Evidence map›Paper›PMID 7858132›Full record

ArticleBiophysical journal1994

Structural connectivity in actin: effect of C-terminal modifications on the properties of actin.

R H Crosbie, C Miller, P Cheung, T Goodnight, A Muhlrad, E Reisler

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
2.1field-weighted citation impact, top 12% 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

29 citing papers in PubMed, 94 citations in OpenAlex.

  1. Article
  2. Article
  3. Photoredox-Catalyzed DecarboxylativeACS chemical biology · 2021
    Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Near-atomic resolution for one state of F-actin.Structure (London, England : 1993) · 2015
    Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Redox signaling and cardiac sarcomeres.The Journal of biological chemistry · 2011
    Review
  15. A nucleotide state-sensing region on actin.The Journal of biological chemistry · 2010
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

6 authors at 1 institution in 1 country.

R H CrosbieDepartment of Chemistry and Biochemistry, University of California, Los Angeles 90024.
C Miller
P Cheung
T Goodnight
A Muhlrad
E Reisler
University of California, Los Angeles · US

Funding

UCLA NIGMS T32 Program AssessmentT32GM007185 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI TORRES, JORGE · 1985 to 2020
$21.7M
DYNAMIC EVENTS IN MYOSIN DURING CONTRACTION OF MUSCLER01AR022031 · NIAMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI REISLER, EMIL · 1986 to 2004
$2.5M
NIAMS NIH HHS AR22031NIAMS NIH HHS R01 AR022031NIGMS NIH HHS GM 07185
6 · The paper itself

Abstract

In this study, we use fluorescent probes and proteolytic digestions to demonstrate structural coupling between distant regions of actin. We show that modifications of Cys-374 in the C-terminus of actin slow the rate of nucleotide exchange in the nucleotide cleft. Conformational coupling between the C-terminus and the DNasal loop in subdomain II is observed in proteolytic digestion experiments in which a new C-terminal cleavage site is exposed upon DNasel binding. The functional consequences of C-terminal modification are evident from S-1 ATPase activity and the in vitro motility experiments with modified actins. Pyrene actin, labeled at Cys-374, activates S-1 ATPase activity only half as well as control actin. This reduction is attributed to a lower Vmax value because the affinity of pyrene actin to S-1 is not significantly altered. The in vitro sliding velocity of pyrene actin is also decreased. However, IAEDANS labeling of actin (also at Cys-374) enhances the Vmax of acto-S-1 ATPase activity and the in vitro sliding velocity by approximately 25%. These results are discussed in terms of conformational coupling between distant regions in actin and the functional implications of the interactions of actin-binding proteins with the C-terminus of actin.

Indexed as

ActinsAnimalsBinding SitesBiophysical PhenomenaBiophysicsFluorescent DyesIn Vitro TechniquesMolecular StructureMyosinsNaphthalenesulfonatesPeptide FragmentsPolymersProtein ConformationRabbitsStructure-Activity Relationship1,5-I-AEDANSActinsFluorescent DyesMyosinsNaphthalenesulfonatesPeptide FragmentsPolymers

Identifiers

PMID7858132
PMCPMC1225570
OpenAlexW2076731840

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.