin, and retinol-binding protein after head and neck cancer surgery: a retrospective cohort study. [PDF]

Front Med (Lausanne)
Huang L, Deng S, Sheng X, Chu H.
europepmc   +3 more sources

Retinoid-binding proteins: similar protein architectures bind similar ligands via completely different ways. [PDF]

PLoS ONE, 2012
BACKGROUND: Retinoids are a class of compounds that are chemically related to vitamin A, which is an essential nutrient that plays a key role in vision, cell growth and differentiation. In vivo, retinoids must bind with specific proteins to perform their
Yu-Ru Zhang, Yu-Qi Zhao, Jing-Fei Huang
doaj   +1 more source