Results 31 to 40 of about 1,195,639 (276)

Purification of rabbit serum histidine-proline-rich glycoprotein via preparative gel electrophoresis and characterization of its glycosylation patterns. [PDF]

PLoS ONE, 2017
Histidine-Proline-rich Glycoprotein (HPRG) is a plasma protein of vertebrates and several marine bivalves. Due to its multidomain structure consisting of several regions HPRG can interact with a variety of ligands, however the exact physiological role ...
Anna Katharina Weyrauch, Mario Jakob, Angelika Schierhorn, Ralf Bernd Klösgen, Dariush Hinderberger   +4 more
doaj   +1 more source

Structural insights into an engineered feruloyl esterase with improved MHET degrading properties

FEBS Letters, EarlyView.
A feruloyl esterase was engineered to mimic key features of MHETase, enhancing the degradation of PET oligomers. Structural and computational analysis reveal how a point mutation stabilizes the active site and reshapes the binding cleft, expading substrate scope.
Panagiota Karampa, Konstantinos Makryniotis, Theofani‐Iosifina Sousani, Evangelos Topakas, Vangelis Daskalakis, Maria Dimarogona   +5 more
wiley   +1 more source

Structural insights and therapeutic targets in Acinetobacter baumannii capsule biosynthesis

FEBS Letters, EarlyView.
Hypervirulent KL49 A. baumannii's capsular polysaccharide contains the nonulosonic acid 8‐epi‐Leg5,7Ac2, synthesized by epimerization via ElaA, ElaB, and ElaC. Crystal structures of ElaA, ElaB, and ElaC reveal their role in CMP‐Leg5,7Ac2 synthesis and regioselective C8 epimerization.
Woo Cheol Lee, Junho Jeong, Chae Yeong Lee, Hyunjoon Cho, Man Hwan Oh, Je Chul Lee, Jee‐Young Lee, Yangmee Kim   +7 more
wiley   +1 more source

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

Affinity chromatography of native and recombinant proteins-from receptors for insulin and IGF-I to recombinant single chain antibodies

Frontiers in Endocrinology, 2015
Affinity chromatography is an efficient method to isolate proteins by taking advantage of their affinities for specific molecules such as substrates, inhibitors, antigens, ligands, antibodies, and other interacting molecules including subunits. Nowadays,
Yoko eFujita-Yamaguchi
doaj   +1 more source

Identification of a Shiga toxin A‐derived peptide internalized into Gb3 receptor‐bearing cells via interaction with the Shiga toxin B subunit

FEBS Letters, EarlyView.
The process of internalization of the Shiga toxin A subunit via formation of a complex with the Shiga toxin B subunit, which specifically binds to the Gb3 receptor. The peptide is designed to act as a carrier of drugs into cancer cells. Here, we explored the potential of peptides derived from the catalytic A subunit of Shiga toxin (STxA) to be drug ...
Giulia Opassi, João C. Encarnação, Valeria Napolitano, Grzegorz Dubin, Grzegorz Popowicz, Karl Andersson, U. Helena Danielson   +6 more
wiley   +1 more source

Conserved binding mode but diverse interfaces of MreC‐PBP2 interactions

FEBS Letters, EarlyView.
The crystal structure of abMreC reveals a conserved two β‐barrel architecture and provides structural insights into its role within the bacterial elongasome. The abMreC–abPBP2 complex model identifies the molecular basis of MreC‐mediated PBP2 recognition, contributing to the regulation of peptidoglycan synthesis.
Hyunseok Jang, Hyo Been Jin, Chang Min Kim, So Yeon Lee, Hyun Ho Park   +4 more
wiley   +1 more source

Incremental Modification in the Existing Approaches for Affinity Chromatographic Enrichment of Phosphoproteins Improves Their Profile in Liquid Chromatography‐Tandem Mass Spectrometry Analysis

Analytical Science Advances
Cell signalling is a vital process in cell physiology, which is driven by protein phosphorylation. Global phosphoproteome analysis by liquid chromatography‐tandem mass spectrometry (LC‐MS/MS) has thus gained importance in cell signalling research ...
Neha Agrawal, Rukmini Govekar
doaj   +1 more source

Consecutive Affinity and Ion-Exchange Chromatography for AAV9 Vectors Purification

Biomedicines
Background: Irrespective of the rapid development of AAV-based gene therapy, the production of clinical-grade vectors has a bottleneck resulting from product-related impurities such as empty and partially filled capsids, which lack a functional ...
Ozgun Firat Duzenli, George Aslanidi
doaj   +1 more source

Single bead affinity detection (SINBAD) for the analysis of protein-protein interactions. [PDF]

PLoS ONE, 2008
We present a miniaturized pull-down method for the detection of protein-protein interactions using standard affinity chromatography reagents. Binding events between different proteins, which are color-coded with quantum dots (QDs), are visualized on ...
Roberta Schulte, Jessica Talamas, Christine Doucet, Martin W Hetzer   +3 more
doaj   +1 more source