Maximally deuterated samples

Show results for

Proteomics (23)
Unknown (1)

Organisms

Andropogon gerardi (23)
Bacteria (23)
Bartonella quintana JK 31 (23)
Canis lupus familiaris (23)
Cnidaria (23)
Ensifer adhaerens (23)
Halictus scabiosae (23)
Human alphaherpesvirus 1 strain 17 (23)
Human alphaherpesvirus 1 strain KOS (23)
Human herpesvirus 2 strain 186 (23)
Human immunodeficiency virus 1 (23)
Mesocricetus auratus (23)
Miscanthus x giganteus (23)
Mus musculus (23)
Panicum virgatum (23)
Platyhelminthes (23)
Pseudomonas aeruginosa PA103 (23)
Rabies virus Nishigahara RCEH (23)
Rattus norvegicus (23)
Rattus rattus (23)
Rhodococcus jostii RHA1 (23)
Rhodopseudomonas palustris (23)
Shigella (23)
Sorghastrum nutans (23)
Streptococcus dysgalactiae subsp. equisimilis SK1249 (23)
Streptococcus pneumoniae (23)
Streptomyces coelicolor A3(2) (23)
Synechocystis sp. PCC 6803 (23)
Tripsacum dactyloides (23)
Viruses (23)

Repository

pride (23)

Tissue

Permanent cell line cell (3)
Kidney (2)
Cell culture (1)
Cell suspension culture (1)
Epithelial cell (1)
Leaf (1)

Disease

COVID-19 (2)
Cervix carcinoma (1)
Immunoglobulin light chain amyloidosis (1)

Technology Type

Mass Spectrometry (23)
HDMSE (13)
MSE (4)
Shotgun proteomics (3)
Bottom-up proteomics (2)
Data-dependent acquisition (2)
Data-independent acquisition (2)
Gel-based experiment (1)
Glycoproteomics (1)

Publication Date

2025 (7)
2023 (6)
2026 (4)
2024 (3)
2022 (1)
2021 (1)
2020 (1)

Release Date

2022 (1)

Lab affiliation

Department of Chemistry & Chemical Biology, Northeastern University (4)
Department of Chemistry, King’s College London, SE1 1DB, London, UK Faculty of Biology, Medicine and Health, School of Biological Sciences, The University of Manchester, M13 9PT, Manchester, UK Manchester Institute of Biotechnology, The University of Manchester, M1 7DN, Manchester, UK (2)
Protein Biogenesis Lab, The Francis Crick Institute, 1 Midland Road, London, NW1 1AT (2)
Biochemistry Department, Kavli Institute for Nanoscience Discovery, University of Oxford, UK (1)
Center for RNA Research, Institute for Basic Science, Seoul 08826, Korea School of Biological Sciences, Seoul National University, Seoul 08826, Korea (1)
Children's Hospital of Phildelphia and University of Pennsylvania (1)
Department of Biochemistry and Biophysics, University of California San Franscisco, San Francisco, CA, USA; Howard Hughes Medical Institute (1)
Department of Chemistry & Chemical Biology, Northeastern University, Boston, MA, USA (1)
Department of Pharmacy, University of Copenhagen (1)
IPBS-Toulouse BP64182 205 route de Narbonne 31077 Toulouse Cedex04 (1)
Medicinal Chemistry, School of Pharmacy, University of Washington, USA (1)
Northeastern University (1)
Pennsylvania State University (1)
Protein Analysis Group, Department of Pharmacy, University of Copenhagen (1)
Protein Analysis Group, Department of Pharmacy, University of Copenhagen, Copehagen, Denmark (1)
The Pennsylvania State University, Department of Chemistry (1)
University of Dundee (1)
University of Victoria (1)

Previous page
1 / 3
You're on page 1
page 2
page 3
Next page

Sort by:

Relevance

Page size

Simple and Fast Maximally Deuterated Control (maxD) preparation for HDX MS Experiments

During the analysis steps of hydrogen deuterium exchange (HDX) mass spectrometry (MS) there is an unavoidable loss of deuterons, or back-exchange. Understanding back-exchange is necessary to correct for loss during analysis, to calculate the absolute amount of exchange, and to ensure that deuterium ...

ORGANISM(S): Bos taurus (Bovine) Homo sapiens (Human) Equus caballus (Horse)

2022-07-08 | PXD032924 | Pride

Simple and Fast Maximally Deuterated Control (maxD) Preparation for Hydrogen-Deuterium Exchange Mass Spectrometry Experiments.

