On the public citation graph

P159 fromMycoplasma hyopneumoniaeBinds Porcine Cilia and Heparin and Is Cleaved in a Manner Akin to Ectodomain Shedding

0 signed · 89 inferred · view as graph

Inferred edges come from two machine sources: sweeps of open repository metadata (mostly SSRN and Zenodo), and a bulk OpenAlex citation snapshot. Every row below is labelled with the one it came from. Neither is a complete citation index — absence here is not evidence of absence.

Is this your work? Sign in with ORCID and put your name on the claims that are yours.
Claim with ORCID
Reference health. See whether every reference in this work resolves to a known work and none has been retracted — and get a dated CiteStamped badge you can embed.
See reference health

What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1002/jcb.20968openalex-snapshot
Hydrogen peroxide and endothelin‐1 are novel activators of betacellulin ectodomain shedding
inferredcites →https://doi.org/10.1002/pmic.200900440openalex-snapshot
Mass spectrometric characterization of the Campylobacter jejuni adherence factor CadF reveals post‐translational processing that removes immunogenicity while retaining fibronectin binding
inferredcites →https://doi.org/10.1002/prot.20735openalex-snapshot
Exploiting heterogeneous sequence properties improves prediction of protein disorder
inferredcites →https://doi.org/10.1007/bf00417864openalex-snapshot
Glycosaminoglycans in porcine lung: an ultrastructural study using Cupromeronic Blue
inferredcites →https://doi.org/10.1016/0165-022x(84)90040-xopenalex-snapshot
Electroblotting of multiple gels: a simple apparatus without buffer tank for rapid transfer of proteins from polycrylamide to nitrocellulose
inferredcites →https://doi.org/10.1016/j.jchromb.2006.02.022openalex-snapshot
Real and imaginary artefacts in proteome analysis via two-dimensional maps
inferredcites →https://doi.org/10.1016/j.vetmic.2004.03.002openalex-snapshot
Efficacy of vaccines against bacterial diseases in swine: what can we expect?
inferredcites →https://doi.org/10.1016/j.vetmic.2007.09.008openalex-snapshot
Control of Mycoplasma hyopneumoniae infections in pigs
inferredcites →https://doi.org/10.1016/s0264-410x(99)00395-3openalex-snapshot
Effect of vaccination on the potentiation of porcine reproductive and respiratory syndrome virus (PRRSV)-induced pneumonia by Mycoplasma hyopneumoniae
inferredcites →https://doi.org/10.1021/pr200758qopenalex-snapshot
Large-Scale Identification of Bacteria–Host Crosstalk by Affinity Chromatography: Capturing the Interactions of Streptococcus suis Proteins with Host Cells
inferredcites →https://doi.org/10.1021/pr201115vopenalex-snapshot
Mycoplasma hyopneumoniae Surface Proteins Mhp385 and Mhp384 Bind Host Cilia and Glycosaminoglycans and Are Endoproteolytically Processed by Proteases That Recognize Different Cleavage Motifs
inferredcites →https://doi.org/10.1021/pr3009012openalex-snapshot
SecretePipe: A Screening Pipeline for Secreted Proteins with Competence to Identify Potential Membrane-Bound Shed Markers
inferredcites →https://doi.org/10.1038/emboj.2011.189openalex-snapshot
FLRT2 and FLRT3 act as repulsive guidance cues for Unc5‐positive neurons
inferredcites →https://doi.org/10.1042/bj20051013openalex-snapshot
A role for exosomes in the constitutive and stimulus-induced ectodomain cleavage of L1 and CD44
inferredcites →https://doi.org/10.1074/jbc.m110.104463openalex-snapshot
A Processed Multidomain Mycoplasma hyopneumoniae Adhesin Binds Fibronectin, Plasminogen, and Swine Respiratory Cilia
inferredcites →https://doi.org/10.1074/jbc.m110.208140openalex-snapshot
Mhp107 Is a Member of the Multifunctional Adhesin Family of Mycoplasma hyopneumoniae
inferredcites →https://doi.org/10.1074/jbc.m111.226084openalex-snapshot
Sequence TTKF↓QE Defines the Site of Proteolytic Cleavage in Mhp683 Protein, a Novel Glycosaminoglycan and Cilium Adhesin of Mycoplasma hyopneumoniae
inferredcites →https://doi.org/10.1074/mcp.m500216-mcp200openalex-snapshot
Cell Surface Labeling and Mass Spectrometry Reveal Diversity of Cell Surface Markers and Signaling Molecules Expressed in Undifferentiated Mouse Embryonic Stem Cells
inferredcites →https://doi.org/10.1083/jcb.128.3.433openalex-snapshot
Transforming growth factor-alpha and beta-amyloid precursor protein share a secretory mechanism.
