Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Structure of Abnormal Heavy Chains in Human Heavy-chain-deposition Disease

1 Apr 1995

Abstract excerpt

The sequences of two immunoglobulin gamma 1 heavy chains involved in the formation of non-amyloid tissue deposits were determined in two patients (RIC and THR) affected with plasma cell monoclonal proliferation and heavy-chain-deposition disease. The proliferating plasma cells of patients RIC and THR synthesized truncated gamma 1 chains of 45 kDa and 24 kDa, respectively, carrying internal deletions of the first...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amyloidosis: Diagnosis, Treatment, Outcomes
Share to Glycosylation and Glycoproteins Research
Share to Monoclonal and Polyclonal Antibodies Research

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 7744049
DOI: 10.1111/j.1432-1033.1995.0054l.x

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 8 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 8 closest

Structure of Abnormal Heavy Chains in Human Heavy-chain-deposition DiseasePMID 7744049Read ↗

Primary structure of a variable region of the VκI subgroup (<i>ISE</i>) in light chain deposition diseaseSemantic proximity Read ↗

Structure of a monoclonal kappa chain of the V kappa IV subgroup in the kidney and plasma cells in light chain deposition disease.Semantic proximity Read ↗

Recombinant immunoglobulin variable domains generated from synthetic genes provide a system for in vitro characterization of light‐chain amyloid proteinsSemantic proximity Read ↗

A molecular basis for nonsecretory myelomaSemantic proximity Read ↗

Analysis of V(lambda)-J(lambda) expression in plasma cells from primary (AL) amyloidosis and normal bone marrow identifies 3r (lambdaIII) as a new amyloid-associated germline gene segment.Semantic proximity Read ↗

Role of complementarity-determining regions 1 and 3 in pathologic amyloid formation by human immunoglobulin κ1 light chainsSemantic proximity Read ↗

Structure of the VH-D-JH segments of human natural polyreactive IgM and IgG antibodies. Use of germline or somatically mutated forms of commonly expressed VH genes.Semantic proximity Read ↗

Role of Complementarity-Determining Regions 1 and 3 in Pathologic Amyloid Formation by Human Immunoglobulin κ1 Light ChainsSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.