Impact Factor
3.10
Journal Citation Impact
Estimated influence, citation density, publishing volume, and citation integrity from the analytics table.
Citation rate
2.95
127 total citations
h5-index
17
h5 depth signal
Cited share
76.7%
33 of 43
Total citations
127
Citation footprint
Metric signal
2.30
External metric anchor
Self-citation
1.6%
2 self-citations
Citations Trend
Monthly Publications Cadence
Citing Geographic Demographics
United States
185
Germany
81
Switzerland
52
France
38
Canada
36
Citing Fields of Research
Protein Structure & Folding
446
Mass Spectrometry
100
Cell Biology
36
Free Radicals & Antioxidants
18
Cellular Membrane Transporters & Receptors
18
Publishing Activity & Reach
Volume, recency, access pattern, and citing-community signals from the journal analytics record.
All-time article footprint
3,380
Articles tracked across the journal lifetime
Indexed publication set
43
33 cited publications
Last 12 months
22
2.4 publications/month
Open access share
77.3%
17 OA publications in the last year
Leading citing country
United States
185 citing publications
Leading citing field
Protein Structure & Folding
446 citing publications
Latest tracked publication
14 October 2026
10 recent records available
Coverage & Indexing History
v1n1,May 1990-
v1n1,May 1990-
Active Coverage
Research Focus & Classification
Indexed Subjects
Protein Structure & Folding
Broad Categories
Molecular Biology
Nuclear Medicine
Protein Structure & Folding
MeSH Descriptors
Biopolymers
Magnetic Resonance Spectroscopy
Latest Publications
Recent article records with DOI-first linking and condensed abstracts.
01
DOI 10.1007/s10858-026-00498-x
Open DOI
Accurate quantification of protein concentrations and state populations by 2D 1H-N Q-BEST NMR
We introduce 2D Q-BEST NMR as a quantitative approach for determining protein concentrations and relative state populations from a set of three 1H–15N correlation spectra. The BEST methodology ensures short overall experimental times and...
02
DOI 10.1007/s10858-026-00496-z
Open DOI
The perfect carbon TOCSY (iPE TOCSY) facilitates assignment of large biomolecules
Side chain assignments are essential for in-depth characterization of proteins. We present here two refined TOCSY experiments based on the use of a variant of “perfect echo” to partially suppress the negative effects arising from homonuc...
03
DOI 10.1007/s10858-026-00497-y
Open DOI
Assessment on site-specific thiol-based paramagnetic labeling strategies of metalloproteins for NMR and EPR applications
Paramagnetic NMR and EPR spectroscopy are important biophysical methods in structural biology, and site-specific protein labeling is generally required for their application in biological systems. Thiol chemistry is widely used for site-...
04
DOI 10.1007/s10858-026-00495-0
Open DOI
Co-sedimentation is the key to the structural investigation of wild-type FAT10
Under inflammatory conditions, the ubiquitin-like modifier FAT10 serves as a tag for protein degradation by the 26S proteasome. FAT10 is degraded along with its substrates and this process is independent of the segregase VCP/p97, which, ...
05
DOI 10.1007/s10858-026-00494-1
Open DOI
pyTRACTnmr: an open source python package for analyzing [15N, 1H]-TRACT experiments
The rotational correlation time () is a one of the fundamental parameters for characterizing biomacromolecules in solution. The [15N, 1H]-TRACT (TROSY for Rotational Correlation Times) NMR experiment is a widely utilized method for deter...
06
DOI 10.1007/s10858-025-00479-6
Open DOI
RelCalc: symbolic evaluation of BWR theory relaxation rates in python, applications to TROSY effects in AX spin systems
Relaxation phenomena greatly influence magnetic resonance experiments, from setting repetition rates and measurement times through to measuring internal motion of molecules. RelCalc provides a convenient and efficient means for symbolic ...
07
DOI 10.1007/s10858-026-00493-2
Open DOI
Solution NMR study of the titin I-band IgI domain I82 shows unusual conformational dynamics
β-sandwich domains of the intermediate immunoglobulin fold (IgI) are key building blocks of many large, multidomain proteins – such as titin. The uniformity of the basic fold of these domains does not seem to be an impediment to their ad...
08
DOI 10.1007/s10858-026-00492-3
Open DOI
Methyl-specific NMR of therapeutic antibodies: cost-effective isotopic labeling strategies in CHO cells for high-resolution structural characterization
Monoclonal antibodies (mAbs) are essential therapeutic agents whose efficacy depends critically on the integrity of their higher-order structure (HOS). Subtle perturbations in HOS, arising from post-translational modifications, chemical ...
09
DOI 10.1007/s10858-026-00491-4
Open DOI
AMIGO - Guided assignment of 13C-methyl labelled proteins
Over the last 20 years, the number of large proteins accessible to protein-NMR analysis has increased significantly due to the development of selective [ 1 H , 13 C]-methyl labelling techniques in combination with methyl-TROSY based NMR ...
10
DOI 10.1007/s10858-026-00490-5
Open DOI
Super-Resolution solid-state NMR Spectroscopy
Solid-state NMR spectroscopy is often limited by low spectral resolution, a problem typically addressed using fast magic-angle spinning (MAS) and ¹H detection, which require costly specialized hardware. Here, we demonstrate that the supe...
Bibliographical & Catalog Notes
Title from cover.
Imprint varies.
Also issued online.
Vol. 1, no. 1 (MAY 1991)19920831 Notice not published Printed on acid-free paper