inferredcites →https://doi.org/10.1098/rsob.130017openalex-snapshot
MHJ_0125 is an M42 glutamyl aminopeptidase that moonlights as a multifunctional adhesin on the surface ofMycoplasma hyopneumoniae
inferredcites →https://doi.org/10.1099/00221287-143-2-663openalex-snapshot
Identification of novel species-specific antigens of Mycoplasma hyopneumoniae by preparative SDS-PAGE ELISA profiling
inferredcites →https://doi.org/10.1111/j.1365-2958.2006.05139.xopenalex-snapshot
P159 is a proteolytically processed, surface adhesin of Mycoplasma hyopneumoniae: defined domains of P159 bind heparin and promote adherence to eukaryote cells.
inferredcites →https://doi.org/10.1111/j.1365-2958.2008.06546.xopenalex-snapshot
Mhp493 (P216) is a proteolytically processed, cilium and heparin binding protein ofMycoplasma hyopneumoniae
inferredcites →https://doi.org/10.1111/j.1365-2958.2010.07345.xopenalex-snapshot
Repeat regions R1 and R2 in the P97 paralogue Mhp271 of Mycoplasma hyopneumoniae bind heparin, fibronectin and porcine cilia
inferredcites →https://doi.org/10.1111/j.1462-5822.2011.01702.xopenalex-snapshot
Mhp182 (P102) binds fibronectin and contributes to the recruitment of plasmin(ogen) to the Mycoplasma hyopneumoniae cell surface
inferredcites →https://doi.org/10.1126/science.252.5009.1162openalex-snapshot
Predicting Coiled Coils from Protein Sequences
inferredcites →https://doi.org/10.1128/iai.00154-10openalex-snapshot
Identification of Lipoprotein MslA as a Neoteric Virulence Factor ofMycoplasma gallisepticum
inferredcites →https://doi.org/10.1128/iai.62.5.1616-1622.1994openalex-snapshot
Microtiter plate adherence assay and receptor analogs for Mycoplasma hyopneumoniae
inferredcites →https://doi.org/10.1128/iai.72.5.2791-2802.2004openalex-snapshot
Proteolytic Processing of theMycoplasma hyopneumoniaeCilium Adhesin
inferredcites →https://doi.org/10.1128/iai.73.5.3137-3146.2005openalex-snapshot
Surface Analyses and Immune Reactivities of Major Cell Wall-Associated Proteins of Group A Streptococcus
inferredcites →https://doi.org/10.1128/iai.74.1.481-487.2006openalex-snapshot
Two Domains within theMycoplasma hyopneumoniaeCilium Adhesin Bind Heparin
inferredcites →https://doi.org/10.1128/jb.186.21.7123-7133.2004openalex-snapshot
The Genome Sequence ofMycoplasma hyopneumoniaeStrain 232, the Agent of Swine Mycoplasmosis
inferredcites →https://doi.org/10.1128/jcm.37.3.620-627.1999openalex-snapshot
Mycoplasma hyopneumoniaePotentiation of Porcine Reproductive and Respiratory Syndrome Virus-Induced Pneumonia
inferredcites →https://doi.org/10.1128/mbio.00282-11openalex-snapshot
Characterization of Cleavage Events in the Multifunctional Cilium Adhesin Mhp684 (P146) Reveals a Mechanism by Which Mycoplasma hyopneumoniae Regulates Surface Topography
inferredcites →https://doi.org/10.1161/01.atv.9.1.21openalex-snapshot
Molecular modeling of protein-glycosaminoglycan interactions.
