Results 91 to 100 of about 72,835,347 (270)

High-Mobility-Group protein I can modulate binding of transcription factors to the U5 region of the human immunodeficiency virus Type 1 proviral promoter [PDF]

open access: yes, 2000
HMG I/Y appears to be a multifunctional protein that relies on in its ability to interact with DNA in a structure-specific manner and with DNA, binding transcriptional activators via distinct protein-protein interaction surfaces.
Henderson, A.   +4 more
core  

The hepatitis B virus X protein activates nuclear factor of activated T cells (NF-AT) by a cyclosporin A-sensitive pathway. [PDF]

open access: yes, 1998
The X gene product of the human hepatitis B virus (HBx) is a transcriptional activator of various viral and cellular genes. We recently have determined that the production of tumor necrosis factor-alpha (TNF-alpha) by HBV-infected hepatocytes is ...
Armesilla, Angel   +11 more
core   +1 more source

The Expression of Tristetraprolin and Its Relationship with Urinary Proteins in Patients with Diabetic Nephropathy. [PDF]

open access: yesPLoS ONE, 2015
Tristetraprolin (TTP), also known as zinc finger protein 36, is an RNA binding protein that has a significant role in regulating the expression of mRNAs containing AU-rich elements.
Fengxun Liu   +7 more
doaj   +1 more source

Data from The IL-18 Antagonist IL-18–Binding Protein Is Produced in the Human Ovarian Cancer Microenvironment

open access: yes, 2023
<div>Abstract<p><b>Purpose:</b> Interleukin (IL)-18 is an immune-enhancing cytokine, which induces IFN-γ production, T-helper 1 responses, and antitumor effects. In turn, IFN-γ stimulates IL-18–binding protein production, which blocks IL-18 activity.
Silvano Ferrini   +10 more
openaire   +1 more source

Functional comparison of EncB and EncC cargo proteins in iron storage within the Myxococcus xanthus encapsulin

open access: yesFEBS Letters, EarlyView.
Encapsulins are protein nanocompartments that play an important role in iron storage. In the Myxococcus xanthus encapsulin system, two cargo proteins called EncB and EncC contribute to iron mineralization. Here, we show that EncB and EncC generate iron‐containing minerals with distinct chemical compositions, suggesting that the composition of stored ...
Harry B. McDowell   +2 more
wiley   +1 more source

Expression of interleukin-18 receptor in fibroblast-like synoviocytes [PDF]

open access: yes, 2001
An excess of the proinflammatory substance IL-18 is present in joints of patients with rheumatoid arthritis (RA), and expression of IL-18 receptor (IL-18R) regulates IL-18 bioactivity in various cell types.
Hoelzer, Dieter (Prof. Dr.)   +15 more
core   +1 more source

Structural and biochemical analysis of a B12 superbinder

open access: yesFEBS Letters, EarlyView.
BtuG proteins are vitamin B12 scavengers in Bacteroides thetaiotaomicron, a dominant human gut bacterium. We present crystal structures of three BtuG homologs bound to cobalamin and its precursor cobinamide, revealing picomolar binding affinities, among the highest known for any natural protein.
Jose M. Martinez Felices   +3 more
wiley   +1 more source

A Computational Model of the LGI1 Protein Suggests a Common Binding Site for ADAM Proteins [PDF]

open access: yes, 2011
Mutations of human leucine-rich glioma inactivated (LGI1) gene encoding the epitempin protein cause autosomal dominant temporal lateral epilepsy (ADTLE), a rare familial partial epileptic syndrome.
Leonardi, Emanuela   +24 more
core   +1 more source

Structures of mycobacterial 3‐methylcrotonyl‐CoA carboxylase reveal carrier‐domain translocation between catalytic sites

open access: yesFEBS Letters, EarlyView.
Mycobacterial 3‐methylcrotonyl‐CoA carboxylase uses a mobile biotin‐carrying domain to shuttle a carboxyl group between two catalytic sites, enabling carboxylation of 3‐methylcrotonyl‐CoA during leucine breakdown. Cryo‐electron microscopy captures the carrier at both sites and reveals an inward loop movement that may prevent futile rebinding to the ...
Ajit Yadav   +2 more
wiley   +1 more source

Functional activities of C-reactive protein on neutrophils [PDF]

open access: yes
C-reactive protein (CRP) is a member of the pentraxin family which opsonises S. pneumoniae through its binding to phosphorylcholine. In addition, CRP binds to Fcγ receptors: FcγRI with high affinity and, probably, FcγRIIA with lower affinity.
Rodriguez, Jairo Antonio
core   +1 more source

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