Evidence map›Paper›PMID 38746339›Full record

ArticlebioRxiv : the preprint server for biology2024

Recombinant manufacturing of multispecies biolubricants.

Marshall J Colville, Ling-Ting Huang, Samuel Schmidt, Kevin Chen, Karan Vishwanath, Jin Su, Rebecca M Williams, Lawrence J Bonassar, Heidi L Reesink, Matthew J Paszek

Abstract readPreprint
PubMed Full text at PMC Publisher
In one paragraph

Article in bioRxiv : the preprint server for biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing 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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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.

Marshall J ColvilleRobert Frederick Smith School of Chemical and Biomolecular Engineering, Cornell University, Ithaca, NY, USA.ORCID 0000-0002-5397-8382
Ling-Ting HuangRobert Frederick Smith School of Chemical and Biomolecular Engineering, Cornell University, Ithaca, NY, USA.ORCID 0009-0004-4343-6039
Samuel SchmidtRobert Frederick Smith School of Chemical and Biomolecular Engineering, Cornell University, Ithaca, NY, USA.ORCID 0000-0001-9001-7970
Kevin ChenDepartment of Clinical Sciences, College of Veterinary Medicine, Cornell University, Ithaca, NY, USA.
Karan VishwanathDepartment of Materials Science and Engineering, Cornell University, Ithaca, NY USA.ORCID 0000-0003-2910-9176
Jin SuDepartment of Clinical Sciences, College of Veterinary Medicine, Cornell University, Ithaca, NY, USA.
Rebecca M WilliamsInstitute of Biotechnology, Cornell University, Ithaca, NY, USA.ORCID 0000-0002-1391-5846
Lawrence J BonassarNancy E. and Peter C. Meinig School of Biomedical Engineering, Cornell University, Ithaca, NY, USA.ORCID 0000-0003-1094-6433
Heidi L ReesinkDepartment of Clinical Sciences, College of Veterinary Medicine, Cornell University, Ithaca, NY, USA.ORCID 0000-0001-8534-8839
Matthew J PaszekRobert Frederick Smith School of Chemical and Biomolecular Engineering, Cornell University, Ithaca, NY, USA.ORCID 0000-0003-0064-9400

Funding

Mechanobiology of the Cellular GlycocalyxDP2GM119133 · NIGMS · CORNELL UNIVERSITY · PI PASZEK, MATTHEW J · 2015 to 2015
$2.3M
In Vivo Optical and MicroCT Imaging Instruments for the Cornell BRC Imaging FacilityS10OD025049 · OD · CORNELL UNIVERSITY · PI WILLIAMS, REBECCA M · 2018 to 2018
$750k
NIGMS NIH HHS DP2 GM119133NIH HHS S10 OD025049
6 · The paper itself

Abstract

Lubricin, a lubricating glycoprotein abundant in synovial fluid, forms a low-friction brush polymer interface in tissues exposed to sliding motion including joints, tendon sheaths, and the surface of the eye. Despite its therapeutic potential in diseases such as osteoarthritis and dry eye disease, there are few sources available. Through rational design, we developed a series of recombinant lubricin analogs that utilize the species-specific tissue-binding domains at the N- and C-termini to increase biocompatibility while replacing the central mucin domain with an engineered variant that retains the lubricating properties of native lubricin. In this study, we demonstrate the tissue binding capacity of our engineered lubricin product and its retention in the joint space of rats. Next, we present a new bioprocess chain that utilizes a human-derived cell line to produce

Indexed as

biomanufacturinglubricationlubricinmucin

Identifiers

PMID38746339
PMCPMC11092771

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.