Jordi Bella

ORCID: 0000-0003-0443-4562
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About
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Research Areas
  • Collagen: Extraction and Characterization
  • Cell Adhesion Molecules Research
  • Viral Infections and Immunology Research
  • Proteoglycans and glycosaminoglycans research
  • Chemical Synthesis and Analysis
  • Glycosylation and Glycoproteins Research
  • Respiratory viral infections research
  • Bone and Dental Protein Studies
  • Monoclonal and Polyclonal Antibodies Research
  • Biopolymer Synthesis and Applications
  • RNA and protein synthesis mechanisms
  • Bacteriophages and microbial interactions
  • Protein Hydrolysis and Bioactive Peptides
  • Protein Structure and Dynamics
  • Supramolecular Self-Assembly in Materials
  • DNA and Nucleic Acid Chemistry
  • Enzyme Structure and Function
  • Animal Disease Management and Epidemiology
  • Cellular transport and secretion
  • Synthesis and properties of polymers
  • Bone health and treatments
  • Connective tissue disorders research
  • Bone Tissue Engineering Materials
  • Protease and Inhibitor Mechanisms
  • Cellular Mechanics and Interactions

University of Manchester
2009-2025

Henry Royce Institute
2021-2025

Manchester Academic Health Science Centre
2017-2023

Wellcome Centre for Cell-Matrix Research
2000-2010

Rutgers, The State University of New Jersey
1994-2006

University of Alberta
2004

Purdue University West Lafayette
1996-2001

State University of New York
2000

Bayer (United States)
1998

Institute of Advanced Chemistry of Catalonia
1996

The structure of a protein triple helix has been determined at 1.9 angstrom resolution by x-ray crystallographic studies collagen-like peptide containing single substitution the consensus sequence. This adopts triple-helical that confirms basic features from fiber diffraction on collagen: supercoiling polyproline II helices and interchain hydrogen bonding follows model Rich Crick. In addition, provides new information concerning nature this fold. Each is surrounded cylinder hydration, with...

10.1126/science.7695699 article EN Science 1994-10-07

Norwalk virus, a noncultivatable human calicivirus, is the major cause of epidemic gastroenteritis in humans. The first x-ray structure calicivirus capsid, which consists 180 copies single protein, has been determined by phase extension from low-resolution electron microscopy structure. capsid protein protruding (P) domain connected flexible hinge to shell (S) that classical eight-stranded β-sandwich motif. P unlike any other viral with subdomain exhibiting fold similar second eukaryotic...

10.1126/science.286.5438.287 article EN Science 1999-10-08

10.1016/s0969-2126(01)00224-6 article EN publisher-specific-oa Structure 1995-09-01

The structure of the extracellular, three-domain poliovirus receptor (CD155) complexed with (serotype 1) has been determined to 22-Å resolution by means cryo-electron microscopy and three-dimensional image-reconstruction techniques. Density corresponding was isolated in a difference electron density map fitted known structures, homologous those three individual CD155 Ig-like domains. fit confirmed location carbohydrate moieties glycoprotein, conserved properties elbow angles structures cell...

10.1073/pnas.97.1.79 article EN Proceedings of the National Academy of Sciences 2000-01-04

The normal function of human intercellular adhesion molecule-1 (ICAM-1) is to provide between endothelial cells and leukocytes after injury or stress. ICAM-1 binds leukocyte function-associated antigen (LFA-1) macrophage-1 (Mac-1). However, also used as a receptor by the major group rhinoviruses catalyst for subsequent viral uncoating during cell entry. three-dimensional atomic structure two amino-terminal domains (D1 D2) has been determined 2.2-Å resolution fitted into cryoelectron...

10.1073/pnas.95.8.4140 article EN Proceedings of the National Academy of Sciences 1998-04-14

Decorin is a ubiquitous extracellular matrix proteoglycan with variety of important biological functions that are mediated by its interactions proteins, cytokines, and cell surface receptors. the prototype family small leucine-rich repeat proteoglycans proteins (SLRPs), characterized protein core composed repeats (LRRs), flanked two cysteine-rich regions. We report here crystal structure dimeric decorin, best member SLRP family. Each monomer adopts curved solenoid fold characteristic LRR...

10.1073/pnas.0402976101 article EN Proceedings of the National Academy of Sciences 2004-10-22

Decorin is the archetypal small leucine rich repeat proteoglycan of vertebrate extracellular matrix (ECM). With its glycosaminoglycuronan chain, it responsible for stabilizing inter-fibrillar organization. Type I collagen predominant member fibrillar family, fulfilling both organizational and structural roles in animal ECMs. In this study, interactions between decoron (the decorin core protein) binding sites d e1 bands type fibril were investigated through molecular modeling their respective...

10.1371/journal.pone.0007028 article EN cc-by PLoS ONE 2009-09-14

The structural basis of the interaction integrin heterodimers with their physiological ligands is poorly understood. We have used solution x-ray scattering to visualize head region alpha 5 beta 1 in an inactive (Ca2+-occupied) state, and complex a fragment fibronectin containing RGD synergy recognition sequences. Shape reconstructions data been interpreted terms appropriate molecular models. suggest that undergoes no gross conformational changes upon ligand binding but do lend support...

10.1074/jbc.m304627200 article EN cc-by Journal of Biological Chemistry 2003-10-01

Collagen is the most ubiquitous biomacromolecule found in animal kingdom and commonly used as a biomaterial regenerative medicine therapies biomedical research. The collagens these applications are typically derived from mammalian sources which poses sociological issues due to widespread religious constraints, rising ethical concern over rights continuous risk of zoonotic disease transmission. These have led increasing research into alternative collagen sources, marine collagens, particular...

10.3390/md21020059 article EN cc-by Marine Drugs 2023-01-19

ABSTRACT Coxsackievirus A21 (CAV21), like human rhinoviruses (HRVs), is a causative agent of the common cold. It uses same cellular receptor, intercellular adhesion molecule 1 (ICAM-1), as does major group HRVs; unlike HRVs, however, it stable at acid pH. The cryoelectron microscopy (cryoEM) image reconstruction CAV21 consistent with highly homologous crystal structure poliovirus 1; other enteroviruses and has canyon-like depression around each 12 fivefold vertices. A cryoEM complexed ICAM-1...

10.1128/jvi.75.5.2444-2451.2001 article EN Journal of Virology 2001-03-01

Significance We present here an entirely novel concept in the field of cell–cell adhesion, whereby flexibility extracellular domains cadherin molecules determines characteristics and behavior intercellular junctions. The structure ectodomain desmosomal desmoglein 2 shows it is flexible its calcium-bound form. This ectodomains may be key facilitating a unique property desmosomes: ability to switch from strong calcium-independent hyperadhesion adult tissues weaker calcium-dependent adhesion wounds.

10.1073/pnas.1420508112 article EN public-domain Proceedings of the National Academy of Sciences 2015-04-08
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