inferredcites →https://doi.org/10.1186/1471-2180-7-63openalex-snapshot
Mapping phosphoproteins in Mycoplasma genitalium and Mycoplasma pneumoniae
inferredcites →https://doi.org/10.1385/1-59259-584-7:531openalex-snapshot
Protein Identification and Analysis Tools in the ExPASy Server
inferredcites →https://doi.org/10.2302/kjm.2012-0003-reopenalex-snapshot
A Brief History of Tumor Necrosis Factor α – converting Enzyme: An Overview of Ectodomain Shedding
inferredcites →https://doi.org/10.2460/ajvr.1977.38.08.1249openalex-snapshot
Scanning Electron Microscopy of Trachea and Bronchi from Gnotobiotic Pigs Inoculated with Mycoplasma hyopneumoniae

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

inferred← citeshttps://doi.org/10.2139/ssrn.4180334openalex-extracted
Identification of the Multiple Roles of Enolase as Plasminogen Receptor and Adhesin in Mycoplasma hyopneumoniae
inferred← citeshttps://doi.org/10.1002/pmic.201400276openalex-snapshot
Identification of immunoreactive proteins of Mycobacterium avium subsp. paratuberculosis
inferred← citeshttps://doi.org/10.1002/pmic.201400386openalex-snapshot
Non‐proteolytic functions of microbial proteases increase pathological complexity
inferred← citeshttps://doi.org/10.1002/pmic.201500319openalex-snapshot
The application of terminomics for the identification of protein start sites and proteoforms in bacteria
inferred← citeshttps://doi.org/10.1007/978-981-96-1885-9_16openalex-snapshot
Genetics of Bacterial Biofilm-Associated Infections in Livestock
inferred← citeshttps://doi.org/10.1007/s00253-022-11960-9openalex-snapshot
Unassembled cell wall proteins form aggregates in the extracellular space of Chlamydomonas reinhardtii strain UVM4
inferred← citeshttps://doi.org/10.1016/j.gene.2025.149709openalex-snapshot
Molecular mechanisms of gene expression regulation in Mycoplasma spp.: insights into virulence-related genes
inferred← citeshttps://doi.org/10.1016/j.heliyon.2023.e16141openalex-snapshot
Differential domains and endoproteolytic processing in dominant surface proteins of unknown function from Mycoplasma hyopneumoniae and Mycoplasma flocculare
inferred← citeshttps://doi.org/10.1016/j.jprot.2018.08.018openalex-snapshot
Differential secretome profiling of a swine tracheal cell line infected with mycoplasmas of the swine respiratory tract
inferred← citeshttps://doi.org/10.1016/j.micpath.2019.103717openalex-snapshot
Intracellular changes of a swine tracheal cell line infected with a Mycoplasma hyopneumoniae pathogenic strain
inferred← citeshttps://doi.org/10.1016/j.micpath.2022.105934openalex-snapshot
Identification of the multiple roles of enolase as an plasminogen receptor and adhesin in Mycoplasma hyopneumoniae
inferred← citeshttps://doi.org/10.1016/j.rvsc.2019.01.007openalex-snapshot
A concise review of vaccines against Mycoplasma hyopneumoniae
inferred← citeshttps://doi.org/10.1016/j.vetmic.2015.04.008openalex-snapshot
Exploitation of plasmin(ogen) by bacterial pathogens of veterinary significance
inferred← citeshttps://doi.org/10.1016/j.vetmic.2016.05.008openalex-snapshot
Mycoplasma hyopneumoniae and Mycoplasma flocculare differential domains from orthologous surface proteins induce distinct cellular immune responses in mice
inferred← citeshttps://doi.org/10.1016/j.vetmic.2016.07.023openalex-snapshot
Cross reactivity among the swine mycoplasmas as identified by protein microarray
