Evidence map›Paper›PMID 23123451›Full record

ReviewPlant signaling & behavior2013

Cyclophilins: proteins in search of function.

Sumita Kumari, Suchismita Roy, Prabhjeet Singh, Sneh L Singla-Pareek, Ashwani Pareek

Open access · hybridAbstract readReview
In one paragraph

Review in Plant signaling & behavior, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing papers in PubMed
6.3field-weighted citation impact, top 3% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

60 citing papers in PubMed, 136 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 4 institutions in 1 country.

Sumita KumariSher-e-Kashmir University of Agricultural Sciences and Technology; Jammu, India.
Suchismita RoyStress Physiology and Molecular Biology Laboratory; School of Life Sciences; Jawaharlal Nehru University; New Delhi, India.
Prabhjeet SinghDepartment of Biotechnology; Guru Nanak Dev University; Amritsar, India.
Sneh L Singla-PareekPlant Molecular Biology; International Centre for Genetic Engineering and Biotechnology; New Delhi, India.
Ashwani PareekStress Physiology and Molecular Biology Laboratory; School of Life Sciences; Jawaharlal Nehru University; New Delhi, India.
Jawaharlal Nehru University · INGuru Nanak Dev University · INInternational Centre for Genetic Engineering and Biotechnology · INSher-e-Kashmir University of Agricultural Sciences and Technology of Kashmir · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cyclophilins constitute a subgroup of large family of proteins called immunophilins, which also include FKBPs and Parvulins. They are remarkably conserved in all genera, highlighting their pivotal role in important cellular processes. Most cyclophilins display PPIase enzymatic activity, multiplicity, diverse cellular locations and active role in protein folding which render them to be included in the class of diverse set of proteins called molecular chaperones. Due to their distinct PPIase function, besides protein disulfide isomerases and protein foldases, cyclophilins have been deemed necessary for in vivo chaperoning activity. Unlike other cellular chaperones, these proteins are specific in their respective targets. Not all cyclophilin proteins possess PPIase activity, indicating a loss of their PPIase activity during the course of evolution and gain of function independent of their PPIase activity. The PPIase function of cyclophilins is also compensated by their functional homologs, like FKBPs. Multiple cyclophilin members in plants like Arabidopsis and rice have been reported to be associated with diverse functions and regulatory pathways through their foldase, scaffolding, chaperoning or other unknown activities. Although many functions of plant cyclophilins were reported or suggested, the physiological relevance and molecular basis of stress-responsive expression of plant cyclophilins is still largely unknown. However, their wide distribution and ubiquitous nature signifies their fundamental importance in plant survival. Several of these members have also been directly linked to multiple stresses. This review attempts to deal with plant cyclophilins with respect to their role in stress response.

Indexed as

Adaptation, PhysiologicalStress, PhysiologicalCyclophilinsPeptidylprolyl IsomerasePlant ProteinsPlantsCyclophilinsPeptidylprolyl IsomerasePlant Proteinscyclophilinprotein foldingstress

Identifiers

PMID23123451
PMCPMC3745578
OpenAlexW2069004691

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.