Evidence map›Paper›PMID 12671004›Full record

ArticleGenome research2003

Ran's C-terminal, basic patch, and nucleotide exchange mechanisms in light of a canonical structure for Rab, Rho, Ras, and Ran GTPases.

Andrew F Neuwald, Natarajan Kannan, Aleksandar Poleksic, Naoya Hata, Jun S Liu

Open access · bronzeAbstract read
In one paragraph

Article in Genome research, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
–field-weighted citation impact
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

30 citing papers in PubMed, 46 citations in OpenAlex.

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  12. A Bayesian sampler for optimization of protein domain hierarchies.Journal of computational biology : a journal of computational molecular cell biology · 2014
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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 2 institutions in 1 country.

Andrew F NeuwaldCold Spring Harbor Laboratory, Cold Spring Harbor, New York 11724, USA. neuwald@cshl.org
Natarajan Kannan
Aleksandar Poleksic
Naoya Hata
Jun S Liu
Cold Spring Harbor Laboratory · USHarvard University · US

Funding

Computational Haplotype Analysis for SNPsR01HG002518 · NHGRI · HARVARD UNIVERSITY · PI LIU, JUN S · 2002 to 2010
$2.5M
ADVANCED SEQUENCE BASED PREDICTION OF PROTEIN FUNCTIONR01LM006747 · NLM · J. CRAIG VENTER INSTITUTE, INC. · PI NEUWALD, ANDREW F · 1998 to 2005
$2.3M
NHGRI NIH HHS HG02518-01NHGRI NIH HHS R01 HG002518NLM NIH HHS LM06747NLM NIH HHS R01 LM006747
6 · The paper itself

Abstract

Proteins comprising the core of the eukaryotic cellular machinery are often highly conserved, presumably due to selective constraints maintaining important structural features. We have developed statistical procedures to decompose these constraints into distinct categories and to pinpoint critical structural features within each category. When applied to P-loop GTPases, this revealed within Rab, Rho, Ras, and Ran a canonical network of molecular interactions centered on bound nucleotide. This network presumably performs a crucial structural and/or mechanistic role considering that it has persisted for more than a billion years after the divergence of these families. We call these 'FY-pivot' GTPases after their most distinguishing feature, a phenylalanine or tyrosine that functions as a pivot within this network. Specific families deviate somewhat from canonical features in interesting ways, presumably reflecting their functional specialization during evolution. We illustrate this here for Ran GTPases, within which two highly conserved histidines, His30 and His139, strikingly diverge from their canonical counterparts. These, along with other residues specifically conserved in Ran, such as Tyr98, Lys99, and Phe138, appear to work in conjunction with FY-pivot canonical residues to facilitate alternative conformations in which these histidines are strategically positioned to couple Ran's basic patch and C-terminal switch to nucleotide exchange and effector binding. Other core components of the cellular machinery are likewise amenable to this approach, which we term Contrast Hierarchical Alignment and Interaction Network (CHAIN) analysis.

Indexed as

Amino Acid SequenceAnimalsbeta KaryopherinsComputational BiologyConserved SequenceEvolution, MolecularGuanine Nucleotide Exchange FactorsGuanosine TriphosphateHumansMolecular Sequence DataMonomeric GTP-Binding ProteinsPeptide FragmentsPhylogenyProtein Structure, Quaternaryrab GTP-Binding Proteinsran GTP-Binding Proteinbeta KaryopherinsGuanine Nucleotide Exchange FactorsGuanosine TriphosphateMonomeric GTP-Binding ProteinsPeptide Fragmentsrab GTP-Binding Proteinsran GTP-Binding Proteinras Proteinsrho GTP-Binding Proteins

Identifiers

PMID12671004
PMCPMC430177
OpenAlexW2163507574

What OpenQuestion 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 OpenQuestion graph.