inferred← citeshttps://doi.org/10.1021/acs.jproteome.6b00182openalex-snapshot
Comparisons of Protein and Peptide Complexity in Poneroid and Formicoid Ant Venoms
inferred← citeshttps://doi.org/10.1021/acs.jproteome.6b00948openalex-snapshot
Combined Peptidomic and Proteomic Analysis of Electrically Stimulated and Manually Dissected Venom from the South American Bullet Ant Paraponera clavata
inferred← citeshttps://doi.org/10.1021/acs.jproteome.7b00212openalex-snapshot
Proteomic Analysis of Extracellular HMGB1 Identifies Binding Partners and Exposes Its Potential Role in Airway Epithelial Cell Homeostasis
inferred← citeshttps://doi.org/10.1021/pr500087copenalex-snapshot
Cilium Adhesin P216 (MHJ_0493) Is a Target of Ectodomain Shedding and Aminopeptidase Activity on the Surface of Mycoplasma hyopneumoniae
inferred← citeshttps://doi.org/10.1038/s41598-017-10644-zopenalex-snapshot
Elongation factor Tu is a multifunctional and processed moonlighting protein
inferred← citeshttps://doi.org/10.1038/s41598-017-11296-9openalex-snapshot
N-terminomics identifies widespread endoproteolysis and novel methionine excision in a genome-reduced bacterial pathogen
inferred← citeshttps://doi.org/10.1038/s41598-018-28678-2openalex-snapshot
Extracellular DNA release from the genome-reduced pathogen Mycoplasma hyopneumoniae is essential for biofilm formation on abiotic surfaces
inferred← citeshttps://doi.org/10.1038/s41598-018-36054-3openalex-snapshot
Mycoplasma hyopneumoniae resides intracellularly within porcine epithelial cells
inferred← citeshttps://doi.org/10.1038/s41598-019-51116-wopenalex-snapshot
Mycoplasma hyopneumoniae surface-associated proteases cleave bradykinin, substance P, neurokinin A and neuropeptide Y
inferred← citeshttps://doi.org/10.1038/s41598-020-63136-yopenalex-snapshot
Cell surface processing of the P1 adhesin of Mycoplasma pneumoniae identifies novel domains that bind host molecules
inferred← citeshttps://doi.org/10.1038/s41598-021-86217-yopenalex-snapshot
Protein cleavage influences surface protein presentation in Mycoplasma pneumoniae
inferred← citeshttps://doi.org/10.1080/21505594.2020.1842659openalex-snapshot
Pathogenicity & virulence ofMycoplasma hyopneumoniae
inferred← citeshttps://doi.org/10.1098/rsob.140175openalex-snapshot
MHJ_0461 is a multifunctional leucine aminopeptidase on the surface of Mycoplasma hyopneumoniae
inferred← citeshttps://doi.org/10.1098/rsob.150210openalex-snapshot
Post-translational processing targets functionally diverse proteins in Mycoplasma hyopneumoniae
inferred← citeshttps://doi.org/10.1111/cmi.12377openalex-snapshot
Proteolytic processing of the cilium adhesin MHJ_0194 (P123J) inMycoplasma hyopneumoniaegenerates a functionally diverse array of cleavage fragments that bind multiple host molecules
inferred← citeshttps://doi.org/10.1111/tbed.13233openalex-snapshot
Mycoplasma hyopneumoniaevariability:Current trends and proposed terminology for genomic classification
inferred← citeshttps://doi.org/10.1128/aem.01439-19openalex-snapshot
Proteases as Secreted Exoproteins in Mycoplasmas from Ruminant Lungs and Their Impact on Surface-Exposed Proteins
inferred← citeshttps://doi.org/10.1186/s12917-020-02560-8openalex-snapshot
Immune responses induced by a combined vaccination with a recombinant chimera of Mycoplasma hyopneumoniae antigens and capsid virus-like particles of porcine circovirus type 2
