Untitled

Mandal, Chitra; Sinha, S. K. P.

doi:10.1023/a:1007167611778

Cited by 15 publications

(8 citation statements)

References 22 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Different molecular variants of CRP are reported to be induced under different toxic aquatic conditions in fresh water fishes [6–10]. Recently, we have convincingly demonstrated that human CRP is glycosylated and distinct molecular variants are induced in several pathological conditions [11].…”

Section: Introductionmentioning

confidence: 89%

Protein A – a new ligand for human C‐reactive protein

Das

Mandal

2004

FEBS Letters

Self Cite

View full text Add to dashboard Cite

Section: Introductionmentioning

confidence: 89%

Protein A – a new ligand for human C‐reactive protein

Das

Mandal

2004

FEBS Letters

Self Cite

View full text Add to dashboard Cite

“…In cyprinids, the carp family fish rohu, Labeo rohita , CRP has been purified by their Ca 2+ -dependent binding to PCh (30, 68, 69). There are three types of glycosylated subunits in rohu CRP, and all three types of subunits move to identical position after desialylation and deglycosylation.…”

Section: Crp In Fishmentioning

confidence: 99%

Evolution of C-Reactive Protein

2019

View full text Add to dashboard Cite

C-reactive protein (CRP) is an evolutionarily conserved protein. From arthropods to humans, CRP has been found in every organism where the presence of CRP has been sought. Human CRP is a pentamer made up of five identical subunits which binds to phosphocholine (PCh) in a Ca 2+ -dependent manner. In various species, we define a protein as CRP if it has any two of the following three characteristics: First, it is a cyclic oligomer of almost identical subunits of molecular weight 20–30 kDa. Second, it binds to PCh in a Ca 2+ -dependent manner. Third, it exhibits immunological cross-reactivity with human CRP. In the arthropod horseshoe crab, CRP is a constitutively expressed protein, while in humans, CRP is an acute phase plasma protein and a component of the acute phase response. As the nature of CRP gene expression evolved from a constitutively expressed protein in arthropods to an acute phase protein in humans, the definition of CRP became distinctive. In humans, CRP can be distinguished from other homologous proteins such as serum amyloid P, but this is not the case for most other vertebrates and invertebrates. Literature indicates that the binding ability of CRP to PCh is less relevant than its binding to other ligands. Human CRP displays structure-based ligand-binding specificities, but it is not known if that is true for invertebrate CRP. During evolution, changes in the intrachain disulfide and interchain disulfide bonds and changes in the glycosylation status of CRP may be responsible for different structure-function relationships of CRP in various species. More studies of invertebrate CRP are needed to understand the reasons behind such evolution of CRP. Also, CRP evolved as a component of and along with the development of the immune system. It is important to understand the biology of ancient CRP molecules because the knowledge could be useful for immunodeficient individuals.

show abstract

“…The calculation of the overlap of reduced density matrices in Section 3 needs the use of the short-interval expansion, which is described in Appendix B. In Section 6 we present our conclusions and make some remarks on inhomogeneous quench [14].…”

Section: Collapse To Higher Spin Black Holesmentioning

confidence: 99%

“…Our calculations in this paper leads us to believe that this feature will continue in the presence of chemical potentials, in the sense that the additional dependence of the time scales 1/γ k on the µ n is fixed by the charge densities corresponding to the additional conserved charges. We hope to address this in [14].…”

Section: Introductionmentioning

confidence: 99%

Thermalization with chemical potentials, and higher spin black holes

Mandal

Sinha

Sorokhaibam

2015

J. High Energ. Phys.

View full text Add to dashboard Cite

We study the long time behaviour of local observables following a quantum quench in 1+1 dimensional conformal field theories possessing additional conserved charges besides the energy. We show that the expectation value of an arbitrary string of local observables supported on a finite interval exponentially approaches an equilibrium value. The equilibrium is characterized by a temperature and chemical potentials defined in terms of the quenched state. For an infinite number of commuting conserved charges, the equilibrium ensemble is a generalized Gibbs ensemble (GGE). We compute the thermalization rate in a systematic perturbation in the chemical potentials, using a new technique to sum over an infinite number of Feynman diagrams. The above technique also allows us to compute relaxation times for thermal Green's functions in the presence of an arbitrary number of chemical potentials. In the context of a higher spin (hs[λ]) holography, the partition function of the final equilibrium GGE is known to agree with that of a higher spin black hole. The thermalization rate from the CFT computed in our paper agrees with the quasinormal frequency of a scalar field in this black hole.

show abstract

Untitled

Cited by 15 publications

References 22 publications

Protein A – a new ligand for human C‐reactive protein

Protein A – a new ligand for human C‐reactive protein

Evolution of C-Reactive Protein

Thermalization with chemical potentials, and higher spin black holes

Contact Info

Product

Resources

About