Not available

S-EPMC9335555 | biostudies-literature

Maximally-multiplexed proteome quantification platform for isotopic metabolic and chemical labeling

Quantitative proteomic platforms based on precursor intensity in mass spectrometry (MS1-level) uniquely support in vivo metabolic labeling with superior quantification accuracy but suffers from limited multiplexity (≤3-plex) and frequent missing quantities. Herein, we present a maximally-multiplexed...

ORGANISM(S): Homo sapiens (Human)

2020-03-19 | PXD009952 | Pride

Diethylation Heat shock Silac-6plex Protein quantification Hela cell Quantification Silac De-6plex Heat shock response

A fold switch regulates conformation of an alphavirus virus RNA-dependent RNA polymerase

Alphaviruses are mosquito-vectored, positive-strand RNA viruses causing rheumatic and neurological diseases. Like all RNA viruses, they encode an RNA-dependent RNA polymerase (RdRp, nsP4). Purification of an nsP4 derivative capable of processive RNA synthesis from a heteropolymeric template has been...

ORGANISM(S): Alphavirus

2026-01-06 | PXD071261 | Pride

Fold switching Hdxms Alphavirus Rna-dependent rna polymerase Rna virus

Conformational differences in the light chain constant domain of immunoglobulin G and free light chain may influence proteolysis in AL amyloidosis

Immunoglobulin light chain amyloidosis (AL) is a life-threatening disease caused by the deposition of monoclonal light chain (LC) and its fragments containing variable (VL) and portions of constant (CL) domains. AL patients feature either monoclonal free LCs circulating as covalent and noncovalent h...

ORGANISM(S): Homo sapiens (Human)

2025-12-08 | PXD055570 | Pride

Igg amyloid light chain hdx-ms al amyloidosis hydrogen/deuterium exchange mass spectrometry

A conservative point mutation in a dynamic antigen-binding loop of human immunoglobulin λ6 light chain promotes pathologic amyloid formation

Immunoglobulin light chain (LC) amyloidosis (AL) is a life-threatening human disease wherein free monoclonal LCs deposit in vital organs. To determine what makes some LCs amyloidogenic, we explored patient-based amyloidogenic and non-amyloidogenic recombinant LCs from the λ6 subtype prevalent in AL....

ORGANISM(S): Homo sapiens (Human)

2021-11-25 | PXD026528 | Pride

Light chain amyloidosis protein conformation hydrogen-deuterium exchange mass spectrometry propagation of mutational effects cdr loops

Stabilization of diverse amyloidogenic antibody light chains by small molecules revealed by hydrogen-deuterium exchange mass spectrometry

Antibody light chains can aggregate as amyloid fibrils to cause systemic AL amyloidosis. Amyloid deposition requires unfolding of the light chain from its native state, but the mechanistic details of how this occurs are not fully understood. Inhibiting amyloid formation by stabilizing the precursor ...

ORGANISM(S): Homo sapiens (Human)

2026-07-27 | PXD068745 | Pride

HDX-MS Analysis of CeSpartin and CtSpartinL

HDX-MS analysis of SPG20, determining the seconday structure of CeSpartin and comparing WT CtSpartinL and A290P CtSpartinL.

ORGANISM(S): Homo sapiens (Human)

2023-12-27 | PXD043175 | Pride

Hdx-ms Spg20 Spartin

Role of Complementarity-Determining Regions 1 and 3 in Pathologic Amyloid Formation by Human Immunoglobulin κ1 Light Chains

Immunoglobulin light chain (LC) amyloidosis is a life-threatening disease whose understanding and treatment is complicated by vast numbers of patient-specific mutations. To address molecular origins of the disease, we explored 14 patient-derived and engineered proteins related to κ1-family germline ...

ORGANISM(S): Homo sapiens (Human)

2023-05-23 | PXD039682 | Pride

Light chain amyloidosis misfolded states protein stability protein dynamics hdx ms hydrogen deuterium exchange mass spectrometry

Epitope Mapping of Human Polyclonal Antibodies to the fHbp Antigen of a Neisseria Meningitidis Vaccine by Hydrogen-Deuterium Exchange Mass Spectrometry (HDX-MS) - part 2

Antigen-antibody interactions play a key role in the immune response post vaccination and the mechanism of action of antibody-based biopharmaceuticals. 4CMenB is a multicomponent vaccine against Neisseria meningitidis serogroup B in which factor H binding protein (fHbp) is one of the key antigens. I...

ORGANISM(S): Homo sapiens (Human)

2024-05-22 | PXD047712 | Pride

Pab Fhbp Hdx-ms

Previous page
1 / 3
You're on page 1
page 2
page 3
Next page

Sort by:

Relevance

Page size

24 Results

Show results for

Organisms

Repository

Tissue

Disease

Technology Type

Publication Date

Release Date

Lab affiliation

OmicsDI is part of the ELIXIR infrastructure

Tweets