inferred← citeshttps://doi.org/10.1186/s13567-026-01836-5openalex-snapshot
Rethinking Mycoplasma hyopneumoniae adhesion: a glycocalyx-mediated infectious niche model in porcine respiratory infection
inferred← citeshttps://doi.org/10.1371/journal.pone.0112596openalex-snapshot
Survey of Surface Proteins from the Pathogenic Mycoplasma hyopneumoniae Strain 7448 Using a Biotin Cell Surface Labeling Approach
inferred← citeshttps://doi.org/10.14800/ics.828openalex-snapshot
Mycoplasmal surface-associated aminopeptidases are multifunctional moonlighting proteins
inferred← citeshttps://doi.org/10.18174/420702openalex-snapshot
Systems analysis of Mycoplasma hyopneumoniae to improve vaccine production
inferred← citeshttps://doi.org/10.22541/au.165851107.74516161/v1openalex-snapshot
Immunogenic characteristics of p113/p126 family in Mycoplasma ovipneumoniae
inferred← citeshttps://doi.org/10.3389/fcimb.2018.00054openalex-snapshot
Extracellular Actin Is a Receptor for Mycoplasma hyopneumoniae
inferred← citeshttps://doi.org/10.3389/fcimb.2019.00209openalex-snapshot
Featured Species-Specific Loops Are Found in the Crystal Structure of Mhp Eno, a Cell Surface Adhesin From Mycoplasma hyopneumoniae
inferred← citeshttps://doi.org/10.3389/fimmu.2020.510943openalex-snapshot
Genomic Variability and Post-translational Protein Processing Enhance the Immune Evasion of Mycoplasma hyopneumoniae and Its Interaction With the Porcine Immune System
inferred← citeshttps://doi.org/10.3389/fmicb.2019.02351openalex-snapshot
The Diverse Functional Roles of Elongation Factor Tu (EF-Tu) in Microbial Pathogenesis
inferred← citeshttps://doi.org/10.3389/fmicb.2020.01679openalex-snapshot
Combined Transcriptome Sequencing of Mycoplasma hyopneumoniae and Infected Pig Lung Tissue Reveals Up-Regulation of Bacterial F1-Like ATPase and Down-Regulation of the P102 Cilium Adhesin in vivo
inferred← citeshttps://doi.org/10.3389/fmicb.2022.853440openalex-snapshot
The Mycoplasma spp. ‘Releasome’: A New Concept for a Long-Known Phenomenon
inferred← citeshttps://doi.org/10.3390/ijms23147899openalex-snapshot
Development of a Multi-Epitope Vaccine for Mycoplasma hyopneumoniae and Evaluation of Its Immune Responses in Mice and Piglets
inferred← citeshttps://doi.org/10.3390/microorganisms12071439openalex-snapshot
Research Progress on Immune Evasion of Mycoplasma hyopneumoniae
inferred← citeshttps://doi.org/10.3390/proteomes3040512openalex-snapshot
P40 and P90 from Mpn142 are Targets of Multiple Processing Events on the Surface of Mycoplasma pneumoniae
inferred← citeshttps://doi.org/10.3390/proteomes5020011openalex-snapshot
A Comprehensive Guide for Performing Sample Preparation and Top-Down Protein Analysis
inferred← citeshttps://doi.org/10.70675/175b6d22zc555z4155za9e1z77a323df2456openalex-snapshot
Metabolic Investigation of the Mycoplasmas from the Swine Respiratory Tract
inferred← citeshttps://doi.org/10.70675/b19bf813z271cz4793z95ffz75a631f85d34openalex-snapshot
Le sécrétome des bactéries du genre Mycoplasma ˸ focus sur les protéases sécrétées et les vésicules extracellulaires produites chez les mycoplasmes des ruminants.
Editorial review for independent work. ICSAC — the Institute for Complexity Science and Advanced Computing — runs a structured editorial panel for researchers publishing outside journals, and publishes on CiteStamp rails. Submission is free and goes through ORCID: icsacinstitute.org/submit.