Results 101 to 110 of about 83,408 (297)

Role of protein disulfide isomerase in activation of integrins

Postępy Higieny i Medycyny Doświadczalnej, 2014
Integrins belong to a large family of transmembrane cell adhesion receptors that communicate biochemical and mechanical signals in a bidirectional manner across the plasma membrane. Integrins and their ligands play a crucial role in a number of physiological and pathological processes, including cell migration, cell differentiation, hemostasis ...
Halszka Ponamarczuk, Marcin Popielarski, Katarzyna Sobierajska, Maria Swiątkowska   +3 more
openaire   +2 more sources

Protein disulfide isomerase mediates integrin‐dependent adhesion [PDF]

FEBS Letters, 2000
Cell adhesion is mediated by the integrin adhesion receptors. Receptor–ligand interaction involves conformational changes in the receptor, but the underlying mechanism remains unclear. Our earlier work implied a role for sulfhydryls in integrin response to ligand binding in the intact blood platelet.
N. Gofer-Dadosh, N. Gofer-Dadosh, J. Luboshitz, J. Luboshitz, Judith Lahav, Judith Lahav, O. Hess, O. Hess, Mati Shaklai, Mati Shaklai   +9 more
openaire   +3 more sources

Multistep, sequential control of the trafficking and function of the multiple sulfatase deficiency gene product, SUMF1 by PDI, ERGIC-53 and ERp44. [PDF]

, 2008
Sulfatase modifying factor 1 (SUMF1) encodes for the formylglicine generating enzyme, which activates sulfatases by modifying a key cysteine residue within their catalytic domains. SUMF1 is mutated in patients affected by multiple sulfatase deficiency, a
Annunziata F., BALLABIO, ANDREA, Cosma M. P., Cozzolino M., FRALDI, ALESSANDRO, Lombardi A., MONTI, MARIA, PUCCI, PIETRO, Sitia R., Spampanato C., Zito E.   +10 more
core   +1 more source

A Protein Disulfide Isomerase Controls Neuronal Migration through Regulation of Wnt Secretion

Cell Reports, 2019
Summary: Appropriate Wnt morphogen secretion is required to control animal development and homeostasis. Although correct Wnt globular structure is essential for secretion, proteins that directly mediate Wnt folding and maturation remain uncharacterized ...
Nanna Torpe, Sandeep Gopal, Oguzhan Baltaci, Lorenzo Rella, Ava Handley, Hendrik C. Korswagen, Roger Pocock   +6 more
doaj  

Biochemical analysis of Komagataella phaffii oxidative folding proposes novel regulatory mechanisms of disulfide bond formation in yeast

Scientific Reports, 2023
Oxidative protein folding in the endoplasmic reticulum (ER) is driven mainly by protein disulfide isomerase PDI and oxidoreductin Ero1. Their activity is tightly regulated and interconnected with the unfolded protein response (UPR).
Arianna Palma, Lukas A. Rettenbacher, Antti Moilanen, Mirva Saaranen, Christian Pacheco-Martinez, Brigitte Gasser, Lloyd Ruddock   +6 more
doaj   +1 more source

Rapid expansion of the protein disulfide isomerase gene family facilitates the folding of venom peptides

Proceedings of the National Academy of Sciences of the United States of America, 2016
Significance The majority of secreted proteins contain disulfide bonds that provide structural stability in the extracellular environment. The formation of correct disulfide bonds is assisted by the enzyme protein disulfide isomerase (PDI). Most secreted
Helena Safavi-Hemami, Qing Li, R. L. Jackson, A. Song, Wouter Boomsma, P. Bandyopadhyay, Christian W. Gruber, A. Purcell, M. Yandell, B. Olivera, L. Ellgaard   +10 more
semanticscholar   +1 more source

Proteome Analysis of Corynebacterium diphtheriae–Macrophage Interaction

PROTEOMICS, EarlyView.
ABSTRACT Contact of Corynebacterium diphtheriae with macrophages induces adaptations on both bacterial and cellular sides. The study presented here was aiming to shed light on the simultaneous intracellular adaptation of the bacteria and changes in the proteome of the phagocytes in response to the internalization of C. diphtheriae.
Luca Musella, Jens Möller, Christopher Lischer, Julio Vera‐Gonzalez, Jörg Hofmann, Lisa Ott, Andreas Burkovski   +6 more
wiley   +1 more source

Binding Differences of the Peptide‐Substrate–Binding Domain of Collagen Prolyl 4‐Hydroxylases I and II for Proline‐ and Hydroxyproline‐Rich Peptides

Proteins: Structure, Function, and Bioinformatics, EarlyView.
ABSTRACT Collagen prolyl 4‐hydroxylase (C‐P4H) catalyzes the 4‐hydroxylation of Y‐prolines of the XYG‐repeat of procollagen. C‐P4Hs are tetrameric α2β2 enzymes. The α‐subunit provides the N‐terminal dimerization domain, the middle peptide‐substrate–binding (PSB) domain, and the C‐terminal catalytic (CAT) domain.
M. Mubinur Rahman, Ramita Sulu, Bukunmi Adediran, Hongmin Tu, Antti M. Salo, Sudarshan Murthy, Johanna Myllyharju, Rik K. Wierenga, M. Kristian Koski   +8 more
wiley   +1 more source

Mechanisms of Disulfide Bond Formation in Nascent Polypeptides Entering the Secretory Pathway

Cells, 2020
Disulfide bonds are an abundant feature of proteins across all domains of life that are important for structure, stability, and function. In eukaryotic cells, a major site of disulfide bond formation is the endoplasmic reticulum (ER).
Philip J. Robinson, Neil J. Bulleid
doaj   +1 more source

Engineering Pt Single‐Atom Doped SeS2/Ti3CNTx MXene with Molecularly Imprinted Polymer for Precision Pancreatic Cancer Diagnostics: DFT and Molecular Dynamics Perspectives

Small Methods, EarlyView.
A novel approach is developed to pancreatic cancer screening by targeting the cyclophili‐B (CypB)protein using a molecularly imprinted polymer with the electrode material containing Pt single‐atom‐doped/SeS2‐Ti3CNTx MXene. The quantification of CypB in pancreatic cancer tissues provide an insight into the association of CypB with pancreatic cancer ...
Sathish Panneer Selvam, Shanmugasundaram Kamalakannan, Agalya Mathivanan, Sungbo Cho   +3 more
wiley   +1 more source