Evidence map›Paper›PMID 38358255›Full record

ArticleProtein science : a publication of the Protein Society2024

A PDZ scaffolding/CaM-mediated pathway in Cryptochrome signaling.

Massimo Bellanda, Milena Damulewicz, Barbara Zambelli, Elisa Costanzi, Francesco Gregoris, Stefano Mammi, Silvio C E Tosatto, Rodolfo Costa, Giovanni Minervini, Gabriella M Mazzotta

Open access · greenAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
1.1field-weighted citation impact, top 28% 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

2 citing papers in PubMed, 4 citations in OpenAlex.

  1. Article
  2. A PDZ scaffolding/CaM-mediated pathway in Cryptochrome signaling.Protein science : a publication of the Protein Society · 2024
    Article
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

10 authors at 3 institutions in 3 countries.

Massimo BellandaDepartment of Chemical Sciences, University of Padova, Padova, Italy.
Milena DamulewiczDepartment of Cell Biology and Imaging, Jagiellonian University, Kraków, Poland.
Barbara ZambelliDepartment of Pharmacy and Biotechnology, University of Bologna, Bologna, Italy.
Elisa CostanziDepartment of Chemical Sciences, University of Padova, Padova, Italy.
Francesco GregorisDepartment of Biomedical Sciences, University of Padova, Padova, Italy.
Stefano MammiDepartment of Chemical Sciences, University of Padova, Padova, Italy.
Silvio C E TosattoDepartment of Biomedical Sciences, University of Padova, Padova, Italy.ORCID 0000-0003-4525-7793
Rodolfo CostaDepartment of Biology, University of Padova, Padova, Italy.ORCID 0000-0002-2489-9116
Giovanni MinerviniDepartment of Biomedical Sciences, University of Padova, Padova, Italy.
Gabriella M MazzottaDepartment of Biology, University of Padova, Padova, Italy.ORCID 0000-0001-5461-6837
University of Padua · ITJagiellonian University · PLUniversity of Bologna · IT

Funding

Fondazione Cassa di Risparmio di Padova e Rovigo (Progetti di Eccellenza 2011-2012)INsecTIME FP7 People: Marie-Curie Actions Initial Training Network PITN-GA-2012-316790Ministero dell'Istruzione, dell'Universitá e della Ricerca (MIUR)National Research Council of ItalyUniversità degli Studi di Padova (P-DiSC) 01BIRD2018Università degli Studi di Padova (P-DiSC) BIRD213814/21
6 · The paper itself

Abstract

Cryptochromes are cardinal constituents of the circadian clock, which orchestrates daily physiological rhythms in living organisms. A growing body of evidence points to their participation in pathways that have not traditionally been associated with circadian clock regulation, implying that cryptochromes may be subject to modulation by multiple signaling mechanisms. In this study, we demonstrate that human CRY2 (hCRY2) forms a complex with the large, modular scaffolding protein known as Multi-PDZ Domain Protein 1 (MUPP1). This interaction is facilitated by the calcium-binding protein Calmodulin (CaM) in a calcium-dependent manner. Our findings suggest a novel cooperative mechanism for the regulation of mammalian cryptochromes, mediated by calcium ions (Ca

Indexed as

CalciumCryptochromesAnimalsCircadian RhythmDrosophilaHumansMammalsSignal TransductionCalciumCryptochromesCalmodulincircadian rhythmscryptochrome signalinghCRY2MUPP1

Identifiers

PMID38358255
PMCPMC10868427
OpenAlexW4391872555

What Socratic holds

Textmetadata
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 Socratic graph.